|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
265-1596 |
2.03e-118 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 414.80 E-value: 2.03e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 265 WLSWgllYAGFVFIMALSLALViksvQFFILTSFMVVFS------LFLL-YGLSMITLAFLMSALVRKSVLTGL--SVFL 335
Cdd:TIGR01257 697 WCTW---FLDSFSIMSMSIFLL----TIFIMHGRILHYSdpfilfLFLLaFSTATIMQCFLLSTFFSKASLAAAcsGVIY 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 336 LTIFWGSLGFTSLYRYLPAPVEWTLSLFSPFAFTLGMAQLLRVDYD---LN-SNAPPDPASGSNL-IIATNFMLVFDAFL 410
Cdd:TIGR01257 770 FTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQglgLQwSNIGNSPLEGDEFsFLLSMKMMLLDAAL 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 411 YLALMMYFEKVLPNEYGHQHSPLFFLKSSFWL-----QTRKPAHV-----ILEDGIDPVPSSG--DSFepVSPEFHG-KE 477
Cdd:TIGR01257 850 YGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLggegcSTREERALektepLTEEMEDPEHPEGinDSF--FERELPGlVP 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISK--EYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSemADLENI 555
Cdd:TIGR01257 928 GVCVKNLVKifEPSGRP----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAV 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQ 635
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 636 IFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKWGVGYHLSLQL 715
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVR 1161
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 716 K------------------------------EVCVPENI--------TSLVKQHIPAAKLSAEGEGKLLYTLPLETTYR- 756
Cdd:TIGR01257 1162 KmkniqsqrggcegtcsctskgfstrcparvDEITPEQVldgdvnelMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQr 1241
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 757 -----FPELCQSLDScpgLGIENYGVSMTTLNEVFLKLEGKASIDEPevdIVGEGQTER---------SGDTERLMEMEQ 822
Cdd:TIGR01257 1242 ayaslFRELEETLAD---LGLSSFGISDTPLEEIFLKVTEDADSGSL---FAGGAQQKRenanlrhpcSGPTEKAGQTPQ 1315
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 823 TLSSLRETEKTD-------------GMALWRQQTCAIAKVRLLKLKHERKTLLSVLLILVVGICP--FLFENISTKIRQS 887
Cdd:TIGR01257 1316 ASHTCSPGQPAAhpegqpppepedpGVPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPatFVFLALMLSIIIP 1395
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 888 SY----TWELSP----HDYFLAPGQQP------------------------QGMLTQLLIIN----KTEASIDDFIHSVE 931
Cdd:TIGR01257 1396 PFgeypALTLHPwmygQQYTFFSMDEPnsehlevladvllnkpgfgnrclkEEWLPEYPCGNstpwKTPSVSPNITHLFQ 1475
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 932 RQ---------------------------------------------------NI---------ALEVDASGTRDGTDDP 951
Cdd:TIGR01257 1476 KQkwtaahpspscrcstrekltmlpecpegagglpppqrtqrsteilqdltdrNIsdflvktypALIRSSLKSKFWVNEQ 1555
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 952 SYNG---------------ALI-----------VSGN-----------------EKNHSFSFACNTKRLNCFPVLMDILS 988
Cdd:TIGR01257 1556 RYGGisiggklpaipitgeALVgflsdlgqmmnVSGGpvtreaskempdflkhlETEDNIKVWFNNKGWHALVSFLNVAH 1635
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 989 NGLLGMVKPSARiqtDRSTYLMDETIHPL----EDLWK-----------TAFWLILT-SACPPYIAMSSVTDYKNRAWFQ 1052
Cdd:TIGR01257 1636 NAILRASLPKDR---DPEEYGITVISQPLnltkEQLSEitvlttsvdavVAICVIFAmSFVPASFVLYLIQERVNKAKHL 1712
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1053 LRVSGLFPSAYWVGQAMVDIPLYC-----FVFLFMSLMDYLFRFPDTMFSIISHVIQIPCSV---GYAISLIFLTYVISF 1124
Cdd:TIGR01257 1713 QFISGVSPTTYWLTNFLWDIMNYAvsaglVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVipmMYPASFLFDVPSTAY 1792
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1125 ISRK------GKKNSGIwslsFYIITVFSVAVILLAFDVDGTQYYIIFlipPSTLVGCLILSLHL------FIGQIFEE- 1191
Cdd:TIGR01257 1793 VALScanlfiGINSSAI----TFVLELFENNRTLLRFNAMLRKLLIVF---PHFCLGRGLIDLALsqavtdVYAQFGEEh 1865
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1192 ---------------GQVIEPFLVFLIPFLHVFIFIFTlrclEWkfgKKTMRKDPIFrisPRNNDVYQnpeepedededv 1256
Cdd:TIGR01257 1866 sanpfqwdligknlvAMAVEGVVYFLLTLLIQHHFFLS----RW---IAEPAKEPIF---DEDDDVAE------------ 1923
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1257 qmERMRtanalVSTSFDEKPVIIASCLRKEYAGkqkhclskkKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG 1336
Cdd:TIGR01257 1924 --ERQR-----IISGGNKTDILRLNELTKVYSG---------TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1337 DTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKEHLEIFAAVRGLrkshAAVAITRLAD----ALKLQDQ 1408
Cdd:TIGR01257 1988 DTTVTSGDATVAGksilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGV----PAEEIEKVANwsiqSLGLSLY 2063
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1409 LKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNtDRGALLTTHYMAEAEALCDRVAI 1488
Cdd:TIGR01257 2064 ADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAI 2142
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1489 LVSGRLRCIGSIQHLKSKFGKDYLLEMKVKT-----LEQVEPLNTEILRLFPQASRQERYSSLMAYKLPVEAvqpLSQAF 1563
Cdd:TIGR01257 2143 MVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSpkddlLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS---LARIF 2219
|
1610 1620 1630
....*....|....*....|....*....|...
gi 254911033 1564 FKLEKVKQTFDLEEYSLSQSTLEQVFLELSKEQ 1596
Cdd:TIGR01257 2220 QLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
479-702 |
2.70e-84 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 275.15 E-value: 2.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLseMADLENILRI 558
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGSSLFLK 702
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1283-1504 |
4.93e-84 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 274.38 E-value: 4.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYagkqkhclsKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGF 1358
Cdd:cd03263 6 LTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1359 LGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILL 1438
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1439 LDEPSTGLDPEGQQQIWQAIRAIIKNtdRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK 1504
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1295-1507 |
8.89e-72 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 239.97 E-value: 8.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTP-GFLGYCPQENALW 1369
Cdd:COG1131 6 LTKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvARDPAEVrRRIGYVPQEPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:COG1131 86 PDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1450 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKF 1507
Cdd:COG1131 166 ARRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
479-697 |
7.01e-70 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 234.57 E-value: 7.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmaDLENILRI 558
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1295-1510 |
4.65e-59 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 203.55 E-value: 4.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-SREGDTPGF---LGYCPQENALW 1369
Cdd:COG4555 7 LSKKyGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGeDVRKEPREArrqIGVLPDERGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:COG4555 87 DRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1450 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKD 1510
Cdd:COG4555 167 ARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
479-697 |
3.15e-57 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 198.54 E-value: 3.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAD--LENIl 556
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReaRRQI- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 riaGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:COG4555 77 ---GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1295-1494 |
9.26e-56 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 191.46 E-value: 9.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALW 1369
Cdd:cd03230 6 LSKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikKEPEEVKRRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNLTVKEHLEifaavrglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:cd03230 86 ENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254911033 1450 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03230 130 SRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1295-1596 |
4.01e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 194.56 E-value: 4.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKKKA-KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREG-DTPGFLGYCPQENALWPNL 1372
Cdd:COG4152 7 LTKRFGdKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpEDRRRIGYLPEERGLYPKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:COG4152 87 KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1453 QIWQAIRAIIkntDRGA--LLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKdyllemkvKTLEQVEPLNTEI 1530
Cdd:COG4152 167 LLKDVIRELA---AKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR--------NTLRLEADGDAGW 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1531 LRLFPQASRQERYSSLMAYKLPVEAV-QPLsqaffkLEKVKQTFDLEEYSLSQSTLEQVFLELSKEQ 1596
Cdd:COG4152 236 LRALPGVTVVEEDGDGAELKLEDGADaQEL------LRALLARGPVREFEEVRPSLNEIFIEVVGEK 296
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
479-692 |
9.18e-55 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 188.76 E-value: 9.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmaDLENILRI 558
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRlfakirgippqdvekevqrvllelemkniqnilaqnLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKtILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1303-1592 |
1.60e-54 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 192.99 E-value: 1.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDT-PGFLGYCPQENALWPNLTVKEHL 1378
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvVREPRKvRRSIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 EIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 1458
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1459 RAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDYlLEMKVKTLEQVEPLNTEILRLFPQAS 1538
Cdd:TIGR01188 168 RA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMLIAELGETG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1539 RQERYSSLMAYKLPVEAVQPLSQAFFKLEKVKQT-FDLEEYSLSQSTLEQVFLEL 1592
Cdd:TIGR01188 246 LGLLAVTVDSDRIKILVPDGDETVPEIVEAAIRNgIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1303-1504 |
3.88e-53 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 186.04 E-value: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKEHL 1378
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 EIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 1458
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1459 RAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK 1504
Cdd:cd03265 175 EKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
479-693 |
6.88e-48 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 170.45 E-value: 6.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGqITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynNNLSEMADLENILRI 558
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI--DGQDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRLK 693
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
479-692 |
1.32e-47 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 169.98 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAD------- 551
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 552 LENIlriaGVCPQanvQF---DFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGI 628
Cdd:cd03255 81 RRHI----GFVFQ---SFnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 629 AILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADiLADRKVFISNGRL 692
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1299-1498 |
1.63e-47 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 169.38 E-value: 1.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1299 KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-FLGYCPQENALWPNLTVKEH 1377
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnRIGYLPEERGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQA 1457
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 1458 IRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:cd03269 171 IRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1277-1595 |
2.40e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 172.96 E-value: 2.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1277 VIIASCLRKEY---------AGKQKHCLS-KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL 1346
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1347 lkgsregdtpgFLGYCP----------------QENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLK 1410
Cdd:COG4586 81 -----------VLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1411 SPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRGA--LLTTHYMAEAEALCDRVAI 1488
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRERGTtiLLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1489 LVSGRLRCIGSIQHLKSKFGKDyllemKVKTLEQVEPLNTEILRLFPQASRQERYSslmaYKLPVEAVQPLSQAffkLEK 1568
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPY-----KTIVLELAEPVPPLELPRGGEVIEREGNR----VRLEVDPRESLAEV---LAR 295
|
330 340
....*....|....*....|....*..
gi 254911033 1569 VKQTFDLEEYSLSQSTLEQVFLELSKE 1595
Cdd:COG4586 296 LLARYPVRDLTIEEPPIEEVIRRIYKE 322
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
479-697 |
1.22e-46 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 167.51 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmADLENILRI 558
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQ-ANVQFDFLTVRENLrLFA-KIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLtfgiAILG---- 632
Cdd:COG1122 77 VGLVFQnPDDQLFAPTVEEDV-AFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV----AIAGvlam 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 633 DSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
480-691 |
1.47e-46 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.49 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 480 RIRNISKEYKGKPNKieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRIA 559
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL-SLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 GVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03225 78 GLVFQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGR 691
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
493-791 |
7.37e-45 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 164.87 E-value: 7.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 493 NKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLenILRIAGVCPQANVQFDFL 572
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK--VRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 573 TVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRH 652
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 653 RVWNLL-KERRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKWG-----VGYHLSLQLKeVCVPENITS 726
Cdd:TIGR01188 162 AIWDYIrALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGkdtleSRPRDIQSLK-VEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 727 LVKQHIPAAKLSAEGEGKLLYTLPLETTyrFPELCQSLDScPGLGIENYGVSMTTLNEVFLKLEG 791
Cdd:TIGR01188 241 LGETGLGLLAVTVDSDRIKILVPDGDET--VPEIVEAAIR-NGIRIRSISTERPSLDDVFLKLTG 302
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1294-1495 |
3.85e-44 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 159.69 E-value: 3.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1294 CLSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS---REGDTPGFLGYCPQENALW 1369
Cdd:cd03268 5 DLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqKNIEALRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNLTVKEHLEIFAAVRGLRKShaavAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:cd03268 85 PNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1450 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLR 1495
Cdd:cd03268 161 GIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
479-692 |
1.22e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.97 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAD------- 551
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 552 LENIlriaGVCPQanvQF---DFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGI 628
Cdd:COG1136 85 RRHI----GFVFQ---FFnllPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 629 AILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADIlADRKVFISNGRL 692
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
479-692 |
1.85e-42 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 154.68 E-value: 1.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynnNLSEMADLENILRI 558
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPpqdvEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 639 LDEPTAGLDPFSRHRVWNLL-KERRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
479-702 |
6.20e-42 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 153.68 E-value: 6.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynNNLSEMADLENILRI 558
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--AGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGSSLFLK 702
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1301-1495 |
7.88e-42 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 153.12 E-value: 7.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGeILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP----GFLGYCPQENALWPNLTVKE 1376
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqklrRRIGYLPQEFGVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEgqQQIwq 1456
Cdd:cd03264 92 FLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE--ERI-- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 1457 AIRAIIKN--TDRGALLTTHYMAEAEALCDRVAILVSGRLR 1495
Cdd:cd03264 168 RFRNLLSElgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1297-1498 |
1.45e-41 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 152.52 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1297 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP----GFLGYCPQENALWPNL 1372
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaearRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1453 QIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:cd03266 174 ALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1301-1593 |
3.50e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 154.58 E-value: 3.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKE 1376
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:PRK13537 100 NLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1457 AIRAIIKntdRGA--LLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL-KSKFGKDyLLEMKVKTLeqvEPLNTEilrL 1533
Cdd:PRK13537 180 RLRSLLA---RGKtiLLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDP---VALRDE---L 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1534 FPQASRQE-RYSSLMAYklpVEAVQPLSQAffklekVKQTFDLeEYSLSQSTLEQVFLELS 1593
Cdd:PRK13537 250 APLAERTEiSGETLFCY---VRDPEPLHAR------LKGRAGL-RYLHRPANLEDVFLRLT 300
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1297-1494 |
1.41e-40 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 150.18 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1297 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGD-TPGFL-------GycpQENAL 1368
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrRKKFLrrigvvfG---QKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1369 WPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 1448
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1449 EGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
479-691 |
1.79e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 148.78 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmaDLENILRI 558
Cdd:COG4133 3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD--AREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEkeVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRAD-RVVLFSTQfmDEADILADRKVFISNGR 691
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARgGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
479-693 |
5.15e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 148.00 E-value: 5.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNnnlsemADLENILRI 558
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG------EPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISN--GRLK 693
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1305-1474 |
9.69e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 146.86 E-value: 9.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKEHLEI 1380
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirDAREDYRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1381 FAAVRGLRKSHAAvaITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 1460
Cdd:COG4133 99 WAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|....*.
gi 254911033 1461 iikNTDRG--ALLTTH 1474
Cdd:COG4133 177 ---HLARGgaVLLTTH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
479-692 |
2.99e-39 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 146.17 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL-----SVPTKGSVTIYNNNLSEMADLE 553
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NILR--IAGVCPQANVqFDfLTVRENLRLFAKIRGIPPQDVEKEVQRVLLEL-----EMKNIQNILAqnLSGGQKRKLTF 626
Cdd:cd03260 77 LELRrrVGMVFQKPNP-FP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKaalwdEVKDRLHALG--LSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 627 GIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
479-696 |
3.60e-39 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 145.59 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTI--YNNNLSEMADLENIl 556
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdgFDVVKEPAEARRRL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 riaGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:cd03266 81 ---GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
479-693 |
7.83e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.00 E-value: 7.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADlenilRI 558
Cdd:COG1116 8 LELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----DR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 aGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLtfGIA--ILGDSQI 636
Cdd:COG1116 83 -GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV--AIAraLANDPEV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISN--GRLK 693
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1303-1493 |
3.64e-38 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 142.96 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF------LGYCPQENALWPNLTVKE 1376
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraragIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEIFAAVRGLRKSHAavaitRLADAL----KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:cd03224 95 NLLLGAYARRRAKRKA-----RLERVYelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 1453 QIWQAIRAIIKnTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:cd03224 170 EIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
479-691 |
8.03e-38 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 139.83 E-value: 8.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRI 558
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFlTVRENLrlfakirgippqdvekevqrvllelemkniqnilaqnLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADiLADRKVFISNGR 691
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
479-730 |
1.99e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 142.18 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRI 558
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQA--NvQFDFLTVR-------ENLrlfakirGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKltfgIA 629
Cdd:TIGR04520 79 VGMVFQNpdN-QFVGATVEddvafglENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR----VA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 630 ILG----DSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQFMDEAdILADRKVFISNGRLKCAGS--SLFL 701
Cdd:TIGR04520 147 IAGvlamRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMNKGKIVAEGTprEIFS 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 254911033 702 K----KKWGVG----YHLSLQLKE--VCVPENITS---LVKQ 730
Cdd:TIGR04520 226 QvellKEIGLDvpfiTELAKALKKrgIPLPPDILTeeeLVDE 267
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1301-1493 |
4.77e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 143.43 E-value: 4.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKE 1376
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
170 180 190
....*....|....*....|....*....|....*....
gi 254911033 1457 AIRAIIKntdRGA--LLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:PRK13536 214 RLRSLLA---RGKtiLLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
480-691 |
9.00e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.61 E-value: 9.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 480 RIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRIa 559
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 GVCPQanvqfdfltvrenlrlfakirgippqdvekevqrvllelemkniqnilaqnLSGGQKRKLTFGIAILGDSQIFLL 639
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 640 DEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGR 691
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1295-1498 |
2.08e-36 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 137.65 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP---GFLGYCPQENALWP 1370
Cdd:cd03259 6 LSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPperRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 NLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 1450
Cdd:cd03259 86 HLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254911033 1451 QQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:cd03259 166 REELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
479-692 |
5.11e-36 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 137.25 E-value: 5.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM--ADLENIL 556
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQANVQFDFLTVRENLRLFAKIRGippQDVEKEV-QRVLLELEM---KNIQNILAQNLSGGQKRKLTFGIAILG 632
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHT---RLSEEEIrEIVLEKLEAvglRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 633 DSQIFLLDEPTAGLDPFSRHRVWNL---LKERRADRVVLFSTQfMDEADILADRKVFISNGRL 692
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLirsLKKELGLTSIMVTHD-LDTAFAIADRIAVLYDGKI 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
498-644 |
7.76e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 133.54 E-value: 7.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRIAGVCPQANVQFDFLTVREN 577
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 578 LRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQN----LSGGQKRKLTFGIAILGDSQIFLLDEPTA 644
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
479-697 |
9.47e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 137.10 E-value: 9.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEnILRI 558
Cdd:COG1120 2 LEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRL-----FAKIRGIPPQDVEKeVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGD 633
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALgryphLGLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 634 SQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
479-691 |
1.37e-35 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 135.64 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgkpnKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdLENILRi 558
Cdd:cd03224 1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP-PHERAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGV--CPQANVQFDFLTVRENLRLFAKIRgiPPQDVEKEVQRVlLEL--EMKNIQNILAQNLSGGQKRKLTFGIAILGDS 634
Cdd:cd03224 75 AGIgyVPEGRRIFPELTVEENLLLGAYAR--RRAKRKARLERV-YELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 635 QIFLLDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGR 691
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVtILLVEQNARFALEIADRAYVLERGR 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
452-711 |
1.56e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 144.14 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 452 LEDGIDPVPSSGDSFEPVSPEFHGkeSIRIRNISKEYKGKPNkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL 531
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGGP--SLELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 532 SVPTKGSVTIYNNNLSEMaDLENILRIAGVCPQANVQFDfLTVRENLRLfAKirgipPQDVEKEVQRVLlelEMKNIQNI 611
Cdd:COG4987 385 LDPQSGSITLGGVDLRDL-DEDDLRRRIAVVPQRPHLFD-TTLRENLRL-AR-----PDATDEELWAAL---ERVGLGDW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 612 LAQ--------------NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEA 677
Cdd:COG4987 454 LAAlpdgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL 533
|
250 260 270
....*....|....*....|....*....|....
gi 254911033 678 DiLADRKVFISNGRLKCAGSSLFLKKKWGVGYHL 711
Cdd:COG4987 534 E-RMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
479-692 |
1.77e-35 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 135.40 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM--ADLENIL 556
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQanvQFDFL---TVRENLRLFAKIRGIPPQDVEKEVQRvLLEL-EMKNIQNILAQNLSGGQKRKLTFGIAILG 632
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEERVLE-LLELvGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 633 DSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1305-1493 |
2.43e-35 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 135.11 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----------SREGdtpgfLGYCPQENALWPNLT 1373
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpphriARLG-----IGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 VKEHLEIFAAVRGLRKSHAAvaitRLADAL----KLQDQLKSPVKTLSEGVKRklcfVLSI----LGNPSILLLDEPSTG 1445
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRA----DLERVYelfpRLKERRRQRAGTLSGGEQQ----MLAIgralMSRPKLLLLDEPSLG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1446 LDPEGQQQIWQAIRAIIkntDRGA--LLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:COG0410 167 LAPLIVEEIFEIIRRLN---REGVtiLLVEQNARFALEIADRAYVLERGR 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
478-748 |
3.29e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 138.04 E-value: 3.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENIlR 557
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA-R 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IaGVCPQ-ANVQFDFlTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:PRK13536 116 I-GVVPQfDNLDLEF-TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKERRA-DRVVLFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKwgvgyHLSLQL 715
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE-----HIGCQV 268
|
250 260 270
....*....|....*....|....*....|....*
gi 254911033 716 KEVC--VPENITSLVKQHipAAKLSAEGEGKLLYT 748
Cdd:PRK13536 269 IEIYggDPHELSSLVKPY--ARRIEVSGETLFCYA 301
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
479-696 |
3.42e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 133.95 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmADLENIlri 558
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-AARNRI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 aGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03269 73 -GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
479-692 |
5.36e-35 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 133.41 E-value: 5.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM-ADLENIlr 557
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVpPERRNI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 iaGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:cd03259 75 --GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1305-1444 |
1.13e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 130.08 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREGDTPGFLGYCPQENALWPNLTVKEHLE 1379
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdDERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 1380 IFAAVRGLRKSHAAVAITRLADALKLQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPST 1444
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
479-697 |
1.16e-34 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 133.57 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM--ADLENIL 556
Cdd:COG1127 6 IEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLseKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQANVQFDFLTVREN----LRLFakiRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLtfGIA--I 630
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENvafpLREH---TDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRV--ALAraL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR-----VVlfsTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsvVV---THDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1295-1499 |
3.96e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 131.51 E-value: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----------SREGdtpgfLGYC 1362
Cdd:cd03218 6 LSKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrARLG-----IGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1363 PQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEP 1442
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1443 STGLDPEGQQQIwQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:cd03218 161 FAGVDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
479-723 |
5.64e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 132.58 E-value: 5.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEY-KGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTI--YNNNLSEMADLENI 555
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRIAGVcpqanVqFDF-------LTVRE-------NLrlfakirGIPPQDVEKEVQRVLLELEMKniQNILAQN---LSG 618
Cdd:TIGR04521 81 RKKVGL-----V-FQFpehqlfeETVYKdiafgpkNL-------GLSEEEAEERVKEALELVGLD--EEYLERSpfeLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 619 GQKRKltfgIAILG----DSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:TIGR04521 146 GQMRR----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 254911033 693 KCAGSS--LFLKKKWGVGYHLSL--------QLKEVCVPEN 723
Cdd:TIGR04521 222 VLDGTPreVFSDVDELEKIGLDVpeitelarKLKEKGLPVP 262
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
479-691 |
9.77e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 133.01 E-value: 9.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENiLRI 558
Cdd:PRK13537 8 IDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 aGVCPQ-ANVQFDFlTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:PRK13537 83 -GVVPQfDNLDPDF-TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKERRA-DRVVLFSTQFMDEADILADRKVFISNGR 691
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
479-692 |
1.35e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.17 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNkieaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRI 558
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDfLTVRENLRLFAKIRGIPP--QDVEKEVQRVLLELEMKNIQnilAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRERKFdrERALELLERLGLPPDILDKP---VERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
479-692 |
1.37e-33 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 130.14 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEY-----------------KGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTI 541
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 542 YNNNLSEMADlENILRIAGVCPQAN-VQFDfLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQ 620
Cdd:cd03267 81 AGLVPWKRRK-KFLRRIGVVFGQKTqLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 621 KRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1303-1494 |
2.01e-33 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 129.86 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP-------GfLGYCPQENALWPNLTVK 1375
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiarlG-IGRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHLEI---------FAAVRGLRKSHAAVA-ITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTG 1445
Cdd:cd03219 94 ENVMVaaqartgsgLLLARARREEREARErAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 1446 LDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03219 174 LNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
479-697 |
2.15e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADlenilRI 558
Cdd:COG1121 7 IELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR-----RI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVcPQ-ANVQFDF-LTVRE--------NLRLFakiRGIPPQDVEKeVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGI 628
Cdd:COG1121 78 GYV-PQrAEVDWDFpITVRDvvlmgrygRRGLF---RRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 629 AILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFIsNGRLKCAGS 697
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
457-697 |
2.36e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 137.58 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 457 DPVPSSGDSFEPVSPEFhgkeSIRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTK 536
Cdd:COG4988 319 EPAAPAGTAPLPAAGPP----SIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 537 GSVTIYNNNLSEMaDLENILRIAGVCPQANVQFDfLTVRENLRLFAkiRGIPPQDVEKEVQRVLLELEMKNIQNIL---- 612
Cdd:COG4988 392 GSILINGVDLSDL-DPASWRRQIAWVPQNPYLFA-GTIRENLRLGR--PDASDEELEAALEAAGLDEFVAALPDGLdtpl 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 613 ---AQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQfmDEADI-LADRKVFIS 688
Cdd:COG4988 468 gegGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLD 545
|
....*....
gi 254911033 689 NGRLKCAGS 697
Cdd:COG4988 546 DGRIVEQGT 554
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
479-692 |
2.54e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.02 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADlENI--L 556
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR-REIpyL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 R--IaGVCPQanvqfDF-----LTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLtfGI- 628
Cdd:COG2884 78 RrrI-GVVFQ-----DFrllpdRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV--AIa 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 629 -AILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFST---QFMDEadiLADRKVFISNGRL 692
Cdd:COG2884 150 rALVNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIAThdlELVDR---MPKRVLELEDGRL 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1303-1494 |
3.04e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 129.77 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----------SREGdtpgfLGYCPQENALWPN 1371
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriARLG-----IARTFQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKEHLEI----------FAAVRGLRKSHAAVAITR-----LADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSI 1436
Cdd:COG0411 94 LTVLENVLVaaharlgrglLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1437 LLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
478-697 |
4.52e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 130.61 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLsemaDLENILR 557
Cdd:COG4152 1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IA------GVCPQanvqfdfLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAIL 631
Cdd:COG4152 73 IGylpeerGLYPK-------MKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 632 GDSQIFLLDEPTAGLDPFSRHRVWNLLKERRA-DRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
479-691 |
1.11e-32 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 125.38 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILR- 557
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 -IAGVCPQANVqFDFLTVRENLRLfakirgippqdvekevqrvllelemkniqnilaqNLSGGQKRKLTFGIAILGDSQI 636
Cdd:cd03229 77 rIGMVFQDFAL-FPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGR 691
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1297-1493 |
1.84e-32 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 126.04 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1297 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP-----GFLGYCPQEnalwP- 1370
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelrRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 ----NLTVKEhlEI-FAAV-RGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCfVLSIL-GNPSILLLDEPS 1443
Cdd:cd03225 86 dqffGPTVEE--EVaFGLEnLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1444 TGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:cd03225 163 AGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
478-692 |
2.52e-32 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 124.97 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKPNKIEA--LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL--SVPTKGSVTIYNNNLsemaDLE 553
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL----DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NILRIAGVCPQANVQFDFLTVRENLRLFAKIRGIppqdvekevqrvllelemkniqnilaqnlSGGQKRKLTFGIAILGD 633
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 634 SQIFLLDEPTAGLDPFSRHRVWNLLKeRRAD--RVVLFST-QFMDEADILADRKVFISNGRL 692
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1305-1514 |
3.54e-32 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 125.91 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQ--ENALWpNLTVKEh 1377
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKdiTKKNLRELrrkVGLVFQnpDDQLF-APTVEE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 lEI-FAAV-RGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCF--VLSIlgNPSILLLDEPSTGLDPEGQQQ 1453
Cdd:COG1122 96 -DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLVLDEPTAGLDPRGRRE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1454 IWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLkskFGKDYLLE 1514
Cdd:COG1122 173 LLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV---FSDYELLE 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
471-711 |
7.33e-32 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 134.58 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 471 PEFHGkeSIRIRNISKEYKgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMa 550
Cdd:COG2274 468 PRLKG--DIELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 551 DLENILRIAGVCPQANVQFdFLTVRENLRLFAKirGIPPQDVEK-----EVQRVLLELEMKnIQNILA---QNLSGGQKR 622
Cdd:COG2274 543 DPASLRRQIGVVLQDVFLF-SGTIRENITLGDP--DATDEEIIEaarlaGLHDFIEALPMG-YDTVVGeggSNLSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 623 KLtfGIA--ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQfmDEADI-LADRKVFISNGRLKCAGSSL 699
Cdd:COG2274 619 RL--AIAraLLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH--RLSTIrLADRIIVLDKGRIVEDGTHE 694
|
250
....*....|..
gi 254911033 700 FLKKKWGVGYHL 711
Cdd:COG2274 695 ELLARKGLYAEL 706
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1276-1499 |
8.07e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.14 E-value: 8.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1276 PVIIASCLRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------ 1349
Cdd:COG1137 2 MTLEAENLVKSYGKRT-----------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1350 -----SREGdtpgfLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKL 1424
Cdd:COG1137 71 pmhkrARLG-----IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1425 CFVLSILGNPSILLLDEPSTGLDP----EgqqqiwqaIRAIIKN-TDRGA--LLTTHYMAEAEALCDRVAILVSGRLRCI 1497
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPiavaD--------IQKIIRHlKERGIgvLITDHNVRETLGICDRAYIISEGKVLAE 217
|
..
gi 254911033 1498 GS 1499
Cdd:COG1137 218 GT 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
478-692 |
1.04e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.27 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEnilR 557
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 -IAGVcPQ--ANvqFDFLTVRENLrLFA-KIRGIPPQDVEKEVQRVlleLEMKNIQNIL---AQNLSGGQKRKLTFGIAI 630
Cdd:COG3839 76 nIAMV-FQsyAL--YPHMTVYENI-AFPlKLRKVPKAEIDRRVREA---AELLGLEDLLdrkPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1305-1499 |
1.24e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 125.16 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-----FLGYCPQENALWPNLTVKE--- 1376
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelarRIAYVPQEPPAPFGLTVRElva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 -----HLEIFAAVRglRKSHAAV--AITRLaDALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:COG1120 98 lgrypHLGLFGRPS--AEDREAVeeALERT-GLEHLADR---PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1450 GQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
479-697 |
3.08e-31 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 123.32 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdlENILRI 558
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP--PHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCP--QANVQFDFLTVRENLRLFAKIRGIPP----------QDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTF 626
Cdd:cd03219 75 LGIGRtfQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 627 GIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLfstqfMDEADI-----LADRKVFISNGRLKCAGS 697
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVL-----LVEHDMdvvmsLADRVTVLDQGRVIAEGT 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
480-696 |
3.11e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 121.39 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 480 RIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMadlenilria 559
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 gvcpqanvqfdfltvreNLRLFAKIRGIPPQdVEKEVQrvLLELEMKNIqnilaQNLSGGQKRKLTFGIAILGDSQIFLL 639
Cdd:cd03214 67 -----------------SPKELARKIAYVPQ-ALELLG--LAHLADRPF-----NELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 640 DEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
479-692 |
4.05e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 122.36 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNnlsEMADLENILRI 558
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
494-698 |
4.97e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 122.78 E-value: 4.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 494 KIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdLENILRiAGV--CPQA-NVqFD 570
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP-PHRIAR-LGIgyVPEGrRI-FP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 571 FLTVRENLRLFAKIRGiPPQDVEKEVQRVlLEL--EMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDP 648
Cdd:COG0410 92 SLTVEENLLLGAYARR-DRAEVRADLERV-YELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 649 FSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGRLKCAGSS 698
Cdd:COG0410 170 LIVEEIFEIIRRLNREGVtILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
479-729 |
5.14e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 125.58 E-value: 5.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYK------G---------KPNK--IEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVti 541
Cdd:COG4586 2 IEVENLSKTYRvyekepGlkgalkglfRREYreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 542 ynnnlsemadlenilRIAGVCPQ----ANVQ-------------FDfLTVRENLRLFAKIRGIPPQDVEKEVQrvllEL- 603
Cdd:COG4586 80 ---------------RVLGYVPFkrrkEFARrigvvfgqrsqlwWD-LPAIDSFRLLKAIYRIPDAEYKKRLD----ELv 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 604 EMKNIQNILAQ---NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQFMDeaD 678
Cdd:COG4586 140 ELLDLGELLDTpvrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD--D 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 679 I--LADRKVFISNGRLKCAGSSLFLKKKWGVGYHLSLQLKEVCVPENITSLVK 729
Cdd:COG4586 218 IeaLCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE 270
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
480-693 |
6.80e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 121.21 E-value: 6.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 480 RIRNISKEYKGKPnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENIlria 559
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 GVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKevqrVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLK 693
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1295-1493 |
6.85e-31 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 119.66 E-value: 6.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF-----LGYCPQenal 1368
Cdd:cd00267 5 LSFRyGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelrrrIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1369 wpnltvkehleifaavrglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 1448
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254911033 1449 EGQQQIWQAIRAIIKNtDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:cd00267 114 ASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1301-1502 |
6.94e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 6.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWPN--LTVKE-- 1376
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVDWDfpITVRDvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 ------HLEIFaavRGLRKSHAAvAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 1450
Cdd:COG1121 99 lmgrygRRGLF---RRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1451 QQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVaILVSGRLRCIGSIQH 1502
Cdd:COG1121 175 EEALYELLRE-LRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
479-697 |
9.41e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 128.87 E-value: 9.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPT---KGSVTIYNNNLSEMADLENI 555
Cdd:COG1123 5 LEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQ 635
Cdd:COG1123 83 RRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 636 IFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1291-1500 |
1.29e-30 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 121.35 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1291 QKHCLSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR--EGDTPGfLGYCPQENA 1367
Cdd:TIGR03740 2 ETKNLSKRfGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwtRKDLHK-IGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1368 LWPNLTVKEHLEIFAAVRGLRKSHaavaITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 1447
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGLPDSR----IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1448 PEGQQQIWQAIRAIiknTDRG--ALLTTHYMAEAEALCDRVAILVSGRLRCIGSI 1500
Cdd:TIGR03740 157 PIGIQELRELIRSF---PEQGitVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1275-1503 |
1.43e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 128.10 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1275 KPVIIASCLRKEYAGKQKHclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG---DTKVTAGQVLLKGSR 1351
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP---------AVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1352 EGDTPGFL-----GYCPQE--NALWPnLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKL 1424
Cdd:COG1123 73 LLELSEALrgrriGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 1425 CFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1298-1498 |
1.59e-30 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 120.48 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1298 KKAKIATRNVSFCVrKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREG-DTPGF---LGYCPQENAL 1368
Cdd:cd03297 8 KRLPDFTLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdSRKKiNLPPQqrkIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1369 WPNLTVKEHLEIfaAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 1448
Cdd:cd03297 87 FPHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1449 EGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
479-660 |
1.79e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 124.42 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEniLRI 558
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE--LRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 A----GVCPQanvQFDFL---TVRENLRLFAKIRGIPPQDVEKEVQRvLLE---LEMKnIQNILAQnLSGGQKRKLtfGI 628
Cdd:COG1135 80 ArrkiGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRKRVAE-LLElvgLSDK-ADAYPSQ-LSGGQKQRV--GI 151
|
170 180 190
....*....|....*....|....*....|....
gi 254911033 629 A--ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE 660
Cdd:COG1135 152 AraLANNPKVLLCDEATSALDPETTRSILDLLKD 185
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
480-696 |
2.24e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 120.33 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 480 RIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADlenilRIA 559
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 GVcPQ-ANVQFDF-LTVRE--NLRLFAKIR--GIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGD 633
Cdd:cd03235 72 YV-PQrRSIDRDFpISVRDvvLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 634 SQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFIsNGRLKCAG 696
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
459-698 |
3.69e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.94 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 459 VPSSGDSFEPVSPEFHGKES-IRIRNISKEYKGK-PNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTK 536
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEPlLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 537 GSVTIYNNNLSEM--ADLENILRIAGVCPQ-ANVQFD-FLTVRENLRLFAKIRGI-PPQDVEKEVQRVL----LELEMKn 607
Cdd:COG1123 320 GSILFDGKDLTKLsrRSLRELRRRVQMVFQdPYSSLNpRMTVGDIIAEPLRLHGLlSRAERRERVAELLervgLPPDLA- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 608 iqNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRV--VLFSTQFMDEADILADRKV 685
Cdd:COG1123 399 --DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGltYLFISHDLAVVRYIADRVA 476
|
250
....*....|...
gi 254911033 686 FISNGRLKCAGSS 698
Cdd:COG1123 477 VMYDGRIVEDGPT 489
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
479-692 |
6.67e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.78 E-value: 6.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM--ADLENIL 556
Cdd:COG3638 3 LELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQanvQFDF---LTVREN--------LRLFAKIRGI-PPQDVEK--EV-QRV-LLELEMKniqniLAQNLSGGQ 620
Cdd:COG3638 80 RRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLfPPEDRERalEAlERVgLADKAYQ-----RADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 621 KRKLtfGIA--ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:COG3638 152 QQRV--AIAraLVQEPKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1301-1489 |
7.54e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 118.79 E-value: 7.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQ-ENALW--PnLTVKE- 1376
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrRSIDRdfP-ISVRDv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 -------HLEIFaavRGLRKSHAAvAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:cd03235 91 vlmglygHKGLF---RRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1450 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAIL 1489
Cdd:cd03235 167 TQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
479-692 |
8.62e-30 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 119.52 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENilri 558
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 agvcpQANVQFDF----------LTVRENLRLFAKIRGIPpqDVEKEVQRVLLELEMKniQNIL----AQnLSGGQKRKL 624
Cdd:COG1124 78 -----RRRVQMVFqdpyaslhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLP--PSFLdrypHQ-LSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 625 TFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1295-1499 |
1.87e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 121.74 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP----GFlGYCPQENALW 1369
Cdd:COG3842 11 VSKRyGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpekrNV-GMVFQDYALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEG-----------VKRklcfvlsilgnPSILL 1438
Cdd:COG3842 90 PHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvalaralAPE-----------PRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1439 LDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
500-696 |
1.91e-29 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 117.59 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 500 DLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynnNLSEMADLENILRIAGVCPQANVQFDFLTVRENLR 579
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI---NGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 580 LFA----KIRGIPPQDVEKEVQRVLLELEMKNiqniLAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVW 655
Cdd:cd03298 93 LGLspglKLTAEDRQAIEVALARVGLAGLEKR----LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 656 NLLKERRADR--VVLFSTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:cd03298 169 DLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
478-692 |
2.00e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 121.36 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM-ADLENIl 556
Cdd:COG3842 5 ALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLpPEKRNV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 riaGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQK------RkltfgiAI 630
Cdd:COG3842 80 ---GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrvalaR------AL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFST--QfmDEADILADRKVFISNGRL 692
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVThdQ--EEALALADRIAVMNDGRI 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1278-1493 |
2.03e-29 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 117.57 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1278 IIASCLRKEYAGKQKhclskkkAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG 1357
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1358 FLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSIL 1437
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1438 LLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILvSGR 1493
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
479-692 |
2.22e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 117.51 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAD--LENIL 556
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
479-697 |
2.96e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.94 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmadlENILRI 558
Cdd:PRK13632 8 IKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK----ENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 ---AGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDS 634
Cdd:PRK13632 82 rkkIGIIFQnPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 635 QIFLLDEPTAGLDPFSRHRVWNLLKERR--ADRVVLFSTQFMDEAdILADRKVFISNGRLKCAGS 697
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1278-1498 |
7.34e-29 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 116.09 E-value: 7.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1278 IIASCLRKEYAGKQKHCLSKKKAKIAT-----------RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL 1346
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGrkgevgefwalKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1347 LKGSregDTPGF-LGYcpqenALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLC 1425
Cdd:cd03220 81 VRGR---VSSLLgLGG-----GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1426 FVLSILGNPSILLLDEP-STGlDPEGQQQIWQAIRAIIKNTdRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:cd03220 153 FAIATALEPDILLIDEVlAVG-DAAFQEKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
479-692 |
7.77e-29 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 116.07 E-value: 7.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMadLENILRI 558
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL--SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGvcpqANVQFDF----------LTVRENLRLFAKIRGIPPQDVEKEvQRVLLELEM----KNIQNILAQNLSGGQKRKL 624
Cdd:cd03257 80 RR----KEIQMVFqdpmsslnprMTIGEQIAEPLRIHGKLSKKEARK-EAVLLLLVGvglpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 625 TFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
479-692 |
9.57e-29 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 116.25 E-value: 9.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRI 558
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVqFDFLTVRENLRLFAKIRGIPPQDVEKEVQRV--LLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:cd03295 78 GYVIQQIGL-FPHMTVEENIALVPKLLKWPKEKIRERADELlaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLK--ERRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
480-692 |
2.56e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 115.52 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 480 RIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEnILRiA 559
Cdd:COG0411 6 EVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IAR-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 GVcpqA----NVQ-FDFLTVRENLRL----------FAKIRGIPP-----QDVEKEVQRVLLELEMKNIQNILAQNLSGG 619
Cdd:COG0411 80 GI---ArtfqNPRlFPELTVLENVLVaaharlgrglLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 620 QKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVlfsTQFMDEADI-----LADRKVFISNGRL 692
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGI---TILLIEHDMdlvmgLADRIVVLDFGRV 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
479-692 |
2.75e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.98 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEniLRI 558
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE--LRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 A----GVCPQanvQFDFL---TVRENLRLFAKIRGIPPQDVEKevqRV--LLEL-EMKNIQNILAQNLSGGQKRKLtfGI 628
Cdd:PRK11153 80 ArrqiGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKA---RVteLLELvGLSDKADRYPAQLSGGQKQRV--AI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 629 A--ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK11153 152 AraLASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1283-1494 |
2.75e-28 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 114.12 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYAGKqkhclskKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregDTPGF---- 1358
Cdd:cd03255 6 LSKTYGGG-------GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT---DISKLseke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1359 --------LGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSI 1430
Cdd:cd03255 76 laafrrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1431 LGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMaEAEALCDRVAILVSGRL 1494
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1295-1512 |
4.73e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 114.36 E-value: 4.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP----GFlGYCPQENALWP 1370
Cdd:cd03299 6 LSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpekrDI-SYVPQNYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 NLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 1450
Cdd:cd03299 85 HMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1451 QQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQ----HLKSKFGKDYL 1512
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
478-697 |
4.89e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 114.36 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEnilR 557
Cdd:cd03296 2 SIEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANVQFDFLTVRENLRLFAKIRGI---PPQDVEKEVQRVLLEL-EMKNIQNILAQNLSGGQKRKLTFGIAILGD 633
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRserPPEAEIRAKVHELLKLvQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 634 SQIFLLDEPTAGLDPFSRHRVWNLLKeRRADRV---VLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLR-RLHDELhvtTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1296-1500 |
4.99e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.41 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1296 SKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdTPGFLGYcpqeNA-LWPNLTV 1374
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSALLEL----GAgFHPELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEHLEIFAAVRGLRKShaavAITRLADALK----LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEP-STGlDPE 1449
Cdd:COG1134 106 RENIYLNGRLLGLSRK----EIDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1450 GQQQIWQAIRAIIKNTdRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSI 1500
Cdd:COG1134 181 FQKKCLARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
479-693 |
5.63e-28 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 113.65 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmADLENIlri 558
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 aGVCPQANVQFDFLTVRENLRLFAKIRGIPpqdvEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:TIGR03740 73 -GSLIESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGRLK 693
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1303-1494 |
6.42e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 113.37 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG--------SREGDTPGFLGYCPQE--NALWPNL 1372
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrRLRKIRRKEIQMVFQDpmSSLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHL-EIFAAVRGLRK-SHAAVAITRLADALKL-QDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:cd03257 100 TIGEQIaEPLRIHGKLSKkEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254911033 1450 GQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03257 180 VQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
479-691 |
8.65e-28 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 113.43 E-value: 8.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM--ADLENIL 556
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 R-IAGVCPQANVqFDFLTVRENL---RLFAK--IRGIPPQDVEKEVQRVLLELE---MKNIQNILAQNLSGGQKRKLtfG 627
Cdd:cd03256 78 RqIGMIFQQFNL-IERLSVLENVlsgRLGRRstWRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLSGGQQQRV--A 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 628 IA--ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGR 691
Cdd:cd03256 155 IAraLMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
477-697 |
1.34e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.71 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 477 ESIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENIL 556
Cdd:PRK13548 1 AMLEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAgVCPQ-ANVQFDFlTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQK------RKLTFGIA 629
Cdd:PRK13548 77 RRA-VLPQhSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 630 ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR-----VVL----FSTQFmdeadilADRKVFISNGRLKCAGS 697
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglaviVVLhdlnLAARY-------ADRIVLLHQGRLVADGT 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
479-698 |
1.54e-27 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 112.64 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRI 558
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGRLKCAGSS 698
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
479-648 |
1.62e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 113.64 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKE-YKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLE---N 554
Cdd:COG1101 2 LELKNLSKTfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKrakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 555 ILRI-----AGVCPQanvqfdfLTVRENLRLFAK-------IRGIPPQDVEKEVQRV-LLELEMKNIQNILAQNLSGGQK 621
Cdd:COG1101 82 IGRVfqdpmMGTAPS-------MTIEENLALAYRrgkrrglRRGLTKKRRELFRELLaTLGLGLENRLDTKVGLLSGGQR 154
|
170 180
....*....|....*....|....*..
gi 254911033 622 RKLTFGIAILGDSQIFLLDEPTAGLDP 648
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDP 181
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
496-697 |
1.72e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 112.23 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 496 EALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILR-IAGVcPQANVQFDFLTV 574
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV-PQGREIFPRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 575 RENLRLFAKIRGIPPQDVEKEVqrvlLEL-----EMKNIQnilAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPf 649
Cdd:TIGR03410 93 EENLLTGLAALPRRSRKIPDEI----YELfpvlkEMLGRR---GGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254911033 650 S----RHRVWNLLKERRaDRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:TIGR03410 165 SiikdIGRVIRRLRAEG-GMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1301-1493 |
1.87e-27 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 110.35 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFL-------GYCPQENALWPNLT 1373
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrriGMVFQDFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 VKEHLEIfaavrglrkshaavaitrladalklqdqlkspvkTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQ 1453
Cdd:cd03229 93 VLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1454 IWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:cd03229 139 VRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
479-697 |
2.20e-27 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 112.33 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNlseMADLENILRI 558
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD---ITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 639 LDEPTAGLDpfSRHRVWNLLKERRADRVV----LFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:cd03300 154 LDEPLGALD--LKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
478-692 |
3.99e-27 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.14 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKPNKieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILR 557
Cdd:cd03245 2 RIEFRNVSFSYPNQEIP--ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANVQFdFLTVRENLRLFAkirgiPPQDVEkevqRVLLELEMKNIQNILA--------------QNLSGGQKRK 623
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLGA-----PLADDE----RILRAAELAGVTDFVNkhpngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 624 LTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADiLADRKVFISNGRL 692
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
471-692 |
5.02e-27 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 110.70 E-value: 5.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 471 PEFHGKESIRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIyNNNLSEMA 550
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVSSLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 551 DLEnilriAGVCPQanvqfdfLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAI 630
Cdd:cd03220 90 GLG-----GGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD-RVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
479-692 |
5.36e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 108.67 E-value: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynnnlsemadlenilri 558
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 agvcpqANVQFDFLTVRENLRLfakirGIppqdvekevqrvllelemkniqNILAQnLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03216 60 ------DGKEVSFASPRDARRA-----GI----------------------AMVYQ-LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
481-668 |
9.61e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 110.98 E-value: 9.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEnILRiAG 560
Cdd:COG4674 13 VEDLTVSFDG----FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHE-IAR-LG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 561 VC-----PqaNVqFDFLTVRENLRL--------FAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFG 627
Cdd:COG4674 87 IGrkfqkP--TV-FEELTVFENLELalkgdrgvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 628 IAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVL 668
Cdd:COG4674 164 MLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVV 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
477-697 |
1.13e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 477 ESIRIRNISKEY------------------KGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGS 538
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 539 VTIyNNNLSEMADLEnilriAGVCPQanvqfdfLTVRENLRLFAKIRGIPPQDVEKEVQRVL--------LELEMKniqn 610
Cdd:COG1134 83 VEV-NGRVSALLELG-----AGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIVefaelgdfIDQPVK---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 611 ilaqNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD-RVVLFSTQFMDEADILADRKVFISN 689
Cdd:COG1134 146 ----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
....*...
gi 254911033 690 GRLKCAGS 697
Cdd:COG1134 222 GRLVMDGD 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
479-688 |
1.35e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.72 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLS-EMADlenilR 557
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgPGAD-----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 iaGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLtfGIA--ILGDSQ 635
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRV--GIAraLAADPR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 636 IFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFIS 688
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
476-692 |
2.01e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.42 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 476 KESIRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENI 555
Cdd:COG1132 337 RGEIEFENVSFSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL-TLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRIAGVCPQANVQFDfLTVRENLRLFAKirGIPPQDVEK-----EVQRVLLELEmKNIQNILAQ---NLSGGQKRKLTFG 627
Cdd:COG1132 413 RRQIGVVPQDTFLFS-GTIRENIRYGRP--DATDEEVEEaakaaQAHEFIEALP-DGYDTVVGErgvNLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 628 IAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVL-----FSTqfmdeadIL-ADRKVFISNGRL 692
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIviahrLST-------IRnADRILVLDDGRI 552
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
475-697 |
3.15e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 475 GKESIRIRNISKEYK--GKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADL 552
Cdd:PRK13633 1 MNEMIKCKNVSYKYEsnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 553 ENILRIAGVCPQ--------ANVQFDFLTVRENLrlfakirGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKl 624
Cdd:PRK13633 81 WDIRNKAGMVFQnpdnqivaTIVEEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 625 tfgIAILG----DSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEAdILADRKVFISNGRLKCAGS 697
Cdd:PRK13633 153 ---VAIAGilamRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
483-692 |
3.27e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 108.51 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 483 NISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL--SVPTKGSVTIYNNnlSEMaDLENILRIAG 560
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveGGGTTSGQILFNG--QPR-KPDQFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 561 VCPQANVQFDFLTVRENLRLFAKIRGiP-----PQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQ 635
Cdd:cd03234 85 YVRQDDILLPGLTVRETLTYTAILRL-PrkssdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 636 IFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQfMDEADI--LADRKVFISNGRL 692
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIH-QPRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1301-1498 |
4.95e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 107.73 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEH 1377
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKdrdIAMVFQNYALYPHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQA 1457
Cdd:cd03301 93 IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 1458 IRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:cd03301 173 LKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1305-1498 |
5.74e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 106.37 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-----FLGYCPQenALwpnltvkehle 1379
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkelarKIAYVPQ--AL----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 ifaavrglrkshAAVAITRLADalklqdqlkSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 1459
Cdd:cd03214 83 ------------ELLGLAHLAD---------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLR 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 254911033 1460 AIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:cd03214 142 RLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
479-696 |
8.55e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 105.86 E-value: 8.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynnNLSEMADLENILRI 558
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL---DGVPVSDLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 A-GVCPQANVQFDfLTVRENLrlfakirGIPpqdvekevqrvllelemkniqnilaqnLSGGQKRKLTFGIAILGDSQIF 637
Cdd:cd03247 76 LiSVLNQRPYLFD-TTLRNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADiLADRKVFISNGRLKCAG 696
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
478-713 |
8.79e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.10 E-value: 8.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEY-KGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynNNLSEMAD----- 551
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKtkdky 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 552 LENILRIAGVC---PQANVQFDflTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKniQNILAQN---LSGGQKRKLT 625
Cdd:PRK13646 80 IRPVRKRIGMVfqfPESQLFED--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 626 FgIAILG-DSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD--RVVLFSTQFMDEADILADRKVFISNGRL--KCAGSSLF 700
Cdd:PRK13646 156 I-VSILAmNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELF 234
|
250
....*....|...
gi 254911033 701 LKKKWGVGYHLSL 713
Cdd:PRK13646 235 KDKKKLADWHIGL 247
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
479-692 |
1.02e-25 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 107.77 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM--ADLENIL 556
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQANVQFDFLTVRENL---RLFAK--IRGIPPQDVEKEVQRVLLELEMKNIQ---NILAQNLSGGQKRKLTFGI 628
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgRLGYKptWRSLLGRFSEEDKERALSALERVGLAdkaYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 629 AILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
479-692 |
2.66e-25 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 105.69 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSemADLENIL-- 556
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT--DDKKNINel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 --RIAGVCPQANVqFDFLTVRENLRL-FAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGD 633
Cdd:cd03262 75 rqKVGMVFQQFNL-FPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 634 SQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1273-1503 |
2.78e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.92 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1273 DEKPVIIASCLRKEYAGKqkhclsKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG--- 1349
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVR------GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1350 --SREGDTPGF---LGYCPQ--ENALWPNLTVKEHLEIFAAVRGLRKSHAAVAitRLADALKL----QDQLKSPVKTLSE 1418
Cdd:COG1123 330 tkLSRRSLRELrrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRE--RVAELLERvglpPDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1419 GVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....*
gi 254911033 1499 SIQHL 1503
Cdd:COG1123 488 PTEEV 492
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
441-671 |
3.33e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 112.07 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 441 WLQTRKPAHVILEDGIDPVPSSGDSFEPVSPEFHGKESIRIRNISKEYKGKPnkiEALKDLTLDIYEGQITAVLGHSGAG 520
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 521 KSTLLNILSGLSVPTKGSVTIYNNNLSEmADLENILRIAGVCPQANVQFDfLTVRENLRLFAKirGIPPQDVEKEVQRVL 600
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPVSS-LDQDEVRRRVSVCAQDAHLFD-TTVRENLRLARP--DATDEELWAALERVG 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 601 LELEMKNIQNIL-------AQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFST 671
Cdd:TIGR02868 450 LADWLRALPDGLdtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLIT 527
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1283-1503 |
6.86e-25 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 104.97 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYAGKqkhclskKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---- 1358
Cdd:cd03258 7 VSKVFGDT-------GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1359 ----LGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNP 1434
Cdd:cd03258 80 arrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 1435 SILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
479-703 |
8.04e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 104.61 E-value: 8.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRI 558
Cdd:cd03254 3 IEFENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFlTVRENLRLFakiRGIPPQDVEKEV-QRVLLELEMKNIQNIL-------AQNLSGGQKRKLTFGIAI 630
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLG---RPNATDEEVIEAaKEAGAHDFIMKLPNGYdtvlgenGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVL-----FSTqfmdeadIL-ADRKVFISNGRLKCAGS--SLFLK 702
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIiiahrLST-------IKnADKILVLDDGKIIEEGThdELLAK 227
|
.
gi 254911033 703 K 703
Cdd:cd03254 228 K 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
471-692 |
1.09e-24 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.50 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 471 PEFHGKesIRIRNISKEYKGkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM- 549
Cdd:TIGR03375 458 PRLQGE--IEFRNVSFAYPG--QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQId 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 550 -ADL-ENIlriaGVCPQANVQFdFLTVRENLRLFAkirgipPQDVEKEVQRVLLELEMKNIQNILAQ-----------NL 616
Cdd:TIGR03375 534 pADLrRNI----GYVPQDPRLF-YGTLRDNIALGA------PYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSL 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 617 SGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFST---QFMDeadiLADRKVFISNGRL 692
Cdd:TIGR03375 603 SGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVThrtSLLD----LVDRIIVMDNGRI 677
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
492-677 |
1.62e-24 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 102.50 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 492 PNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNL--SEMADLENILRIAGVCPQANVQF 569
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 570 DFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPF 649
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*....
gi 254911033 650 SRHRVWNLLKERRAD-RVVLFSTQFMDEA 677
Cdd:TIGR01166 162 GREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1305-1494 |
1.68e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.63 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTA--GQVLLKG--SREGDTPGFLGYCPQENALWPNLTVKEHLEI 1380
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGrpLDKRSFRKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1381 FAAVRGLrkshaavaitrladalklqdqlkspvktlSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 1460
Cdd:cd03213 106 AAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190
....*....|....*....|....*....|....*
gi 254911033 1461 iIKNTDRGALLTTHY-MAEAEALCDRVAILVSGRL 1494
Cdd:cd03213 157 -LADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1305-1474 |
2.29e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 102.64 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDT--PGFLGYCPQENALWPNLTVKEHLEIFA 1382
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1383 AVRGLRKSHAAVAItrlaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAii 1462
Cdd:PRK13539 99 AFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-- 172
|
170
....*....|....
gi 254911033 1463 kNTDRG--ALLTTH 1474
Cdd:PRK13539 173 -HLAQGgiVIAATH 185
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
479-693 |
2.36e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.02 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKiealkdLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEnilRI 558
Cdd:TIGR01277 1 LALDKVRYEYEHLPME------FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ---RP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLfakirGIPP----QDVEKE-VQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGD 633
Cdd:TIGR01277 72 VSMLFQENNLFAHLTVRQNIGL-----GLHPglklNAEQQEkVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 634 SQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLK 693
Cdd:TIGR01277 147 NPILLLDEPFSALDPLLREEMLALVKQlcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
451-685 |
3.69e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 108.91 E-value: 3.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 451 ILEDGIDPVPSSGDSFEPVSPefhgkeSIRIRNISKEYKGKPNkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSG 530
Cdd:TIGR02857 300 VLDAAPRPLAGKAPVTAAPAS------SLEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 531 LSVPTKGSVTIYNNNLSEmADLENILRIAGVCPQANVQFDfLTVRENLRLFAkiRGIPPQDVEKEVQRV-LLELEM---K 606
Cdd:TIGR02857 371 FVDPTEGSIAVNGVPLAD-ADADSWRDQIAWVPQHPFLFA-GTIAENIRLAR--PDASDAEIREALERAgLDEFVAalpQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 607 NIQNILAQN---LSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQfmDEADI-LAD 682
Cdd:TIGR02857 447 GLDTPIGEGgagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--RLALAaLAD 524
|
...
gi 254911033 683 RKV 685
Cdd:TIGR02857 525 RIV 527
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1305-1493 |
4.30e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 103.24 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL-LKGSREGDTPGF-----LGYCPQENALW--PNLTVke 1376
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDVWelrkrIGLVSPALQLRfpRDETV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 hLEI----FAAVRGLRKSHAAVAITR---LADALKLQDQLKSPVKTLSEGVKRKlcfVL---SILGNPSILLLDEPSTGL 1446
Cdd:COG1119 98 -LDVvlsgFFDSIGLYREPTDEQRERareLLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254911033 1447 DPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:COG1119 174 DLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1305-1494 |
4.85e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.05 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-----REGDTPGF---LGYCPQENALWPNLTVKE 1376
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlKRREIPYLrrrIGVVFQDFRLLPDRTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEIFAAVRGLRKSHAAvaiTRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQ 1453
Cdd:COG2884 99 NVALPLRVTGKSRKEIR---RRVREVLDlvgLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 1454 IWQAIRAIikNtDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG2884 176 IMELLEEI--N-RRGTtvLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
479-713 |
7.72e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.56 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGK-PNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLS---EMADLEN 554
Cdd:PRK13634 3 ITFQKVEHRYQYKtPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 555 ILRIAGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKniQNILAQN---LSGGQKRKltfgIAI 630
Cdd:PRK13634 83 LRKKVGIVFQfPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP--EELLARSpfeLSGGQMRR----VAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 631 LG----DSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS--SLFLK 702
Cdd:PRK13634 157 AGvlamEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFAD 236
|
250
....*....|.
gi 254911033 703 KKWGVGYHLSL 713
Cdd:PRK13634 237 PDELEAIGLDL 247
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
479-692 |
9.25e-24 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 102.72 E-value: 9.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNK--------------------IEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGS 538
Cdd:cd03294 1 IKIKGLYKIFGKNPQKafkllakgkskeeilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 539 VTIYNNNLSEM--ADLENILR--IAGVCpQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQ 614
Cdd:cd03294 81 VLIDGQDIAAMsrKELRELRRkkISMVF-QSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 615 NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD--RVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
478-697 |
1.04e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.20 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEY-KGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNL-SEMADLENI 555
Cdd:PRK13637 2 SIKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRIAGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRV--LLELEMKNIQNILAQNLSGGQKRKltfgIAILG 632
Cdd:PRK13637 82 RKKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRR----VAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 633 ----DSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK13637 158 vvamEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
478-697 |
1.11e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYK-GKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NNLSEMADLE 553
Cdd:PRK13649 2 GINLQNVSYTYQaGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtliTSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NILRIAGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKevqRVLLELEMKNI-QNILAQN---LSGGQKRKltfgI 628
Cdd:PRK13649 82 QIRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEA---LAREKLALVGIsESLFEKNpfeLSGGQMRR----V 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 629 AILG----DSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK13649 155 AIAGilamEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
498-696 |
1.68e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 100.45 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDI---YEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSV----TIYNNNLSEMaDLENILRIAGVCPQANVQFD 570
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLFDSRKKI-NLPPQQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 571 FLTVRENLrLFAKIRGIPPQDvEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFS 650
Cdd:cd03297 89 HLNVRENL-AFGLKRKRNRED-RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254911033 651 RHRVWNLLKERRAD--RVVLFSTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:cd03297 167 RLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
479-692 |
1.77e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.08 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLS-EMADLENILR 557
Cdd:PRK13639 2 LETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKltfgIAILG---- 632
Cdd:PRK13639 79 TVGIVFQnPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR----VAIAGilam 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 633 DSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
479-697 |
2.17e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 101.35 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLS-----EMAdle 553
Cdd:COG4559 2 LEAENLSVRLGGRT----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawspwELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 nilRIAGVCPQA-NVQFDFlTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAIL- 631
Cdd:COG4559 75 ---RRRAVLPQHsSLAFPF-TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 632 ------GDSQIFLLDEPTAGLDPFSRHRVWNLLKeRRADR-----VVL----FSTQFmdeadilADRKVFISNGRLKCAG 696
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLAR-QLARRgggvvAVLhdlnLAAQY-------ADRILLLHQGRLVAQG 222
|
.
gi 254911033 697 S 697
Cdd:COG4559 223 T 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
479-696 |
3.36e-23 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 100.10 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynnNLSEMADLENILRI 558
Cdd:cd03299 1 LKVENLSKDWKEF-----KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL---NGKDITNLPPEKRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLlelEMKNIQNILAQN---LSGGQKRKLTFGIAILGDSQ 635
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIA---EMLGIDHLLNRKpetLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 636 IFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
479-682 |
3.37e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.07 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSemADLENILRI 558
Cdd:COG1126 2 IEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 agvcpQANV----Q----FDFLTVRENLRLfA--KIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQK-Rkltfg 627
Cdd:COG1126 76 -----RRKVgmvfQqfnlFPHLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQqR----- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 628 IAI---LG-DSQIFLLDEPTAGLDPFSRHRVWNLLKE------------------RR-ADRVVlfstqFMDEADILAD 682
Cdd:COG1126 145 VAIaraLAmEPKVMLFDEPTSALDPELVGEVLDVMRDlakegmtmvvvthemgfaREvADRVV-----FMDGGRIVEE 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1305-1494 |
3.49e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTP------GfLGYCPQENALWPNLTVKEH 1377
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvRFRSPrdaqaaG-IAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 leIF----AAVRGLRKSHAAVAITR-LADALKLQDQLKSPVKTLSEGvKRKLcfVL---SILGNPSILLLDEPSTGLDPE 1449
Cdd:COG1129 100 --IFlgrePRRGGLIDWRAMRRRAReLLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254911033 1450 GQQQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG1129 175 EVERLFRIIRRL---KAQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1302-1494 |
4.61e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1302 IATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTPGF-----LGYCPQENALWPNLTVK 1375
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvRIRSPRDaialgIGMVHQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHLeIFAA--VRGLRKSHAAVA--ITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 1451
Cdd:COG3845 99 ENI-VLGLepTKGGRLDRKAARarIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254911033 1452 QQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG3845 178 DELFEILRRL---AAEGKsiIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
479-691 |
4.98e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.44 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkiealKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdlenilri 558
Cdd:COG3840 2 LRLDDLTYRYGDFP------LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 agvcP---------QANVQFDFLTVRENLRLfakirGIPP---------QDVEKEVQRV-LLELEMKniqniLAQNLSGG 619
Cdd:COG3840 68 ----PaerpvsmlfQENNLFPHLTVAQNIGL-----GLRPglkltaeqrAQVEQALERVgLAGLLDR-----LPGQLSGG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 620 QKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQFMDEADILADRKVFISNGR 691
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
479-726 |
5.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.03 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVP---TKGSVTIYNNNLSE--MADLE 553
Cdd:PRK13640 6 VEFKHVSFTYPD--SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAktVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NilRIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKltfgIAILG- 632
Cdd:PRK13640 84 E--KVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR----VAIAGi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 633 ---DSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR-VVLFS-TQFMDEADiLADRKVFISNGRLKCAGS--SLFLK--- 702
Cdd:PRK13640 158 lavEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSpvEIFSKvem 236
|
250 260 270
....*....|....*....|....*....|.
gi 254911033 703 -KKWGVG----YHLSLQLKE--VCVPENITS 726
Cdd:PRK13640 237 lKEIGLDipfvYKLKNKLKEkgISVPQEINT 267
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1303-1494 |
5.52e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 97.11 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSRegdtpgflgycpqenalwpnltvkehleifa 1382
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1383 avrglrkshaaVAITRLADALKL------QdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:cd03216 64 -----------VSFASPRDARRAgiamvyQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1457 AIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03216 124 VIRRL---RAQGVavIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1300-1503 |
5.81e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 105.23 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-----REGDTPGFLGYCPQENALWpNLTV 1374
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdlDEDDLRRRIAVVPQRPHLF-DTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEHLEIF------AAVRglrkshAAVAITRLADALK-LQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:COG4987 426 RENLRLArpdatdEELW------AALERVGLGDWLAaLPDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1444 TGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHL 1503
Cdd:COG4987 500 EGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
479-678 |
5.93e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 106.75 E-value: 5.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgkpnKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENIL-R 557
Cdd:NF033858 2 ARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCpR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVcPQA---NVQFDfLTVRENLRLFAKIRGippQDVEKEVQRvllelemknIQNIL------------AQNLSGGQKR 622
Cdd:NF033858 78 IAYM-PQGlgkNLYPT-LSVFENLDFFGRLFG---QDAAERRRR---------IDELLratglapfadrpAGKLSGGMKQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 623 KLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRV---VLFSTQFMDEAD 678
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATAYMEEAE 202
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
488-685 |
6.69e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 6.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 488 YKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNnlsemadleniLRIAGVCPQANV 567
Cdd:NF040873 2 YGGRP----VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 568 QFDF-LTVRE--------NLRLFAKIRGIPPQDVEKEVQRV-LLELEMKNIQNilaqnLSGGQKRKLTFGIAILGDSQIF 637
Cdd:NF040873 67 PDSLpLTVRDlvamgrwaRRGLWRRLTRDDRAAVDDALERVgLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKERRAD-RVVLFSTQFMDEAdILADRKV 685
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELV-RRADPCV 189
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
476-749 |
6.70e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.47 E-value: 6.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 476 KESIRIRNISKEYKGkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmadlENI 555
Cdd:PRK13635 3 EEIIRVEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE----ETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 L----RIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKltfgIAIL 631
Cdd:PRK13635 77 WdvrrQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQR----VAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 632 G----DSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQFMDEAdILADRKVFISNGRLKCAG--SSLFlkk 703
Cdd:PRK13635 153 GvlalQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEA-AQADRVIVMNKGEILEEGtpEEIF--- 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 704 kwgvgyHLSLQLKE----VCVPENITSLVKQH---IPAAKLSAEGEGKLLYTL 749
Cdd:PRK13635 229 ------KSGHMLQEigldVPFSVKLKELLKRNgilLPNTYLTMESLVDELWTL 275
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
479-692 |
6.83e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.73 E-value: 6.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLS--VP---TKGSVTIYNNN-LSEMADL 552
Cdd:COG1117 12 IEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGEDiYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 553 ENI-LRIAGVCPQANVqfdF-LTVRENLRLFAKIRGIPPQD-----VEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLT 625
Cdd:COG1117 88 VELrRRVGMVFQKPNP---FpKSIYDNVAYGLRLHGIKSKSeldeiVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 626 fgIA--ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:COG1117 165 --IAraLAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1305-1504 |
8.00e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 99.11 E-value: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREGDTPGFL--GYCPQENALWPNLTV-- 1374
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglSEAELYRLRRrmGMLFQSGALFDSLTVfe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 ------KEHL-----EIFAAVR------GLRkshaavaitrlADALKLQDQLkspvktlSEGVKRKLCFVLSILGNPSIL 1437
Cdd:cd03261 97 nvafplREHTrlseeEIREIVLekleavGLR-----------GAEDLYPAEL-------SGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1438 LLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK 1504
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1303-1525 |
8.63e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.98 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsREGDtPGFL------GYCPQENALWPNLTVKE 1376
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG-QPVD-AGDIatrrrvGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1457 AI-------RAIIkntdrgaLLTTHYMAEAEaLCDRVAILVSGRLRCIGSIQHLKSKFGKDYLLEMKVKTLEQVEP 1525
Cdd:NF033858 439 LLielsredGVTI-------FISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARGAATLEEAFIAYLEEAAG 506
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1283-1499 |
9.04e-23 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 98.85 E-value: 9.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYAGKqkhclskkkakIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---L 1359
Cdd:cd03300 6 VSKFYGGF-----------VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrpV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1360 GYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLL 1439
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1440 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
479-711 |
1.11e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 98.46 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRI 558
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFlTVRENLRlFAKiRGIPPQDVEKEVQRV-LLELEMK---NIQNILAQN---LSGGQKRKLTFGIAIL 631
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA-YGR-PGATREEVEEAARAAnAHEFIMElpeGYDTVIGERgvkLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 632 GDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVL-----FSTqFMDeadilADRKVFISNGRLKCAGSSLFLKKKWG 706
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST-IEN-----ADRIVVLEDGKIVERGTHEELLAQGG 228
|
....*
gi 254911033 707 VGYHL 711
Cdd:cd03251 229 VYAKL 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
478-692 |
1.23e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNN--NLSEMADLENI 555
Cdd:PRK11124 2 SIQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 --LR--IAGVCPQANVqFDFLTVRENL-RLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAI 630
Cdd:PRK11124 78 reLRrnVGMVFQQYNL-WPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD---RVVLfsTQFMDEADILADRKVFISNGRL 692
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
498-663 |
1.23e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.64 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNnnlSEMADLENILRIAGVCPQaNVQFDFLTVREN 577
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHR-NAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 578 LRLFAKIRGIPPQDVEKEVQRVllelEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNL 657
Cdd:PRK13539 94 LEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAEL 169
|
....*.
gi 254911033 658 LKERRA 663
Cdd:PRK13539 170 IRAHLA 175
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
479-692 |
1.53e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.69 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLS-----VPTKGSVtIYN--NNLSEMAD 551
Cdd:PRK14239 6 LQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSI-VYNghNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 552 LENILRIAGVCPQANVQFDFlTVRENLRLFAKIRGIPPQD-----VEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTF 626
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQvldeaVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 627 GIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
478-692 |
1.53e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNN--NLSEMADLENI 555
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 --LR--IAGVCPQANVqFDFLTVRENLrLFAKIR--GIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIA 629
Cdd:COG4161 78 rlLRqkVGMVFQQYNL-WPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 630 ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRA---DRVVLfsTQFMDEADILADRKVFISNGRL 692
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIV--THEVEFARKVASQVVYMEKGRI 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1305-1500 |
2.07e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 97.54 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsREGDTPG------FLGYcpqenALWPNLTVKEH- 1377
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-KQITEPGpdrmvvFQNY-----SLLPWLTVRENi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 -LEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:TIGR01184 76 aLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254911033 1457 AIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSI 1500
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
478-697 |
2.35e-22 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 97.18 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILR 557
Cdd:cd03244 2 DIEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANVQFDFlTVRENLRLFAkirgippQDVEKEVQRVLLELEMKNIQNILA-----------QNLSGGQKRKLTF 626
Cdd:cd03244 79 RISIIPQDPVLFSG-TIRSNLDPFG-------EYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 627 GIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQ----FMDeadilADRKVFISNGRLKCAGS 697
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1305-1504 |
2.72e-22 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 97.74 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREGDTP-----GFLGycpQENALWPNLT 1373
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglSEKELYElrrriGMLF---QGGALFDSLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 VKEHLEIfaavrGLRKsHaavaiTRLADALKlqDQLkspvktlsegVKRKLCFV------------LS------------ 1429
Cdd:COG1127 99 VFENVAF-----PLRE-H-----TDLSEAEI--REL----------VLEKLELVglpgaadkmpseLSggmrkrvalara 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1430 ILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK 1504
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1306-1501 |
3.08e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.92 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF-----LGYCPQENALWPNLTVKEHLEI 1380
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrRAVLPQHSSLSFPFTVEEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1381 FAAVRGLRKSHAAVAIT---RLADALKLQDqlkSPVKTLSEGVK------RKLCFVLSILGNPSILLLDEPSTGLDPEGQ 1451
Cdd:PRK13548 100 GRAPHGLSRAEDDALVAaalAQVDLAHLAG---RDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEPTSALDLAHQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1452 QQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQ 1501
Cdd:PRK13548 177 HHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
479-711 |
6.08e-22 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 96.45 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdLENILRI 558
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDfLTVRENLRLfakirGIPPQDVEkEVQRVlleLEMKNIQNILAQ--------------NLSGGQKRKL 624
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRY-----GKPDATDE-EVEEA---AKKANIHDFIMSlpdgydtlvgergsQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 625 TFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVL-----FSTqfmdeadIL-ADRKVFISNGRLKCAGSS 698
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLST-------IRnADLIAVLQNGQVVEQGTH 221
|
250
....*....|...
gi 254911033 699 LFLKKKWGVGYHL 711
Cdd:cd03249 222 DELMAQKGVYAKL 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
465-660 |
6.18e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 102.43 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 465 SFEPVSPEFHGKESIRI---RNISKEYKGKPNKIeALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVP-TKGSVT 540
Cdd:TIGR00955 6 RNSDVFGRVAQDGSWKQlvsRLRGCFCRERPRKH-LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 541 IYNNnlSEMADLENILRIAGVCPQANVQFDFLTVRENLRLFAKIRgiPPQDVEKE-----VQRVLLELEMKNIQNILAQ- 614
Cdd:TIGR00955 85 VLLN--GMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLR--MPRRVTKKekrerVDEVLQALGLRKCANTRIGv 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 615 -----NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE 660
Cdd:TIGR00955 161 pgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
479-697 |
7.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRI 558
Cdd:PRK13644 2 IRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:PRK13644 79 VGIVFQnPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 638 LLDEPTAGLDPFSRHRVW-NLLKERRADRVVLFSTQFMDEADIlADRKVFISNGRLKCAGS 697
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLeRIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1305-1493 |
7.49e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 93.99 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL-----LKGSREGDTPGFLGYCPQENALWpNLTVKEHLe 1379
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdLRDLDLESLRKNIAYVPQDPFLF-SGTIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 ifaavrglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 1459
Cdd:cd03228 97 ------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|....
gi 254911033 1460 AIIKntDRGALLTTHYMAEAEaLCDRVAILVSGR 1493
Cdd:cd03228 141 ALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1276-1494 |
9.49e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 96.28 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1276 PVIIASCLRKEYAGKQKhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDT 1355
Cdd:COG3638 1 PMLELRNLSKRYPGGTP----------ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1356 PGF--------LGYCPQENALWPNLTVKE--------HLEIFAAVRGL-RKSHAAVAITRLaDALKLQDQLKSPVKTLSE 1418
Cdd:COG3638 71 RGRalrrlrrrIGMIFQQFNLVPRLSVLTnvlagrlgRTSTWRSLLGLfPPEDRERALEAL-ERVGLADKAYQRADQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1419 G------VKRKLCfvlsilGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRG--ALLTTHYMAEAEALCDRVAILV 1490
Cdd:COG3638 150 GqqqrvaIARALV------QEPKLILADEPVASLDPKTARQVMDLLRRI--AREDGitVVVNLHQVDLARRYADRIIGLR 221
|
....
gi 254911033 1491 SGRL 1494
Cdd:COG3638 222 DGRV 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1301-1516 |
1.06e-21 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 96.73 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDtpgflgycpqENALW----------- 1369
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD----------EENLWeirkkvgmvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 -P-----NLTVKE------------HLEIfaavrglrkshaavaITRLADALK---LQDQLKSPVKTLSEGVKRKLCfVL 1428
Cdd:TIGR04520 85 nPdnqfvGATVEDdvafglenlgvpREEM---------------RKRVDEALKlvgMEDFRDREPHLLSGGQKQRVA-IA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1429 SILG-NPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSKf 1507
Cdd:TIGR04520 149 GVLAmRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ- 226
|
....*....
gi 254911033 1508 gKDYLLEMK 1516
Cdd:TIGR04520 227 -VELLKEIG 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
482-659 |
1.13e-21 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 94.23 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 482 RNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSvpTKGSVT--IYnnnLSEMADLENILRIA 559
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVITgeIL---INGRPLDKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 GVCPQANVQFDFLTVRENLRLFAKIRGippqdvekevqrvllelemkniqnilaqnLSGGQKRKLTFGIAILGDSQIFLL 639
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFL 132
|
170 180
....*....|....*....|
gi 254911033 640 DEPTAGLDPFSRHRVWNLLK 659
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLK 152
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1297-1494 |
1.22e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.42 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1297 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG---DTKVTAGQVLLKG--SREGDTPGFLGYCPQENALWPN 1371
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGqpRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKEHLEIFAAVRGLRKSHAA-------------VAITRLADALklqdqlkspVKTLSEGVKRKLCFVLSILGNPSILL 1438
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDAirkkrvedvllrdLALTRIGGNL---------VKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1439 LDEPSTGLDPEGQQQIWQAIRAIIKnTDRGALLTTHY-MAEAEALCDRVAILVSGRL 1494
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
479-700 |
1.45e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.33 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRI 558
Cdd:PRK11614 6 LSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW-QTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 A-GVCPQANVQFDFLTVRENLRL---FAKirgipPQDVEKEVQRV---LLELEMKNIQNilAQNLSGGQKRKLTFGIAIL 631
Cdd:PRK11614 81 AvAIVPEGRRVFSRMTVEENLAMggfFAE-----RDQFQERIKWVyelFPRLHERRIQR--AGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 632 GDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLF-STQFMDEADILADRKVFISNGR--LKCAGSSLF 700
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFlVEQNANQALKLADRGYVLENGHvvLEDTGDALL 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1300-1499 |
1.47e-21 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 96.37 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF--------LGYCPQ--ENALW 1369
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKklkdlrkkVGLVFQfpEHQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNlTVKEhlEI-FAAVR-GLRKSHAAVAITRLADALKLQDQL--KSPVKtLSEGVKRKLCF--VLSIlgNPSILLLDEPS 1443
Cdd:TIGR04521 97 EE-TVYK--DIaFGPKNlGLSEEEAEERVKEALELVGLDEEYleRSPFE-LSGGQMRRVAIagVLAM--EPEVLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1444 TGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1305-1513 |
1.78e-21 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 101.45 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQENALWP-----NLTV 1374
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlRQIDPASLrrqIGVVLQDVFLFSgtireNITL 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 -KEHLEIFAAVRGLRKSHAavaitrLADALKLQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:COG2274 572 gDPDATDEEIIEAARLAGL------HDFIEALPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAE 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1450 GQQQIWQAIRAIIKNtdRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSKFGKDYLL 1513
Cdd:COG2274 646 TEAIILENLRRLLKG--RTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
479-690 |
1.93e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLS-EMADLENILR 557
Cdd:PRK11248 2 LQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgPGAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANVQfdfltvrENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:PRK11248 78 NEGLLPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNG 690
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
498-690 |
2.02e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.84 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdlenilriagvcPQANVQFD------F 571
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG------------PDRMVVFQnysllpW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 572 LTVRENLRLfAKIRGIPpqDVEKEVQRVLLE--LEMKNIQNILAQ---NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGL 646
Cdd:TIGR01184 69 LTVRENIAL-AVDRVLP--DLSKSERRAIVEehIALVGLTEAADKrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254911033 647 DPFSR----HRVWNLLKERRAdrVVLFSTQFMDEADILADRKVFISNG 690
Cdd:TIGR01184 146 DALTRgnlqEELMQIWEEHRV--TVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
479-646 |
2.14e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.86 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMA-DLENILR 557
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IaGVCPQANVQFDFLTVRENL---RLFA-KIRGIPPQDVEKEVQR---VLLELEMKNIQNILAQNLSGGQKRKLTFGIAI 630
Cdd:PRK09700 82 I-GIIYQELSVIDELTVLENLyigRHLTkKVCGVNIIDWREMRVRaamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170
....*....|....*.
gi 254911033 631 LGDSQIFLLDEPTAGL 646
Cdd:PRK09700 161 MLDAKVIIMDEPTSSL 176
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1300-1494 |
2.40e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 93.27 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTPGF-----LGYCP---QENALWP 1370
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvTRRSPRDairagIAYVPedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 NLTVKEHLeifaavrglrkshaavAITRLadalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 1450
Cdd:cd03215 92 DLSVAENI----------------ALSSL----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1451 QQQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03215 140 KAEIYRLIREL---ADAGKavLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
479-696 |
2.64e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.57 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRI 558
Cdd:PRK13647 5 IEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKltfgIAILG----DS 634
Cdd:PRK13647 82 GLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR----VAIAGvlamDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 635 QIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
483-697 |
2.66e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.96 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 483 NISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRIAGVC 562
Cdd:PRK10895 8 NLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 563 PQANVQFDFLTVRENLRLFAKIRgippQDVEKEVQR-----VLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIR----DDLSAEQREdraneLMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
500-697 |
3.03e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 97.48 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 500 DLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENIL----RIaGVCPQ-ANVqFDFLTV 574
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRI-GYVFQeARL-FPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 575 RENLRlFAkIRGIPPQDVEKEVQRV--LLELEmkniqNILA---QNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPF 649
Cdd:COG4148 95 RGNLL-YG-RKRAPRAERRISFDEVveLLGIG-----HLLDrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 650 SRHRVWNLLkERRADRV---VLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:COG4148 168 RKAEILPYL-ERLRDELdipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
478-712 |
3.32e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYK-GKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMA---DLE 553
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NILRIAGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVE----KEVQRVLLELEMKNIQNIlaqNLSGGQKRKLTFGI 628
Cdd:PRK13641 82 KLRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKekalKWLKKVGLSEDLISKSPF---ELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 629 AILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRL--KCAGSSLFLKKKW 705
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEW 238
|
....*..
gi 254911033 706 GVGYHLS 712
Cdd:PRK13641 239 LKKHYLD 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1301-1493 |
3.86e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.77 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---------------SREGDTPgFLGYCPqe 1365
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeykrakyiGRVFQDP-MMGTAP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1366 nalwpNLTVKEHLEIfAAVRG--------LRKSHAAVAITRLAD-ALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSI 1436
Cdd:COG1101 96 -----SMTIEENLAL-AYRRGkrrglrrgLTKKRRELFRELLATlGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1437 LLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
500-697 |
5.47e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 96.72 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 500 DLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMA---DLENILRIAGVCPQANVQFDFLTVRE 576
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 577 NLRL-FAKIRGIPPQDVEKEVQRVLlelemkNIQNILAQ---NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRH 652
Cdd:TIGR02142 95 NLRYgMKRARPSERRISFERVIELL------GIGHLLGRlpgRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254911033 653 RVWNLLkERRADRV---VLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:TIGR02142 169 EILPYL-ERLHAEFgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
478-697 |
5.50e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEnilR 557
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANVQFDFLTVREN----LRLFAKiRGIPPQDVEKevQRVLLELEMKNIQNiLAQ----NLSGGQKRKLTFGIA 629
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNiafgLTVLPR-RERPNAAAIK--AKVTQLLEMVQLAH-LADrypaQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 630 ILGDSQIFLLDEPTAGLDPFSRH--RVW--NLLKERRADRVvlFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKelRRWlrQLHEELKFTSV--FVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1303-1494 |
5.82e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 93.04 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS----------REGdtpgfLGYCPQENALWpNL 1372
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlRRN-----IGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHLEIFAAV----RGLRKSHAAVA---ITRLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTG 1445
Cdd:cd03245 93 TLRDNITLGAPLaddeRILRAAELAGVtdfVNKHPNGLDLQIGERG--RGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 1446 LDPEGQQQIWQAIRAIIKntDRGALLTTHYMAeAEALCDRVAILVSGRL 1494
Cdd:cd03245 171 MDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
452-691 |
6.06e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.83 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 452 LEDGID-PVPSSGDSFEPVspefhgkesIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSG 530
Cdd:PRK11607 1 MNDAIPrPQAKTRKALTPL---------LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 531 LSVPTKGSVTIYNNNLSEMADLEnilRIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQN 610
Cdd:PRK11607 68 FEQPTAGQIMLDGVDLSHVPPYQ---RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 611 ILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHR----VWNLLkERRADRVVLFsTQFMDEADILADRKVF 686
Cdd:PRK11607 145 RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDIL-ERVGVTCVMV-THDQEEAMTMAGRIAI 222
|
....*
gi 254911033 687 ISNGR 691
Cdd:PRK11607 223 MNRGK 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
479-683 |
1.01e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENI-LR 557
Cdd:COG1129 5 LEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVcPQANVQFDFLTVRENL---RLFAKIRGIPPQDVEKEVQRVLLELEMkNIQ-NILAQNLSGGQK------Rkltfg 627
Cdd:COG1129 81 IAII-HQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQqlveiaR----- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 628 iAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADR 683
Cdd:COG1129 154 -ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADR 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1277-1499 |
1.33e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1277 VIIASCLRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------- 1349
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1350 ----SREGdtpgfLGYCPQENALWPNLTVKEHLEIFAAVR-GLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKL 1424
Cdd:PRK10895 72 lharARRG-----IGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1425 CFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
479-697 |
1.42e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.84 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLE----- 553
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElakrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NILRiagvcpQANVQFDFLTVREnLRLFAKI---RGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQkRKLTFgIA- 629
Cdd:COG4604 78 AILR------QENHINSRLTVRE-LVAFGRFpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQ-RQRAF-IAm 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 630 -ILGDSQIFLLDEPTAGLDPfsRHRVwNLLKE-RRADR-------VVLFSTQFmdeADILADRKVFISNGRLKCAGS 697
Cdd:COG4604 149 vLAQDTDYVLLDEPLNNLDM--KHSV-QMMKLlRRLADelgktvvIVLHDINF---ASCYADHIVAMKDGRVVAQGT 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
479-713 |
2.32e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.99 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAD-LENILR 557
Cdd:PRK13636 6 LKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKgLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQA-NVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:PRK13636 83 SVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAG--SSLFLKKKWGVGYHLS 712
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLR 242
|
.
gi 254911033 713 L 713
Cdd:PRK13636 243 L 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
479-696 |
2.43e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 92.07 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKG-SVTIYNNNLSEmadlENIL- 556
Cdd:COG1119 4 LELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGG----EDVWe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 ---RIAGVCPQanVQFDF---LTVRENLR--LFAKI---RGIPPQDVEKeVQRVLLELEMKNIQNILAQNLSGGQKRKLT 625
Cdd:COG1119 76 lrkRIGLVSPA--LQLRFprdETVLDVVLsgFFDSIglyREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 626 FGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEadILA--DRKVFISNGRLKCAG 696
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1303-1506 |
2.46e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 97.14 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQeNALWPNLTVKEH 1377
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlSDLDPASWrrqIAWVPQ-NPYLFAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LEIFAAVRGLRKSHAAVAITRLADALK-LQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:COG4988 431 LRLGRPDASDEELEAALEAAGLDEFVAaLPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1453 QIWQAIRAIIKntDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSK 1506
Cdd:COG4988 511 EILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
478-691 |
3.76e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.14 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NNLsEMADlen 554
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNEL-EPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 555 ilR-IAGVcpqanvqfdF--------LTVRENLRLFAKIRGIPPQDVEKEVQRV--LLELE----MKNIQnilaqnLSGG 619
Cdd:PRK11650 76 --RdIAMV---------FqnyalyphMSVRENMAYGLKIRGMPKAEIEERVAEAarILELEplldRKPRE------LSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 620 QKRKLTFGIAILGDSQIFLLDEPTAGLDpfSRHRVWNLLKERRADRVV----LFSTQFMDEADILADRKVFISNGR 691
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLD--AKLRVQMRLEIQRLHRRLkttsLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1305-1492 |
4.38e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 90.39 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR--EGDTPGFLGYCPQEnalwPNL-----TVKEH 1377
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikAKERRKSIGYVMQD----VDYqlftdSVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LEIfaavrGLRKSHAAVAITR-LADALKLQD-QLKSPvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIW 1455
Cdd:cd03226 93 LLL-----GLKELDAGNEQAEtVLKDLDLYAlKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 254911033 1456 QAIRaIIKNTDRGALLTTHYMAEAEALCDRVAILVSG 1492
Cdd:cd03226 167 ELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1275-1449 |
4.39e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1275 KPVIIASCLRKEYAGKqkhclskkkaKIAtRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllkgsREGD 1354
Cdd:COG0488 313 KKVLELEGLSKSYGDK----------TLL-DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1355 TpGFLGYCPQENA-LWPNLTVKEHLEifAAVRGLRKSHaavAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGN 1433
Cdd:COG0488 377 T-VKIGYFDQHQEeLDPDKTVLDELR--DGAPGGTEQE---VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170
....*....|....*.
gi 254911033 1434 PSILLLDEPSTGLDPE 1449
Cdd:COG0488 451 PNVLLLDEPTNHLDIE 466
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
478-686 |
5.56e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.64 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKpnKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLS-----VPTKGSVTIYNNNLSEMADL 552
Cdd:PRK14258 7 AIKVNNLSFYYDTQ--KI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 553 ENILR--IAGVCPQANVqFDfLTVRENLRLFAKIRGIPPQ-----DVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLT 625
Cdd:PRK14258 83 LNRLRrqVSMVHPKPNL-FP-MSVYDNVAYGVKIVGWRPKleiddIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 626 FGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKER--RADRVVLFSTQFMDEADILADRKVF 686
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAF 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
478-710 |
6.37e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNnnlSEMADLENILR 557
Cdd:PRK11000 3 SVTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 638 LLDEPTAGLDPFSR--HRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGSSLFLkkkwgvgYH 710
Cdd:PRK11000 156 LLDEPLSNLDAALRvqMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
496-648 |
7.20e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 89.34 E-value: 7.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 496 EALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADL--ENILRIA---GVCPQanvqfd 570
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENILYLGhlpGLKPE------ 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 571 fLTVRENLRLFAKIRGIPPQDVEKEVQRVLLelemKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDP 648
Cdd:TIGR01189 88 -LSALENLHFWAAIHGGAQRTIEDALAAVGL----TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1303-1512 |
7.30e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.75 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEHLE 1379
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYqrpINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 IFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 1459
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1460 AIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS----IQHLKSKFGKDYL 1512
Cdd:PRK11607 194 DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
479-697 |
1.11e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.33 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYK-GKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NNLSEMADLEN 554
Cdd:PRK13643 2 IKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 555 ILRIAGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRvllELEMKNIQNILAQN----LSGGQKRKLTFGIA 629
Cdd:PRK13643 82 VRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKspfeLSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 630 ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
479-711 |
1.25e-19 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 89.85 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSeMADLENILRI 558
Cdd:cd03252 1 ITFEHVRFRYK--PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDfLTVRENLRLfakirGIPPQDVEK--EVQRV------LLELEmKNIQNILAQN---LSGGQKRKLTFG 627
Cdd:cd03252 78 VGVVLQENVLFN-RSIRDNIAL-----ADPGMSMERviEAAKLagahdfISELP-EGYDTIVGEQgagLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 628 IAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMdEADILADRKVFISNGRLKCAGSSLFLKKKWGV 707
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
....
gi 254911033 708 GYHL 711
Cdd:cd03252 230 YAYL 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1295-1498 |
1.48e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 90.40 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsreGDTPGF------------LGYC 1362
Cdd:cd03294 31 LKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDG---QDIAAMsrkelrelrrkkISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1363 PQENALWPNLTVKEHLEIFAAVRGLRKshaAVAITRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLL 1439
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPR---AEREERAAEALElvgLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1440 DEPSTGLDP----EGQQQIWQairaIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:cd03294 185 DEAFSALDPlirrEMQDELLR----LQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
495-677 |
1.78e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.19 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 495 IEAlKDLT-------------LDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLsEMADLENILRIaGV 561
Cdd:NF033858 267 IEA-RGLTmrfgdftavdhvsFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIATRRRV-GY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 562 CPQAnvqfdF-----LTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:NF033858 344 MSQA-----FslygeLTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLF-STQFMDEA 677
Cdd:NF033858 419 LILDEPTSGVDPVARDMFWRLLIElSREDGVTIFiSTHFMNEA 461
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
479-697 |
2.56e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.93 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLS----EMADLEN 554
Cdd:PRK09452 15 VELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvpaENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 555 ILriagvcpQANVQFDFLTVRENLRLFAKIRGIPPQDVEKevqRVLLELEMKNIQNiLAQ----NLSGGQKRKLTFGIAI 630
Cdd:PRK09452 91 VF-------QSYALFPHMTVFENVAFGLRMQKTPAAEITP---RVMEALRMVQLEE-FAQrkphQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWNLLK--ERRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
482-693 |
2.57e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 88.72 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 482 RNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM-----ADLENil 556
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakAELRN-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:PRK11629 87 QKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILaDRKVFISNGRLK 693
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1305-1494 |
2.86e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 86.89 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-----REGDTPGFLGYCPQENALWPNlTVKEHLe 1379
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwDPNELGDHVGYLPQDDELFSG-SIAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 ifaavrglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 1459
Cdd:cd03246 97 ------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 254911033 1460 AIIKntdRGA--LLTTHYMaEAEALCDRVAILVSGRL 1494
Cdd:cd03246 141 ALKA---AGAtrIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
475-692 |
3.01e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 87.10 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 475 GKESIRIRNISKEYkgkpnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynnnlsemadlen 554
Cdd:cd03215 1 GEPVLEVRGLSVKG--------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 555 ilriagvcpqANVQFDFLTVRENLRlfAKIRGIPpqdveKEVQRVLLELEMKNIQNI-LAQNLSGGQKRKLTFGIAILGD 633
Cdd:cd03215 60 ----------DGKPVTRRSPRDAIR--AGIAYVP-----EDRKREGLVLDLSVAENIaLSSLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 634 SQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQfMDEADILADRKVFISNGRL 692
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGkaVLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1303-1494 |
3.95e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 90.11 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG---DTKVTAGQVLLKGS-------------REGDtpgfLGYCPQE- 1365
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkiRGRE----IQMIFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1366 -NALWPNLTVKEHL-EIFAAVRGLRKshaAVAITRLADALKLQdQLKSPVKT-------LSEGVKRKLCFVLSILGNPSI 1436
Cdd:COG0444 96 mTSLNPVMTVGDQIaEPLRIHGGLSK---AEARERAIELLERV-GLPDPERRldrypheLSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1437 LLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
497-688 |
4.58e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.07 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 497 ALKDLTLDIYEGQITAVLGHSGAGKSTLL---NILSGL--SVPTKGSVTIYNNNL--SEMADLENILRIAGVCPQANvQF 569
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLipGFRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPN-PF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 570 DfLTVRENLRLFAKIRGIP---PQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGL 646
Cdd:PRK14243 104 P-KSIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254911033 647 DPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFIS 688
Cdd:PRK14243 183 DPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1298-1499 |
5.36e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 88.13 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1298 KKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF-----LGYCPQENALWPNL 1372
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelrrkIGYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHLeifAAVRGLRKSHAAVAITRLADALKLQDQlkSPVK-------TLSEGVKRKLCFVLSILGNPSILLLDEPSTG 1445
Cdd:cd03295 91 TVEENI---ALVPKLLKWPKEKIRERADELLALVGL--DPAEfadryphELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1446 LDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
478-697 |
6.52e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.15 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILR 557
Cdd:PRK11231 2 TLRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAgVCPQANVQFDFLTVRE--------NLRLFAKIRgippQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIA 629
Cdd:PRK11231 78 LA-LLPQHHLTPEGITVRElvaygrspWLSLWGRLS----AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 630 ILGDSQIFLLDEPTAGLDpfSRHRV--WNLLKERRAD-RVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLD--INHQVelMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1305-1494 |
7.84e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.00 E-value: 7.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTP------GfLGYCP---QENALWPNLTV 1374
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvRIRSPrdairaG-IAYVPedrKGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KE-----HLEIFAAVRGLRKSHAAVAITRLADALKL----QDQlksPVKTLSEGVKRKLcfVLS--ILGNPSILLLDEPS 1443
Cdd:COG1129 348 REnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQ---PVGNLSGGNQQKV--VLAkwLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1444 TGLDPEGQQQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG1129 423 RGIDVGAKAEIYRLIREL---AAEGKavIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
478-697 |
8.28e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.20 E-value: 8.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKGKPNKieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdlENILR 557
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--EAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IA-GVCPQaNVQFDFLTVRENLRLfakirGIPPQDVEK--EV-QRVLLElemKNIQNILAQN---------LSGGQKRKL 624
Cdd:PRK11160 414 QAiSVVSQ-RVHLFSATLRDNLLL-----AAPNASDEAliEVlQQVGLE---KLLEDDKGLNawlgeggrqLSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 625 TFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFST-------QFmdeadilaDRKVFISNGRLKCAGS 697
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIThrltgleQF--------DRICVMDNGQIIEQGT 556
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
480-692 |
9.11e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 480 RIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNL---SEMADLEnil 556
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 riAGVC---------PQanvqfdfLTVRENL---RLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKL 624
Cdd:PRK11288 79 --AGVAiiyqelhlvPE-------MTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 625 TFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD-RVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1303-1494 |
9.46e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 86.69 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG--------FLGYCPQENALWPNLTV 1374
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylrrKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEHLEIfaAVRGLRKSHAAVAiTRLADALKLQDqLKSPVKT----LSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEg 1450
Cdd:cd03292 96 YENVAF--ALEVTGVPPREIR-KRVPAALELVG-LSHKHRAlpaeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1451 qqQIWQAIRAIIKNTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03292 171 --TTWEIMNLLKKINKAGTtvVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1303-1499 |
1.03e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 87.39 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEHLE 1379
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQernVGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 IFAAVRGLRKSHAAVAITRLADAL-------KLQDQLKSpvkTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYPA---QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254911033 1453 QIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1303-1461 |
1.10e-18 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 85.55 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREG---------------DTPGFLGYC 1362
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepldySRKGllerrqrvglvfqdpDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1363 PQENALWP-NLTVKEHlEIFAAVRGlrkshaavAITrladALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDE 1441
Cdd:TIGR01166 87 DQDVAFGPlNLGLSEA-EVERRVRE--------ALT----AVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180
....*....|....*....|
gi 254911033 1442 PSTGLDPEGQQQIWQAIRAI 1461
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRL 173
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
479-667 |
1.14e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 84.96 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNnnlsemADLEnilri 558
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG------ADIS----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 agvcpqanvQFDFLTVRENLrlfakirGIPPQDVEkevqrvLLElemkniqNILAQN-LSGGQKRKLTFGIAILGDSQIF 637
Cdd:cd03246 68 ---------QWDPNELGDHV-------GYLPQDDE------LFS-------GSIAENiLSGGQRQRLGLARALYGNPRIL 118
|
170 180 190
....*....|....*....|....*....|...
gi 254911033 638 LLDEPTAGLDPFSRHRVWNL---LKERRADRVV 667
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAiaaLKAAGATRIV 151
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
479-677 |
1.22e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVtIYNNNLSEMADLENILRI 558
Cdd:PRK13648 8 IVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQ--------ANVQFDFLTVRENlrlfakiRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTF-GIA 629
Cdd:PRK13648 85 IGIVFQnpdnqfvgSIVKYDVAFGLEN-------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIaGVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 630 ILGDSQIfLLDEPTAGLDPFSRHRVWNLLKERRADR-VVLFS-TQFMDEA 677
Cdd:PRK13648 158 ALNPSVI-ILDEATSMLDPDARQNLLDLVRKVKSEHnITIISiTHDLSEA 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
502-692 |
1.42e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.56 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 502 TLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEnilRIAGVCPQANVQFDFLTVREN---- 577
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR---RPVSMLFQENNLFSHLTVAQNiglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 578 ----LRLFAKIRgippQDVEKEVQRVLLElemkNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHR 653
Cdd:PRK10771 96 lnpgLKLNAAQR----EKLHAIARQMGIE----DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 654 VWNLLKERRADR--VVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK10771 168 MLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-692 |
1.73e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.82 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 496 EALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL-----SVPTKGSVTIYNNNL-SEMADLENILRIAGVCPQANVQF 569
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIySPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 570 DFLTVRENLRLFAKIRGIP------PQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPT 643
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVkskkelDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 644 AGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1303-1540 |
1.74e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.11 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQV-LLKGS------REGDTPGfLGYCPQ---ENaLWPNL 1372
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDmadarhRRAVCPR-IAYMPQglgKN-LYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:NF033858 94 SVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1453 QIWQAIRAIikNTDRGA---LLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDyllemkvkTLEQVeplnte 1529
Cdd:NF033858 174 QFWELIDRI--RAERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGAD--------TLEAA------ 236
|
250
....*....|.
gi 254911033 1530 ILRLFPQASRQ 1540
Cdd:NF033858 237 FIALLPEEKRR 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1303-1494 |
2.05e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGFLG------YcpQENALWPNLTV 1374
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemRFASTTAALAagvaiiY--QELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEHLEI--FAAVRGLRKSHAAVAITRLA-DALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 1451
Cdd:PRK11288 97 AENLYLgqLPHKGGIVNRRLLNYEAREQlEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 1452 QQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK11288 177 EQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1283-1494 |
2.25e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 85.70 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLK----MISGDTKV-TAGQVLLKGSREGDtpg 1357
Cdd:cd03260 6 LNVYYGDKH-----------ALKDISLDIPKGEITALIGPSGCGKSTLLRllnrLNDLIPGApDEGEVLLDGKDIYD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1358 flgycPQENALW-----------PNL---TVKEHLEIFAAVRGLRKSHAAVAITRlaDALK---LQDQLKSPVK--TLSE 1418
Cdd:cd03260 72 -----LDVDVLElrrrvgmvfqkPNPfpgSIYDNVAYGLRLHGIKLKEELDERVE--EALRkaaLWDEVKDRLHalGLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1419 GVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
481-662 |
2.31e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.32 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM-ADLENILRIA 559
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 --GVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:PRK10535 87 hfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180
....*....|....*....|....*
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKERR 662
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLR 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1303-1508 |
2.35e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 88.64 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSlkmisgdtkvtAGQVLLKGSREGDTP-GFLGYCPQENALW------------ 1369
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-----------ALPAHV*GPDAGRRPwRF*TWCANRRALRrtig*hrpvr*g 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 --PNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 1447
Cdd:NF000106 97 rrESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1448 PEGQQQIWQAIRAIIKNtdrGA--LLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFG 1508
Cdd:NF000106 177 PRTRNEVWDEVRSMVRD---GAtvLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1305-1447 |
2.77e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLL-KGSRegdtpgfLGYCPQENALWPNLTVKE-----HL 1378
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLR-------IGYLPQEPPLDDDLTVLDtvldgDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 EIFAAVRGLRKSHAAVA---------------------------ITRLADALKL-QDQLKSPVKTLSEGVKRK--LCFVL 1428
Cdd:COG0488 88 ELRALEAELEELEAKLAepdedlerlaelqeefealggweaearAEEILSGLGFpEEDLDRPVSELSGGWRRRvaLARAL 167
|
170
....*....|....*....
gi 254911033 1429 siLGNPSILLLDEPSTGLD 1447
Cdd:COG0488 168 --LSEPDLLLLDEPTNHLD 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
456-693 |
4.78e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 456 IDPVPSSGD---SFEPvsPEFHGKESIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLS 532
Cdd:COG0488 292 EEPPRRDKTveiRFPP--PERLGKKVLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 533 VPTKGSVTIYNNnlsemadleniLRIaGVCPQANVQFDF-LTVRENLRLFA------KIRGI------PPQDVEKEVQRv 599
Cdd:COG0488 366 EPDSGTVKLGET-----------VKI-GYFDQHQEELDPdKTVLDELRDGApggteqEVRGYlgrflfSGDDAFKPVGV- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 600 llelemkniqnilaqnLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKErrADRVVLFST---QFMDE 676
Cdd:COG0488 433 ----------------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD--FPGTVLLVShdrYFLDR 494
|
250
....*....|....*..
gi 254911033 677 adiLADRKVFISNGRLK 693
Cdd:COG0488 495 ---VATRILEFEDGGVR 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
479-731 |
4.82e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.48 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLS--VPTKGSVtIYNNNLSEMAD-LENI 555
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IYHVALCEKCGyVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRIAGVCPQ-----ANVQFDFL----TVRENL---------RLFA----------KIRGIPPQDVE--KEVQRVLLELEM 605
Cdd:TIGR03269 76 SKVGEPCPVcggtlEPEEVDFWnlsdKLRRRIrkriaimlqRTFAlygddtvldnVLEALEEIGYEgkEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 606 KNIQNI---LAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADIL 680
Cdd:TIGR03269 156 VQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 681 ADRKVFISNGRLKCAGSSLFLKKKWGVGYHLSLQLKEVCVPENITSL--VKQH 731
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVrnVSKR 288
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
479-710 |
5.18e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 84.97 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgkPNKiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRI 558
Cdd:cd03253 1 IEFENVTFAYD--PGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-TLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDfLTVRENLRlFAKIrGIPPQDVEKEVQRVLLELEMKNI----QNILAQN---LSGGQKRKLTFGIAIL 631
Cdd:cd03253 77 IGVVPQDTVLFN-DTIGYNIR-YGRP-DATDEEVIEAAKAAQIHDKIMRFpdgyDTIVGERglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 632 GDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLF-----STqFMDeadilADRKVFISNGRLKCAGSSLFLKKKWG 706
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIViahrlST-IVN-----ADKIIVLKDGRIVERGTHEELLAKGG 227
|
....
gi 254911033 707 VgYH 710
Cdd:cd03253 228 L-YA 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
479-683 |
6.21e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMA-DLENILR 557
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVcPQANVQFDFLTVRENLrLFakirGIP-PQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:PRK15439 88 IYLV-PQEPLLFPNLSVKENI-LF----GLPkRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADR 683
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADR 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
479-692 |
6.30e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.29 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEY-KGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVT-IYNN-------NLSEM 549
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwIFKDeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 550 ADLENILR---------IAGVCPQANVQFDFL-------TVRENLRLFAKIRGIPPQDVEKevqRVLLELEMKNI-QNIL 612
Cdd:PRK13651 83 VLEKLVIQktrfkkikkIKEIRRRVGVVFQFAeyqlfeqTIEKDIIFGPVSMGVSKEEAKK---RAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 613 AQ---NLSGGQKRKltfgIAILG----DSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRK 684
Cdd:PRK13651 160 QRspfELSGGQKRR----VALAGilamEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRT 235
|
....*...
gi 254911033 685 VFISNGRL 692
Cdd:PRK13651 236 IFFKDGKI 243
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
513-698 |
6.37e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 86.78 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 513 VLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLeniLRIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDV 592
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH---LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 593 EkevQRVLLELEMKNIQNILAQ---NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLK--ERRADRVV 667
Cdd:TIGR01187 78 K---PRVLEALRLVQLEEFADRkphQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|.
gi 254911033 668 LFSTQFMDEADILADRKVFISNGRLKCAGSS 698
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
497-697 |
7.36e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.78 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 497 ALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLE----NILRIAGVCpQANVQFDFL 572
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVF-QSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 573 TVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRH 652
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254911033 653 RVWNLLKERRA--DRVVLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK10070 202 EMQDELVKLQAkhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
479-692 |
7.48e-18 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 84.41 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRI 558
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGvcpqANVQFDF--------LTVRENLRLFAKIRGIP-PQDV-EKEVQRVLLElemKNIQNILAQnLSGG-QKRkltfg 627
Cdd:COG4181 88 RA----RHVGFVFqsfqllptLTALENVMLPLELAGRRdARARaRALLERVGLG---HRLDHYPAQ-LSGGeQQR----- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 628 IAI----LGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR---VVLFSTqfmDEAdiLA---DRKVFISNGRL 692
Cdd:COG4181 155 VALarafATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgttLVLVTH---DPA--LAarcDRVLRLRAGRL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
479-692 |
8.04e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.76 E-value: 8.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIynNNLS---EMADLENI 555
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV--DGLKvndPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRIAGVCPQANVQFDFLTVRENLrLFA--KIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGD 633
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 634 SQIFLLDEPTAGLDPFSRH---RVWNLLKERRADRVVLfsTQFMDEADILADRKVFISNGRL 692
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHevlKVMQDLAEEGMTMVIV--THEIGFAEKVASRLIFIDKGRI 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
479-691 |
8.08e-18 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 83.67 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIE-ALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNnnlsemadlenilR 557
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANVQFDflTVRENLrLFAKirgipPQDvEKEVQRVL----LELEMKniqnILAQ-----------NLSGGQKR 622
Cdd:cd03250 68 IAYVSQEPWIQNG--TIRENI-LFGK-----PFD-EERYEKVIkacaLEPDLE----ILPDgdlteigekgiNLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 623 KLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWN--LLKERRADRVVLFST---QFMDEadilADRKVFISNGR 691
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVThqlQLLPH----ADQIVVLDNGR 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1307-1498 |
8.42e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 8.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPG-FLGYCPQENALWPNLTVKE----- 1376
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddveALSARAASrRVASVPQDTSLSFEFDVRQvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 ---HLEIFAAV-----RGLRKSHAAVAITRLADalklqdqlkSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 1448
Cdd:PRK09536 102 rtpHRSRFDTWtetdrAAVERAMERTGVAQFAD---------RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1449 EGQQQIWQAIRAIIkNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:PRK09536 173 NHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
481-692 |
9.70e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.73 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVtiynnnlsemadlenilrIAG 560
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------------LAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 561 VCPQANvqfdfltVRENLRL-FAKIRGIPPQDV------------EKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFG 627
Cdd:PRK11247 73 TAPLAE-------AREDTRLmFQDARLLPWKKVidnvglglkgqwRDAALQALAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 628 IAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1308-1503 |
1.13e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.04 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1308 SFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPgflgycP---------QENALWPNLTVKEHL 1378
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP------PaerpvsmlfQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 EIfaAVR-GLRKShaAVAITRLADALK---LQDQLKSPVKTLSEGVKRKL----CFVlsiLGNPsILLLDEPSTGLDPEG 1450
Cdd:COG3840 93 GL--GLRpGLKLT--AEQRAQVEQALErvgLAGLLDRLPGQLSGGQRQRValarCLV---RKRP-ILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1451 QQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:COG3840 165 RQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1305-1474 |
1.23e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.93 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTPG----FLGYcpqENALWPNLTVKEH 1377
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepiRRQRDEYHqdllYLGH---QPGIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LEIFAAVRGLrkSHAAVAITRLAdALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIwqa 1457
Cdd:PRK13538 95 LRFYQRLHGP--GDDEALWEALA-QVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL--- 168
|
170
....*....|....*....
gi 254911033 1458 IRAIIKNTDRG--ALLTTH 1474
Cdd:PRK13538 169 EALLAQHAEQGgmVILTTH 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
479-732 |
1.51e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmADLENILRI 558
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIR-GIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGS--SLFLKKKWGVGYHLSL 713
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQPDLLARVHLDL 239
|
250
....*....|....*....
gi 254911033 714 QLkevcVPENITSLVKQHI 732
Cdd:PRK13652 240 PS----LPKLIRSLQAQGI 254
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1275-1499 |
1.78e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.15 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1275 KPVIIASCLRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGD 1354
Cdd:PRK09452 12 SPLVELRGISKSFDGKE-----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1355 TPG--------FLGYcpqenALWPNLTVKEHLEIfaavrGLR--KSHAAVAITRLADALK---LQDQLKSPVKTLSEGVK 1421
Cdd:PRK09452 81 VPAenrhvntvFQSY-----ALFPHMTVFENVAF-----GLRmqKTPAAEITPRVMEALRmvqLEEFAQRKPHQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1422 RKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
475-697 |
2.34e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.90 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 475 GKESIRIRNISKEYKGK-PNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVT---IYNN------ 544
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdIYIGdkknnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 545 ------NLSEMADLENILRIAGVCPQANVQFDFLTVRENLRLFAKIR-GIPPQDVEKEVQRVLLELEMKniQNILAQN-- 615
Cdd:PRK13631 98 elitnpYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVAlGVKKSEAKKLAKFYLNKMGLD--DSYLERSpf 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 616 -LSGGQKRKltfgIAILG----DSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD-RVVLFSTQFMDEADILADRKVFISN 689
Cdd:PRK13631 176 gLSGGQKRR----VAIAGilaiQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDK 251
|
....*...
gi 254911033 690 GRLKCAGS 697
Cdd:PRK13631 252 GKILKTGT 259
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1306-1474 |
2.55e-17 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 81.91 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSREGDT-PGFLGYCPQENALWPNLTVKEHLEIFA 1382
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNfQRSTGYVEQQDVHSPNLTVREALRFSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1383 AVRGLRKSHAavaitrladalklqdqlkspvKTLSEGVKrklcfvlsILGNPSILLLDEPSTGLDPEGQQQIWQAIRAII 1462
Cdd:cd03232 105 LLRGLSVEQR---------------------KRLTIGVE--------LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
170
....*....|..
gi 254911033 1463 kNTDRGALLTTH 1474
Cdd:cd03232 156 -DSGQAILCTIH 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1311-1486 |
2.89e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 83.23 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1311 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsrEGDTpgfLGYCPQEnalwpnLTVKEHLEIFAAVRGLRKS 1390
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI----ELDT---VSYKPQY------IKADYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1391 HAAVA--ITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRG 1468
Cdd:cd03237 89 FYTHPyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKT 168
|
170
....*....|....*...
gi 254911033 1469 ALLTTHYMAEAEALCDRV 1486
Cdd:cd03237 169 AFVVEHDIIMIDYLADRL 186
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
479-691 |
3.03e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 82.48 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYK-----GKpnKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTI-YNNNLSEMADL 552
Cdd:COG4778 5 LEVENLSKTFTlhlqgGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 553 EN--ILRI----AGVCPQanvqfdFLTVR----------ENLRLfakiRGIPPQDVEKEVQRVLLELEmkniqniLAQNL 616
Cdd:COG4778 83 SPreILALrrrtIGYVSQ------FLRVIprvsaldvvaEPLLE----RGVDREEARARARELLARLN-------LPERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 617 --------SGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTqFMDEA--DILADRKVF 686
Cdd:COG4778 146 wdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADRVVD 224
|
....*
gi 254911033 687 ISNGR 691
Cdd:COG4778 225 VTPFS 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1300-1494 |
3.45e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 82.73 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG--------FLGYCPQENALWPN 1371
Cdd:TIGR02315 14 GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklrklrrRIGMIFQHYNLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKEHLEI--FAAVRGLR-------KSHAAVAITRLaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEP 1442
Cdd:TIGR02315 94 LTVLENVLHgrLGYKPTWRsllgrfsEEDKERALSAL-ERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1443 STGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:TIGR02315 173 IASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
479-692 |
3.79e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTI------YNNNLSEMADL 552
Cdd:PRK11264 4 IEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 553 ENILRI-AGVCPQANVQFDFLTVRENLRLFAKI-RGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAI 630
Cdd:PRK11264 80 IRQLRQhVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWN----LLKERRADRVVlfsTQFMDEADILADRKVFISNGRL 692
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNtirqLAQEKRTMVIV---THEMSFARDVADRAIFMDQGRI 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1275-1492 |
3.90e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1275 KPVIIASCLRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGD 1354
Cdd:PRK15439 9 PPLLCARSISKQYSGVE-----------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1355 -TPGF---LG-Y-CPQENALWPNLTVKEHLeIFaavrGLRKSHAAVA-ITRLADALKLQDQLKSPVKTLsEGVKRKLCFV 1427
Cdd:PRK15439 78 lTPAKahqLGiYlVPQEPLLFPNLSVKENI-LF----GLPKRQASMQkMKQLLAALGCQLDLDSSAGSL-EVADRQIVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1428 L-SILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSG 1492
Cdd:PRK15439 152 LrGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-692 |
4.33e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.65 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL-----SVPTKGSV-----TIYNNNLSE 548
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVyldgqDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 549 MAD-LENILRIAGVCPQANVqFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFG 627
Cdd:PRK14247 80 LRRrVQMVFQIPNPIPNLSI-FENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 628 IAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
475-698 |
4.59e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.79 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 475 GKESIRIRNISKEYKGKPNKiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL------SVPTKGSVTIYNNNLSE 548
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 549 MaDLENILRIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQD-----VEKEVQRVLLELEMKNIQNILAQNLSGGQKRK 623
Cdd:PRK14246 83 I-DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 624 LTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGSS 698
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1297-1513 |
5.17e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 82.15 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1297 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDT-PGFL----GYCPQENALWpN 1371
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLrrqvGVVLQENVLF-N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKEHLeifAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKT--------LSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:cd03252 90 RSIRDNI---ALADPGMSMERVIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1444 TGLDPEGQQQIWQAIRAIIKNtdRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDYLL 1513
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
476-697 |
5.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.24 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 476 KESIRIRNISKEYKGKPNKIEaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmadlENI 555
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE----ENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 L----RIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAIL 631
Cdd:PRK13650 77 WdirhKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 632 GDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQFMDEAdILADRKVFISNGRLKCAGS 697
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1311-1494 |
5.95e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 81.39 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1311 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREGDTPGFLGYcpQENALWPNLTVKEHLEIfAAVR 1385
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaAPPADRPVSMLF--QENNLFAHLTVEQNVGL-GLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1386 GLR-KSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKN 1464
Cdd:cd03298 98 GLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|
gi 254911033 1465 TDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1300-1500 |
7.24e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENAL---WPNL---- 1372
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLvfqYPEYqlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 -TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQL---KSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 1448
Cdd:PRK13637 99 eTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1449 EGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSI 1500
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
479-668 |
7.60e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.92 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSE--MADLENil 556
Cdd:TIGR02203 331 VEFRNVTFRYPGR--DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRR-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVcPQANVQFDFlTVRENLRLfakirGIPPQDVEKEVQRVLlelEMKNIQNILAQ--------------NLSGGQKR 622
Cdd:TIGR02203 407 QVALV-SQDVVLFND-TIANNIAY-----GRTEQADRAEIERAL---AAAYAQDFVDKlplgldtpigengvLLSGGQRQ 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 623 KLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVL 668
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTL 522
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1293-1493 |
7.97e-17 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 81.85 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1293 HCLSK--KKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF--------LGYC 1362
Cdd:cd03256 4 ENLSKtyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1363 PQENALWPNLTVKE--------HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNP 1434
Cdd:cd03256 84 FQQFNLIERLSVLEnvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 1435 SILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1305-1494 |
9.13e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 80.65 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFL-------GYCPQENALWPNLTVKEH 1377
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrqkvGMVFQQFNLFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LeIFA--AVRGLRKShAAVAITRlaDALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:cd03262 97 I-TLApiKVKGMSKA-EAEERAL--ELLEkvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254911033 1453 QIWQAIRAIIKnTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:cd03262 173 EVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1305-1501 |
9.37e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.09 E-value: 9.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-----FLGYCPQENALWPNLTVKEHLE 1379
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelarRRAVLPQHSSLAFPFTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 IFAAVRGLRKSHAAVAITR---LADALKLQDQLkspVKTLSEGVK------RKLCFVL-SILGNPSILLLDEPSTGLDPE 1449
Cdd:COG4559 98 LGRAPHGSSAAQDRQIVREalaLVGLAHLAGRS---YQTLSGGEQqrvqlaRVLAQLWePVDGGPRWLFLDEPTSALDLA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1450 GQQQIWQAIRAIiknTDRGA--------L-LTTHYmaeaealCDRVAILVSGRLRCIGSIQ 1501
Cdd:COG4559 175 HQHAVLRLARQL---ARRGGgvvavlhdLnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
479-665 |
9.43e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 83.18 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL---SVPTKGSVTIYNNNLSEM--ADLE 553
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLseKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NIL--RIAGVcPQanvqfD-------FLTVR----ENLRLFakiRGIPPQDVEKEVQRVLLELEMKNIQNILAQ---NLS 617
Cdd:COG0444 82 KIRgrEIQMI-FQ-----DpmtslnpVMTVGdqiaEPLRIH---GGLSKAEARERAIELLERVGLPDPERRLDRyphELS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254911033 618 GGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR 665
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQREL 200
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
498-706 |
1.46e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.00 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDI-----YEGqITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENI----LRIAGVCPQANVq 568
Cdd:PRK11144 10 LGDLCLTVnltlpAQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppekRRIGYVFQDARL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 569 FDFLTVRENLRLfakirGIPPQDVEKEVQRVLLeLEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDP 648
Cdd:PRK11144 88 FPHYKVRGNLRY-----GMAKSMVAQFDKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 649 FSRHRVWNLLkERRADRV---VLFSTQFMDEADILADRKVFISNGRLKCAGSslfLKKKWG 706
Cdd:PRK11144 162 PRKRELLPYL-ERLAREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1307-1474 |
1.48e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 79.84 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLG----YCPQENALWPNLTVKEHLEIFA 1382
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1383 AVrglrksHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAii 1462
Cdd:cd03231 99 AD------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-- 170
|
170
....*....|....
gi 254911033 1463 kNTDRG--ALLTTH 1474
Cdd:cd03231 171 -HCARGgmVVLTTH 183
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1284-1509 |
1.59e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1284 RKEYAGKQKHCLSKKKA-KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMIS----GDTKVtAGQVLLKGSREgDTPGF 1358
Cdd:TIGR00955 20 WKQLVSRLRGCFCRERPrKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspKGVKG-SGSVLLNGMPI-DAKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1359 ---LGYCPQENALWPNLTVKEHLEIFAAVR---GLRKSHAAVAITRLADALKLQD------QLKSPVKTLSEGVKRKLCF 1426
Cdd:TIGR00955 98 raiSAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1427 VLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHY-MAEAEALCDRVAILVSGRLRCIGSIQHLKS 1505
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
....
gi 254911033 1506 KFGK 1509
Cdd:TIGR00955 257 FFSD 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
481-647 |
1.81e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNnlsemadleniLRIAG 560
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 561 VcPQANVQFDFLTVRENL--------RLFAKIRGI-----PPQDVEKEVQRVLLELEMKN-------IQNILAQ------ 614
Cdd:COG0488 66 L-PQEPPLDDDLTVLDTVldgdaelrALEAELEELeaklaEPDEDLERLAELQEEFEALGgweaearAEEILSGlgfpee 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 615 -------NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:COG0488 145 dldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
479-691 |
1.97e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 77.87 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNnlsemadleniLRI 558
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AgvcpqanvqfdfltvrenlrlfakirgippqdvekevqrvllelemkniqnILAQnLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03221 66 G---------------------------------------------------YFEQ-LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 639 LDEPTAGLDPFSRHRVWNLLKERRadRVVLFST---QFMDEadiLADRKVFISNGR 691
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYP--GTVILVShdrYFLDQ---VATKIIELEDGK 144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
479-683 |
2.03e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNlsemadleniLRI 558
Cdd:COG3845 6 LELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP----------VRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGvcPQANVQ------------FDFLTVRENLRLFAKIRG---IPPQDVEKEVQRVL----LELEMkniqNILAQNLSGG 619
Cdd:COG3845 72 RS--PRDAIAlgigmvhqhfmlVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSerygLDVDP----DAKVEDLSVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 620 QKRKLTfgI--AILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD-RVVLFSTQFMDEADILADR 683
Cdd:COG3845 146 EQQRVE--IlkALYRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADR 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
474-692 |
5.47e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 79.05 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 474 HGKESIRIRNISKEYKGKPNKiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSeMADLE 553
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NILRIAGVCPQANVQFDfLTVRENLRLfaKIRGIPPQDVEKEVQRV-------LLELEMKNIQNILAQNLSGGQKRKLTF 626
Cdd:cd03248 85 YLHSKVSLVGQEPVLFA-RSLQDNIAY--GLQSCSFECVKEAAQKAhahsfisELASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 627 GIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADiLADRKVFISNGRL 692
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
496-670 |
6.11e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.05 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 496 EALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNL--SEMADLENILRIAGVCPQANVQFDFLT 573
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 574 VRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHR 653
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170
....*....|....*....
gi 254911033 654 VWNLLKE--RRADRVVLFS 670
Cdd:PRK13638 175 MIAIIRRivAQGNHVIISS 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
500-647 |
6.77e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.92 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 500 DLTLDiyEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADL--ENILRIAgvcpQANVQFDFLTVREN 577
Cdd:cd03231 20 SFTLA--AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYLG----HAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 578 LRLFAKIRGippqdvEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:cd03231 94 LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
479-697 |
6.84e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.05 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGK-PNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYN----NNLSEMADLE 553
Cdd:PRK13645 7 IILDNVSYTYAKKtPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NILRIAGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEM-KNIQNILAQNLSGGQKRKLTFGIAIL 631
Cdd:PRK13645 87 RLRKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 632 GDSQIFLLDEPTAGLDPFSRHRVWNL---LKERRADRVVLFsTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRIIMV-THNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1301-1506 |
7.01e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.65 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREG--DTPGFLGYCPQEnalwPN---- 1371
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiSKENlkEIRKKIGIIFQN----PDnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 -LTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCfVLSILG-NPSILLLDEPSTGLDPE 1449
Cdd:PRK13632 98 gATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA-IASVLAlNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1450 GQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQH-LKSK 1506
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
475-706 |
7.35e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.93 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 475 GKESIRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAG--KSTLLNILSGlsvPTKGSVTIynNNLSEMADL 552
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 553 ENILRIAGVC-PQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAIL 631
Cdd:NF000106 81 RALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 632 GDSQIFLLDEPTAGLDPFSRHRVWNLLKER-RADRVVLFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKWG 706
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
286-647 |
7.77e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 83.62 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 286 VIKSVQFFILTSFMVVF----SLFLLYGLSMITLAFLMSALVR---------KSVLTGLSVFLLTIFWGSlGFTSLYRYL 352
Cdd:TIGR00956 509 IIESVVFNIILYFMVNFrrtaGRFFFYLLILFICTLAMSHLFRsigavtktlSEAMTPAAILLLALSIYT-GFAIPRPSM 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 353 PAPVEWtLSLFSPFAFT---LGMAQLLRVDYDLNSNAPPDPAS-----------------GSNLIIATNFM--------- 403
Cdd:TIGR00956 588 LGWSKW-IYYVNPLAYAfesLMVNEFHGRRFECSQYVPSGGGYdnlgvtnkvctvvgaepGQDYVDGDDYLklsfqyyns 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 404 ------------LVFDAFLYLALMMYFEkvlPNEygHQHSPLFFLKSSfwLQTRKPAHVILED-GIDPVPSSGDSFEPVS 470
Cdd:TIGR00956 667 hkwrnfgiiigfTVFFFFVYILLTEFNK---GAK--QKGEILVFRRGS--LKRAKKAGETSASnKNDIEAGEVLGSTDLT 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 471 PEFH------------GKESIRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSG---LSVPT 535
Cdd:TIGR00956 740 DESDdvndekdmekesGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVIT 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 536 KGSVTIYNNNLSemadlENILRIAGVCPQANVQFDFLTVRENLRLFAKIRgiPPQDVEKE-----VQRVLLELEMKNIQN 610
Cdd:TIGR00956 820 GGDRLVNGRPLD-----SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLR--QPKSVSKSekmeyVEEVIKLLEMESYAD 892
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 254911033 611 IL----AQNLSGGQKRKLTFGIAILGDSQIFL-LDEPTAGLD 647
Cdd:TIGR00956 893 AVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
496-659 |
8.07e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 83.25 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 496 EALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRIAGVCPQANVQFDFlTVR 575
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHTLRQFINYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 576 ENLRLFAKiRGIPPQDVEKEVQRVLLELEMKNIQ-------NILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDP 648
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPlgyqtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170
....*....|..
gi 254911033 649 FSRHR-VWNLLK 659
Cdd:TIGR01193 645 ITEKKiVNNLLN 656
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1292-1498 |
9.27e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1292 KHCLSKKKAKI-ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsREGD------TPGF------ 1358
Cdd:TIGR03269 287 KRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDewvdmtKPGPdgrgra 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1359 ---LGYCPQENALWPNLTVKEHLEIFAAVR-----GLRKshaAVAITRLA--DALKLQDQLKSPVKTLSEGVKRKLCFVL 1428
Cdd:TIGR03269 364 kryIGILHQEYDLYPHRTVLDNLTEAIGLElpdelARMK---AVITLKMVgfDEEKAEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1429 SILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1305-1499 |
1.11e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.52 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsreGDTP----------GFLGYCPQENALWpNLTV 1374
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-----DGVDirdltleslrRQIGVVPQDTFLF-SGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEHL----------EIFAAvrgLRKSHAAVAITRLAdalklqDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLD 1440
Cdd:COG1132 431 RENIrygrpdatdeEVEEA---AKAAQAHEFIEALP------DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 1441 EPSTGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGS 1499
Cdd:COG1132 502 EATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
479-700 |
1.19e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.98 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmADLENILRI 558
Cdd:PRK13642 5 LEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQ-ANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIF 637
Cdd:PRK13642 83 IGMVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 638 LLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEAdILADRKVFISNGRL--KCAGSSLF 700
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEikEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1303-1489 |
1.38e-15 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 81.95 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsreGDTPGF--------LGYCPQENALWPNlTV 1374
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG---VPLADAdadswrdqIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEHLEIF---AAVRGLRKSHAAVAITRLADALK--LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:TIGR02857 413 AENIRLArpdASDAEIREALERAGLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1450 GQQQIWQAIRAIIKNtdRGALLTTHYMAEAEaLCDRVAIL 1489
Cdd:TIGR02857 493 TEAEVLEALRALAQG--RTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1309-1474 |
1.38e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 77.58 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1309 FCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG--SREGDTPGFLGYCPQENALWPNLTVKEHLEIFAAVRG 1386
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1387 LRKSH---AAVAITRLADalkLQDQLkspVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIK 1463
Cdd:PRK13543 112 RRAKQmpgSALAIVGLAG---YEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLR 185
|
170
....*....|.
gi 254911033 1464 nTDRGALLTTH 1474
Cdd:PRK13543 186 -GGGAALVTTH 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
475-692 |
1.43e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.77 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 475 GKESIRIRNISKEY----KGKpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTI-YNNNLSEM 549
Cdd:TIGR03269 276 GEPIIKVRNVSKRYisvdRGV---VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 550 ADLENILR-----IAGVCPQANVQFDFLTVRENLrlfAKIRGIPPQDvEKEVQRVLLELEM--------KNIQNILAQNL 616
Cdd:TIGR03269 353 TKPGPDGRgrakrYIGILHQEYDLYPHRTVLDNL---TEAIGLELPD-ELARMKAVITLKMvgfdeekaEEILDKYPDEL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 617 SGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWN-LLKERRA-DRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1305-1499 |
1.57e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.80 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSREGDTPgflgycPQENALwpnltvkehLEIFA 1382
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLP------PEERAR---------LGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1383 AvrglrkSHAAVAITrladALKLQDQLKSPVKTLSEGvKRKLCFVLSILG-NPSILLLDEPSTGLDPEGQQQIWQAIRAi 1461
Cdd:cd03217 82 A------FQYPPEIP----GVKNADFLRYVNEGFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLDIDALRLVAEVINK- 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 254911033 1462 IKNTDRGALLTTHYMAEAEAL-CDRVAILVSGRLRCIGS 1499
Cdd:cd03217 150 LREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1283-1494 |
2.86e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.97 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYAgkqkhclSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------SREgdt 1355
Cdd:COG1135 7 LSKTFP-------TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalsERE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1356 pgfL-------GYCPQENALWPNLTVKEH----LEIfaavRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVK--- 1421
Cdd:COG1135 77 ---LraarrkiGMIFQHFNLLSSRTVAENvalpLEI----AGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKqrv 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1422 ---RKLCfvlsilGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG1135 150 giaRALA------NNPKVLLCDEATSALDPETTRSILDLLKDI--NRELGLtiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
482-647 |
4.53e-15 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 75.76 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 482 RNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPT---KGSVTIYNNNLSEMAdlENILRI 558
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA--EKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFLTVRENLRLFAKIRGippqdveKEVQRVllelemkniqnilaqnLSGGQKRKLTFGIAILGDSQIFL 638
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG-------NEFVRG----------------ISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 254911033 639 LDEPTAGLD 647
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1304-1498 |
4.64e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1304 TRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEHLEI 1380
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1381 FAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 1460
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 254911033 1461 IIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:PRK11000 179 LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1494 |
5.41e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.04 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS------------REgdTPGFLGYCPQENALWP 1370
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevRK--TVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 nlTVKEHLEIFAAVRGLRKSHAAvaiTRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 1447
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVE---KRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 1448 PEGQQQIwqaIRAIIKNTDRG--ALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK13639 170 PMGASQI---MKLLYDLNKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1305-1494 |
5.57e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.66 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTS----LKMISGDTKVTAGQVLLKGSR--EGDTPGFLGYCPQEN---ALWPNLTVK 1375
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPvaPCALRGRKIATIMQNprsAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EH-LEIFAAVRGLRKSHAAVAITR---LADALKLqdqLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 1451
Cdd:PRK10418 100 THaRETCLALGKPADDATLTAALEavgLENAARV---LKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 1452 QQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1306-1494 |
5.59e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.20 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKM-------------ISGD-----TKVTAGQV-LLKGSregdtpgfLGYCPQEN 1366
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVlnlletpdsgqlnIAGHqfdfsQKPSEKAIrLLRQK--------VGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1367 ALWPNLTVKEHLeIFAAVR--GLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 1444
Cdd:COG4161 92 NLWPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1445 GLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG4161 171 ALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1306-1492 |
6.14e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllkgsrEGDTPGFLGYCPQENALWPN--LTVKEhleiFAA 1383
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYLDTTlpLTVNR----FLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1384 VR-GLRKSHAAVAITRLaDALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAII 1462
Cdd:PRK09544 92 LRpGTKKEDILPALKRV-QAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
170 180 190
....*....|....*....|....*....|....*
gi 254911033 1463 KNTDRGALLTTH----YMAEA-EALCDRVAILVSG 1492
Cdd:PRK09544 168 RELDCAVLMVSHdlhlVMAKTdEVLCLNHHICCSG 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1297-1494 |
6.50e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.05 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1297 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDT------PGFLGYCP---- 1363
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLwdirnkAGMVFQNPdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1364 ------QENALWP-NLTVkEHLEIfaavrglRKshaavaitRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGN 1433
Cdd:PRK13633 99 vativeEDVAFGPeNLGI-PPEEI-------RE--------RVDESLKkvgMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1434 PSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRL 1494
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1302-1493 |
8.49e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1302 IATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF----LGYCP--QENALWPNLTVK 1375
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiarMGVVRtfQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 E--------HLE--IFA---AVRGLRKSHAAvAITRLA---DALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLL 1439
Cdd:PRK11300 99 EnllvaqhqQLKtgLFSgllKTPAFRRAESE-ALDRAAtwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1440 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1303-1501 |
9.44e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsREGD--TPGF-----LGYCPQENALWPNLTVK 1375
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-INYNklDHKLaaqlgIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHLEI----FAAVRGLR-------KSHAAVAITRLAdalkLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 1444
Cdd:PRK09700 99 ENLYIgrhlTKKVCGVNiidwremRVRAAMMLLRVG----LKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1445 GLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQ 1501
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQ-LRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1306-1506 |
1.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.31 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREgdtpgflgycpQENALW------------PN-- 1371
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-----------TEENVWdirhkigmvfqnPDnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 ---LTVKEHLEIFAAVRGLrkSHAAVaITRLADALKL---QD-QLKSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPST 1444
Cdd:PRK13650 94 fvgATVEDDVAFGLENKGI--PHEEM-KERVNEALELvgmQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1445 GLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSK 1506
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1305-1493 |
1.31e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTK--VTAGQVLLKG-----------SREGdtpgfLGYC---PQEnal 1368
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGedilelspderARAG-----IFLAfqyPVE--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1369 WPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKL----QDQLKSPV-KTLSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:COG0396 89 IPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKElgldEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1444 TGLDpegqqqIWqAIRAI------IKNTDRGALLTTHYmaeaEAL-----CDRVAILVSGR 1493
Cdd:COG0396 169 SGLD------ID-ALRIVaegvnkLRSPDRGILIITHY----QRIldyikPDFVHVLVDGR 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1305-1508 |
1.46e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 74.96 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQENALWpNLTVKEHL- 1378
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdiREVTLDSLrraIGVVPQDTVLF-NDTIGYNIr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 ---------EIFAAVrglRKSHAAVAITRLADA---------LKlqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLD 1440
Cdd:cd03253 97 ygrpdatdeEVIEAA---KAAQIHDKIMRFPDGydtivgergLK-----------LSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1441 EPSTGLDPEGQQQIWQAIRAIIKNtdRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSKFG 1508
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1303-1550 |
1.67e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 78.39 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGflgycpqeNALWPNLTVKEHLEIFA 1382
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS--------SGLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1383 AVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiI 1462
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE-F 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1463 KNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGkDYLLEMKVKTLEQVEPLNTEILRLFPQASRQER 1542
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-EFLKKYNQMSVEERKDFREEQISQFQHGLLQED 268
|
....*...
gi 254911033 1543 YSSLMAYK 1550
Cdd:PRK13545 269 QTGRERKR 276
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1305-1481 |
1.98e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.06 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTA-GQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEHL 1378
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlSPAFSAsGEVLLNGRRLTALPAEqrrIGILFQDDLLFPHLSVGENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 eIFAAVRGLRKS--HAAVAiTRLADAlKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:COG4136 98 -AFALPPTIGRAqrRARVE-QALEEA-GLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180
....*....|....*....|....*..
gi 254911033 1457 AIRAIIKntDRG--ALLTTHYMAEAEA 1481
Cdd:COG4136 175 FVFEQIR--QRGipALLVTHDEEDAPA 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
479-696 |
2.06e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRI 558
Cdd:PRK09536 4 IDVSDLSVEFGDTT----VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFlTVRENLRL-----FAKIRGIPPQDvEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGD 633
Cdd:PRK09536 80 ASVPQDTSLSFEF-DVRQVVEMgrtphRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 634 SQIFLLDEPTAGLDpfSRHRVWNLLKERR---ADRVVLFSTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:PRK09536 158 TPVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1305-1474 |
2.63e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 71.71 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREgdtpgfLGYCPQenalwpnltvkehleifaav 1384
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK------IGYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1385 rglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAiraiIKN 1464
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA----LKE 115
|
170
....*....|
gi 254911033 1465 TDRGALLTTH 1474
Cdd:cd03221 116 YPGTVILVSH 125
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1295-1447 |
3.02e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.49 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKKKAKIATR--NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKvTAGQVLLKGSREGDTPG-----FLGYCPQENA 1367
Cdd:COG4138 1 LQLNDVAVAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAaelarHRAYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1368 LWPNLTVKEHLEIFAAvRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSIL-----GNPS--ILLLD 1440
Cdd:COG4138 80 PPFAMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLD 158
|
....*..
gi 254911033 1441 EPSTGLD 1447
Cdd:COG4138 159 EPMNSLD 165
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
479-692 |
3.12e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.84 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYK-----GKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMA--- 550
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 551 ------DLENILR--IAGVCPQANVQFdflTVRENLRLFAKIrgippqDVEKEVQRVLLELEM----KNIQNILAQNLSG 618
Cdd:TIGR02769 83 rrafrrDVQLVFQdsPSAVNPRMTVRQ---IIGEPLRHLTSL------DESEQKARIAELLDMvglrSEDADKLPRQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 619 GQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD--RVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1305-1494 |
3.19e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 73.66 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---------------SREGDTPGFLGYCPQENALW 1369
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhskvSLVGQEPVLFARSLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 pNLTVKEHLEIFAAVrglRKSHAAVAITRLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:cd03248 111 -GLQSCSFECVKEAA---QKAHAHSFISELASGYDTEVGEKG--SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254911033 1450 GQQQIWQAIRAiiKNTDRGALLTTHYMAEAEAlCDRVAILVSGRL 1494
Cdd:cd03248 185 SEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1292-1497 |
3.40e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1292 KHCLSKKKAKIatRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTP--------GFLGYC 1362
Cdd:PRK09700 269 RNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPldavkkgmAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1363 PQENALWPNLTVKEHLEI--------FAAVRGLRKSHAAvaiTRLADALKLQDQLK-----SPVKTLSEGVKRKLCFVLS 1429
Cdd:PRK09700 347 RRDNGFFPNFSIAQNMAIsrslkdggYKGAMGLFHEVDE---QRTAENQRELLALKchsvnQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1430 ILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCI 1497
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1305-1494 |
3.53e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTP------GfLGYCPQE---NALWPNLTV 1374
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDiTGLSPrerrrlG-VAYIPEDrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEHLeIFAAVRGLRKSHAAV----AITRLADAL------KLQDqLKSPVKTLSEGVKRKlcFVLS--ILGNPSILLLDEP 1442
Cdd:COG3845 354 AENL-ILGRYRRPPFSRGGFldrkAIRAFAEELieefdvRTPG-PDTPARSLSGGNQQK--VILAreLSRDPKLLIAAQP 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1443 STGLDPEGQQQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG3845 430 TRGLDVGAIEFIHQRLLEL---RDAGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
479-658 |
3.60e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENI-LR 557
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAkLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 iagvcpQANVQFDF--------LTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEM-KNIQNILAQnLSGGQKRKLTFGI 628
Cdd:PRK10584 87 ------AKHVGFVFqsfmliptLNALENVELPALLRGESSRQSRNGAKALLEQLGLgKRLDHLPAQ-LSGGEQQRVALAR 159
|
170 180 190
....*....|....*....|....*....|
gi 254911033 629 AILGDSQIFLLDEPTAGLDPFSRHRVWNLL 658
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
491-671 |
3.67e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 491 KPNKIEAlKDLTLDIYEGQI--------------TAVLGHSGAGKSTLLNILSGLsVPTKGSVTIYNNNLSEMaDLENIL 556
Cdd:PRK11174 346 DPVTIEA-EDLEILSPDGKTlagplnftlpagqrIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPESWR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 R-IAGVcpQANVQFDFLTVRENLRLfAKirgipPQDVEKEVQRVLlelEMKNIQNILAQ--------------NLSGGQK 621
Cdd:PRK11174 423 KhLSWV--GQNPQLPHGTLRDNVLL-GN-----PDASDEQLQQAL---ENAWVSEFLPLlpqgldtpigdqaaGLSVGQA 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 622 RKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFST 671
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT 541
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1283-1494 |
4.24e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.61 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYAGKqkhclskKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREGDT- 1355
Cdd:PRK11153 7 ISKVFPQG-------GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalSEKELRk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1356 ---------PGFlgycpqenalwpNL----TVKEH----LEIfaavRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSE 1418
Cdd:PRK11153 80 arrqigmifQHF------------NLlssrTVFDNvalpLEL----AGTPKAEIKARVTELLELVGLSDKADRYPAQLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1419 GVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRG--ALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRELGltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
479-692 |
4.47e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLEN--IL 556
Cdd:PRK10908 2 IRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQI 636
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
471-668 |
4.77e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 72.83 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 471 PEfHGkeSIRIRNISKEYKgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMa 550
Cdd:cd03369 2 PE-HG--EIEVENLSVRYA--PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 551 DLENILRIAGVCPQANVQFDFlTVRENLRLFAKIRgippqdvEKEVQRVLLELEMKNiqnilaqNLSGGQKRKLTFGIAI 630
Cdd:cd03369 76 PLEDLRSSLTIIPQDPTLFSG-TIRSNLDPFDEYS-------DEEIYGALRVSEGGL-------NLSQGQRQLLCLARAL 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 254911033 631 LGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVL 668
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTIL 178
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
497-687 |
5.02e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 497 ALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEmADLENIlrIAGVCPQANVQFDFLTVRE 576
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNL--VAYVPQSEEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 577 NLRLFAK------IRGIPPQD---VEKEVQRV-LLELEMKNIQNilaqnLSGGQKRKLTFGIAILGDSQIFLLDEPTAGL 646
Cdd:PRK15056 99 DVVMMGRyghmgwLRRAKKRDrqiVTAALARVdMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254911033 647 DPFSRHRVWNLLKERRAD-RVVLFSTQFMDEADILADRKVFI 687
Cdd:PRK15056 174 DVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1303-1494 |
5.42e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF------LGYCPQENALWPNLTVKE 1376
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimreaVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEI--FAAVRGLRKSHaavaITRLADAL-KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQ 1453
Cdd:PRK11614 100 NLAMggFFAERDQFQER----IKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 1454 IWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK11614 176 IFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1303-1503 |
7.40e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLK----MISGDtKVTAGQVLLKG---SREGDTPGFL-------GYCPQENAL 1368
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGD-KSAGSHIELLGrtvQREGRLARDIrksrantGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1369 WPNLTVKEHLEI------------FAAVRGLRKSHAAVAITRLADALKLQDQlkspVKTLSEGVKRKLCFVLSILGNPSI 1436
Cdd:PRK09984 98 VNRLSVLENVLIgalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQR----VSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1437 LLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1299-1494 |
8.50e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 71.19 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1299 KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR----EGDTPGFLGYCPQENALWpNLTV 1374
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsdlEKALSSLISVLNQRPYLF-DTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEHLeifaavrGLRkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 1454
Cdd:cd03247 92 RNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1455 WQAIRAIIKntDRGALLTTHYMAEAEALcDRVAILVSGRL 1494
Cdd:cd03247 138 LSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1295-1465 |
8.68e-14 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 72.64 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS----------REGdtpgfLGYCPQ 1364
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslRSM-----IGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1365 ----------ENALWPNLTVKEHLEIFAAvrglRKSHAAVAITRLADALklQDQLKSPVKTLSEGVKRKLCFVLSILGNP 1434
Cdd:cd03254 85 dtflfsgtimENIRLGRPNATDEEVIEAA----KEAGAHDFIMKLPNGY--DTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190
....*....|....*....|....*....|.
gi 254911033 1435 SILLLDEPSTGLDPEGQQQIWQAIRAIIKNT 1465
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGR 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1506 |
9.99e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.34 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREG-----DTPGFLGYCPqENALWpNL 1372
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidySRKGlmklrESVGMVFQDP-DNQLF-SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1453 QIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSK 1506
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
479-698 |
1.38e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkpNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGS---VTIYNNNLSEMADLENI 555
Cdd:PRK09984 5 IRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRIA----GVCPQanvQFDF---LTVRENLRLFAK---------IRGIPPQDVEKEVQrVLLELEMKNIQNILAQNLSGG 619
Cdd:PRK09984 81 IRKSrantGYIFQ---QFNLvnrLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 620 QKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE-RRADRV-VLFSTQFMDEADILADRKVFISNGRLKCAGS 697
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGItVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
.
gi 254911033 698 S 698
Cdd:PRK09984 237 S 237
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
493-647 |
1.51e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 76.42 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 493 NKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVP--TKGSVTIYNNNLSEmadlENILRIAGVCPQANVQFD 570
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQ----ETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 571 FLTVRENLRLFAKIRgiPPQDVEKE-----VQRVLLELEMKNIQNILA-----QNLSGGQKRKLTFGIAILGDSQIFLLD 640
Cdd:PLN03140 967 QVTVRESLIYSAFLR--LPKEVSKEekmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
....*..
gi 254911033 641 EPTAGLD 647
Cdd:PLN03140 1045 EPTSGLD 1051
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1308-1505 |
1.55e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1308 SFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPgflgycP---------QENALWPNLTVKEHL 1378
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP------PsrrpvsmlfQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 EIFAAvRGLRKSHAAVA-ITRLADALKLQDQLKSPVKTLSEGVKRKL----CFVLSilgNPsILLLDEPSTGLDPEGQQQ 1453
Cdd:PRK10771 93 GLGLN-PGLKLNAAQREkLHAIARQMGIEDLLARLPGQLSGGQRQRValarCLVRE---QP-ILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1454 IWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKS 1505
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1294-1513 |
2.14e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1294 CLSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-------RE-GDTPGFLGYCPQE 1365
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkeniREvRKFVGLVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1366 NALWPnlTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTG 1445
Cdd:PRK13652 90 QIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1446 LDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLkskFGKDYLL 1513
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1297-1522 |
2.42e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.16 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1297 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllkgSREGDtpgfLGYCPQENALWPNLTVKE 1376
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----DRNGE----VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1457 AIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFgKDYLLEMKVKTLEQ 1522
Cdd:PRK13546 185 KIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1301-1506 |
2.85e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.17 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTPGF--------LGYCPQENALW 1369
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhiTPETGNKNLkklrkkvsLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNlTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQL--KSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 1447
Cdd:PRK13641 100 EN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1448 PEGQQQIWQairaIIKNTDRGA---LLTTHYMAEAEALCDRVAILVSGRLrcigsIQHLKSK 1506
Cdd:PRK13641 178 PEGRKEMMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1298-1513 |
2.94e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 71.11 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1298 KKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregDTPGF--------LGYCPQENALW 1369
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH---DVRDYtlaslrrqIGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 pNLTVKEHleIFAAVRGlrKSHAAV-AITRLADAL----KLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSILLLD 1440
Cdd:cd03251 89 -NDTVAEN--IAYGRPG--ATREEVeEAARAANAHefimELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1441 EPSTGLDPEGQQQIWQAIRAIIKNtdRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDYLL 1513
Cdd:cd03251 164 EATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1316-1505 |
3.00e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1316 ILGLLGHNGAGKSTSLKMISG-DTKVT----AGQVLLKGSREGDTPGFLGYCPQENALW--PN---LTVKEHleIFAAVR 1385
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSIFNYRDVLEFRRRVGMLFqrPNpfpMSIMDN--VLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1386 GL----RKSHAAVAITRLA-----DALKlqDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:PRK14271 127 AHklvpRKEFRGVAQARLTevglwDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1457 AIRAIiknTDR-GALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKS 1505
Cdd:PRK14271 205 FIRSL---ADRlTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
479-711 |
3.14e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.76 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRI 558
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY-DHHYLHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDfLTVRENLRL---FAKIRGIPPQDVEKEVQRVLLELEMKNIQNI--LAQNLSGGQKRKLTFGIAILGD 633
Cdd:TIGR00958 557 VALVGQEPVLFS-GSVRENIAYgltDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVgeKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 634 SQIFLLDEPTAGLDPFSRHRVWNLLKerRADRVVLFSTQFMDEADiLADRKVFISNGRLKCAGSSLFLKKKWGVGYHL 711
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1307-1447 |
3.41e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGdTKVTAGQVLLKGSREGDTPG-----FLGYCPQENALWPNLTVKEHLEIF 1381
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAaelarHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1382 AAVrGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSIL-----GNPS--ILLLDEPSTGLD 1447
Cdd:PRK03695 94 QPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLD 165
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
481-647 |
3.48e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.25 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGKPnkIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSV--PTKGSVTIYNNNLSEMADLE----- 553
Cdd:COG0396 3 IKNLHVSVEGKE--I--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDErarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 ------NILRIAGVcpqanvqfdflTVRENLRLFA-KIRG--IPPQDVEKEVQRVLLELEMKN--IQNILAQNLSGGQKR 622
Cdd:COG0396 79 iflafqYPVEIPGV-----------SVSNFLRTALnARRGeeLSAREFLKLLKEKMKELGLDEdfLDRYVNEGFSGGEKK 147
|
170 180
....*....|....*....|....*.
gi 254911033 623 KL-TFGIAILgDSQIFLLDEPTAGLD 647
Cdd:COG0396 148 RNeILQMLLL-EPKLAILDETDSGLD 172
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1305-1474 |
3.52e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-SREGDTPGF---LGYCPQENALWPNLTVKEHlei 1380
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqSIKKDLCTYqkqLCFVGHRSGINPYLTLREN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1381 faAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 1460
Cdd:PRK13540 95 --CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....*
gi 254911033 1461 iiKNTDRGA-LLTTH 1474
Cdd:PRK13540 173 --HRAKGGAvLLTSH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1303-1503 |
3.73e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKS-TSLKMI----SGDTKVTAGQVLLK------------------GSREGDtpgfL 1359
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleQAGGLVQCDKMLLRrrsrqvielseqsaaqmrHVRGAD----M 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1360 GYCPQE--NALWPNLTVKEhlEIFAAVR---GLRKSHAAVAITRLADALKL---QDQLKSPVKTLSEGVKRKLCFVLSIL 1431
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGE--QIAESIRlhqGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1432 GNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
479-697 |
5.37e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.84 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdLENILRI 558
Cdd:PRK13657 335 VEFDDVSFSY---DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDfLTVRENLRLfAKirgipPQDVEKEVQRVL-----LELEMKNIQNILAQ------NLSGGQKRKLTFG 627
Cdd:PRK13657 411 IAVVFQDAGLFN-RSIEDNIRV-GR-----PDATDEEMRAAAeraqaHDFIERKPDGYDTVvgergrQLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 628 IAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRvvlfsTQFMDeADIL-----ADRKVFISNGRLKCAGS 697
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-----TTFII-AHRLstvrnADRILVFDNGRVVESGS 552
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1295-1526 |
5.92e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.30 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSR-----EGDTPGFLGY-CP-- 1363
Cdd:TIGR03269 6 LTKKfDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALcekcgYVERPSKVGEpCPvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1364 ------QENALWpNLTVKEHLEI-----------FA----------AVRGLRKS--HAAVAITRLADAL---KLQDQLKS 1411
Cdd:TIGR03269 86 ggtlepEEVDFW-NLSDKLRRRIrkriaimlqrtFAlygddtvldnVLEALEEIgyEGKEAVGRAVDLIemvQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1412 PVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVS 1491
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
250 260 270
....*....|....*....|....*....|....*
gi 254911033 1492 GRLRCIGSIQHLKSKFGKDYLLEMKVKTLEQVEPL 1526
Cdd:TIGR03269 245 GEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPI 279
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
499-660 |
7.13e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 499 KDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRIAGVCPQANVQFDfLTVRE-- 576
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGD-ITVQElv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 577 ------NLRLFAKIRgippQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFS 650
Cdd:PRK10253 103 argrypHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170
....*....|
gi 254911033 651 RHRVWNLLKE 660
Cdd:PRK10253 179 QIDLLELLSE 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1305-1494 |
7.76e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsREGDTpgflgYCPQE---------------NALW 1369
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-HEVVT-----RSPQDglangivyisedrkrDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNLTVKEHLEIFAavrgLRK-SHAAVAITRLADALKLQD-----QLKSP-----VKTLSEGVKRKLCFVLSILGNPSILL 1438
Cdd:PRK10762 343 LGMSVKENMSLTA----LRYfSRAGGSLKHADEQQAVSDfirlfNIKTPsmeqaIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1439 LDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQ-FKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1314-1523 |
8.11e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 8.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1314 GEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQENALWPNLTVKEHLEIfaavrGLR 1388
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFarkVAYLPQQLPAAEGMTVRELVAI-----GRY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1389 KSHAAVAITRLADALKLQDQLK----SP-----VKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 1459
Cdd:PRK10575 112 PWHGALGRFGAADREKVEEAISlvglKPlahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVH 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1460 AIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLkskfgkdylleMKVKTLEQV 1523
Cdd:PRK10575 192 RLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL-----------MRGETLEQI 244
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1318-1449 |
8.15e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1318 GLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsregdTPGF-LGYCPQENALWPNLTVKEHLE-----IFAAVRGLRKSH 1391
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------APGIkVGYLPQEPQLDPEKTVRENVEegvaeVKAALDRFNEIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1392 AAVAiTRLA--DAL-----KLQDQLKS------------------------PVKTLSEGVKRK--LCFVLsiLGNPSILL 1438
Cdd:PRK11819 110 AAYA-EPDAdfDALaaeqgELQEIIDAadawdldsqleiamdalrcppwdaKVTKLSGGERRRvaLCRLL--LEKPDMLL 186
|
170
....*....|.
gi 254911033 1439 LDEPSTGLDPE 1449
Cdd:PRK11819 187 LDEPTNHLDAE 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
500-647 |
1.03e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 500 DLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAD--LENILRI---AGVCPQanvqfdfLTV 574
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyHQDLLYLghqPGIKTE-------LTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 575 RENLRLFAKIRGipPQDVEkEVQRVLLELEMKNIQNILAQNLSGGQKRKltfgIAI----LGDSQIFLLDEPTAGLD 647
Cdd:PRK13538 92 LENLRFYQRLHG--PGDDE-ALWEALAQVGLAGFEDVPVRQLSAGQQRR----VALarlwLTRAPLWILDEPFTAID 161
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1305-1493 |
1.07e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.83 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVtagqvllKGSREGDT--------------PGFLGYCPQENALWP 1370
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEG-------NVSVEGDIhyngipykefaekyPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 NLTVKEHLEIFAAVRGlrkshaavaitrladalklqDQLkspVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 1450
Cdd:cd03233 97 TLTVRETLDFALRCKG--------------------NEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254911033 1451 QQQIWQAIRAIIKNTdRGALLTTHYMA--EAEALCDRVAILVSGR 1493
Cdd:cd03233 154 ALEILKCIRTMADVL-KTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1311-1476 |
1.20e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1311 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL--LKGSregdtpgflgYCPQENALWPNLTVKEHLEifAAVRGLR 1388
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKIS----------YKPQYIKPDYDGTVEDLLR--SITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1389 KSHaavAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRG 1468
Cdd:PRK13409 430 SSY---YKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREAT 506
|
170
....*....|
gi 254911033 1469 ALLTTH--YM 1476
Cdd:PRK13409 507 ALVVDHdiYM 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1283-1449 |
1.61e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.28 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYAGKqKHCLskkkakiatRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKgsregdtPGF-LGY 1361
Cdd:TIGR03719 10 VSKVVPPK-KEIL---------KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIkVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1362 CPQENALWPNLTVKEHLEifAAVRGLRKshaavAITRL-------------ADAL-----KLQDQLKS------------ 1411
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVE--EGVAEIKD-----ALDRFneisakyaepdadFDKLaaeqaELQEIIDAadawdldsqlei 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1412 ------------PVKTLSEGVKRK--LCFVLsiLGNPSILLLDEPSTGLDPE 1449
Cdd:TIGR03719 146 amdalrcppwdaDVTKLSGGERRRvaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
467-692 |
1.72e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 467 EPVSPefhGKESIRIRNISkeYKGkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNL 546
Cdd:COG3845 249 APAEP---GEVVLEVENLS--VRD-DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 547 SEMADLENI-LRIA---------GVCPQanvqfdfLTVRENLRL-------FAKIRGIPPQDVEKEVQRVLLELEMK--N 607
Cdd:COG3845 323 TGLSPRERRrLGVAyipedrlgrGLVPD-------MSVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDVRtpG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 608 IqNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR--VVLFSTQfMDEADILADRKV 685
Cdd:COG3845 396 P-DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGaaVLLISED-LDEILALSDRIA 473
|
....*..
gi 254911033 686 FISNGRL 692
Cdd:COG3845 474 VMYEGRI 480
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1295-1512 |
1.86e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.22 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1295 LSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTP------GFLGYCPQE 1365
Cdd:PRK10070 35 LEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAElrevrrKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1366 NALWPNLTVKEHLEIFAAVRGLRkshAAVAITRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEP 1442
Cdd:PRK10070 115 FALMPHMTVLDNTAFGMELAGIN---AEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1443 STGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDYL 1512
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
476-668 |
1.87e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.97 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 476 KESIRIRNISKEYKGKPNKieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSE--MADLE 553
Cdd:PRK11176 339 KGDIEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NilRIAGVCPQANVQFDflTVRENLrLFAKIRGIPPQDVEKeVQRVLLELE----MKN-IQNILAQN---LSGGQKRKLT 625
Cdd:PRK11176 417 N--QVALVSQNVHLFND--TIANNI-AYARTEQYSREQIEE-AARMAYAMDfinkMDNgLDTVIGENgvlLSGGQRQRIA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 626 FGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVL 668
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1300-1503 |
1.89e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.66 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMI-------SGDTKVtAGQVLlkgsregdtpgflgycpQENALW--- 1369
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnglllpeAGTITV-GGMVL-----------------SEETVWdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 ---------PN-----LTVKEHLEIFAAVRGLRKSHAavaITRLADALKL---QDQLKSPVKTLSEGVKRKLCFVLSILG 1432
Cdd:PRK13635 81 rqvgmvfqnPDnqfvgATVQDDVAFGLENIGVPREEM---VERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1433 NPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1303-1494 |
2.68e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-----REGDTPgFL----GYCPQENALWPNLT 1373
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlKNREVP-FLrrqiGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 VKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEgqqq 1453
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA---- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254911033 1454 IWQAIRAIIKNTDR---GALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK10908 172 LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
496-696 |
3.15e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.46 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 496 EALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRIAG-------------VC 562
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADknqlrllrtrltmVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 563 PQANVqFDFLTVREN-LRLFAKIRGIPPQDVEKEVQRVLLELEM-KNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLD 640
Cdd:PRK10619 99 QHFNL-WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 641 EPTAGLDP---FSRHRVWNLLKERRADRVVLfsTQFMDEADILADRKVFISNGRLKCAG 696
Cdd:PRK10619 178 EPTSALDPelvGEVLRIMQQLAEEGKTMVVV--THEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
497-662 |
3.65e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 497 ALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADlENILRIAGVCPQANVQ-FDFLTVR 575
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARMGVVRTFQHVRlFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 576 ENL----------RLFAKIRGIPP-QDVEKE-VQRVLLELE---MKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLD 640
Cdd:PRK11300 99 ENLlvaqhqqlktGLFSGLLKTPAfRRAESEaLDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180
....*....|....*....|..
gi 254911033 641 EPTAGLDPFSRHRVWNLLKERR 662
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELR 200
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1301-1494 |
3.86e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--------DTKVTAGQVLLKGSREGDTPGFLGYCPQE-NALWPN 1371
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCfVLSILG-NPSILLLDEPSTGLDPEG 1450
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA-IAGILAvEPKIIILDESTSMLDPAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254911033 1451 QQQIWQAIRAIIKNTDRGALLTTHYMAEAEaLCDRVAILVSGRL 1494
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1305-1493 |
3.87e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.71 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFL-------GYCPQENALWPNLTVKEH 1377
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvGMVFQQFNLFPHLTVLEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LEIfaA---VRGLRKSHA-AVAITRLADaLKLQDQLKSPVKTLSEGVK------RKLCFvlsilgNPSILLLDEPSTGLD 1447
Cdd:COG1126 98 VTL--ApikVKKMSKAEAeERAMELLER-VGLADKADAYPAQLSGGQQqrvaiaRALAM------EPKVMLFDEPTSALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1448 PEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:COG1126 169 PELVGEVLDVMRD-LAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1307-1502 |
4.16e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTPGF-----LGYCPQ---ENALWPNLTVKEH 1377
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPiDIRSPRDairagIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LEIFAAVRGLR----------KSHAAVAITRLADALKLQDQlksPVKTLSEGVKRKlcfvlSILG-----NPSILLLDEP 1442
Cdd:PRK11288 352 INISARRHHLRagclinnrweAENADRFIRSLNIKTPSREQ---LIMNLSGGNQQK-----AILGrwlseDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1443 STGLDPEGQQQIWQAIRAIIKnTDRGALLTTHYMAEAEALCDRVAILVSGRLRciGSIQH 1502
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
508-654 |
4.25e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 508 GQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMadlENILRIAGVCPQANVQFDFLTVRENLRLFAKIR-- 585
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPT---KQILKRTGFVTQDDILYPHLTVRETLVFCSLLRlp 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 586 -GIPPQDVEKEVQRVLLELEMKNIQNILAQN-----LSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRV 654
Cdd:PLN03211 171 kSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1305-1494 |
4.57e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMIS------GDTKVtAGQVLLKGSREGDTP--------GFLGYCPqeNALwP 1370
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNrlielyPEARV-SGEVYLDGQDIFKMDvielrrrvQMVFQIP--NPI-P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 NLTVKEHLEIFAAVRGLRKSHAAVAiTRLADALK-------LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:PRK14247 96 NLSIFENVALGLKLNRLVKSKKELQ-ERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1444 TGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1291-1474 |
4.88e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.53 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1291 QKHCLSKK--KAKIAT---RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---------------S 1350
Cdd:PRK11629 7 QCDNLCKRyqEGSVQTdvlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1351 REgdtpgfLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSI 1430
Cdd:PRK11629 87 QK------LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254911033 1431 LGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTH 1474
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1285-1495 |
4.91e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1285 KEYAGKQKHCLSkkkakIATrNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS---------REGDT 1355
Cdd:PRK10584 13 KKSVGQGEHELS-----ILT-GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeeaRAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1356 PGFLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPS 1435
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1436 ILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLR 1495
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
479-647 |
5.03e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVtiynnnlsemaDLENILRI 558
Cdd:PRK09544 5 VSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 aGVCPQaNVQFDF---LTVRENLRLFAkirGIPPQDVEKEVQRV----LLELEMkniqnilaQNLSGGQKRKLTFGIAIL 631
Cdd:PRK09544 70 -GYVPQ-KLYLDTtlpLTVNRFLRLRP---GTKKEDILPALKRVqaghLIDAPM--------QKLSGGETQRVLLARALL 136
|
170
....*....|....*.
gi 254911033 632 GDSQIFLLDEPTAGLD 647
Cdd:PRK09544 137 NRPQLLVLDEPTQGVD 152
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1305-1509 |
6.36e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP--------GFLGYCPQENALWPNLTVKE 1376
Cdd:TIGR00956 78 KPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPeeikkhyrGDVVYNAETDVHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1377 HLEIFAAVR-------GLRKSHAAVAITRLADAL---------KLQDQLkspVKTLSEGVKRKLCFVLSILGNPSILLLD 1440
Cdd:TIGR00956 158 TLDFAARCKtpqnrpdGVSREEYAKHIADVYMATyglshtrntKVGNDF---VRGVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1441 EPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTThYMAEAEA--LCDRVAILVSGRLRCIGSIQHLKSKFGK 1509
Cdd:TIGR00956 235 NATRGLDSATALEFIRALKTSANILDTTPLVAI-YQCSQDAyeLFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1306-1512 |
7.33e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMI-------SGDTKVtAGQVLLKGSREGDTPGFL-----GYCPQENALWPNLT 1373
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNI-AGNHFDFSKTPSDKAIRElrrnvGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 VKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:PRK11124 99 VQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1453 QIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK----SKFgKDYL 1512
Cdd:PRK11124 179 QIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTqpqtEAF-KNYL 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
448-698 |
7.46e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 448 AHVILEDGIDPVPSSGDSFEPVSPEFHGKESIRIRNISKEYKGKPNKIEA-----LKDLTLDIYEGQITAVLGHSGAGKS 522
Cdd:PTZ00243 621 VVVEDTDYGSPSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFELepkvlLRDVSVSVPRGKLTVVLGATGSGKS 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 523 TLLNILSGLSVPTKGSVtiynnnLSEMAdlenilrIAGVCPQA---NVqfdflTVRENLRLFAKIRGIPPQDV------E 593
Cdd:PTZ00243 701 TLLQSLLSQFEISEGRV------WAERS-------IAYVPQQAwimNA-----TVRGNILFFDEEDAARLADAvrvsqlE 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 594 KEVQRVL--LELEM--KNIqnilaqNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWN--LLKERRADRVV 667
Cdd:PTZ00243 763 ADLAQLGggLETEIgeKGV------NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALAGKTRV 836
|
250 260 270
....*....|....*....|....*....|.
gi 254911033 668 LFSTQFMDEAdiLADRKVFISNGRLKCAGSS 698
Cdd:PTZ00243 837 LATHQVHVVP--RADYVVALGDGRVEFSGSS 865
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1303-1512 |
9.52e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.32 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWPN-------LTVK 1375
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpetqfvgRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIW 1455
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1456 QAIRAiIKNTDRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDYL 1512
Cdd:PRK13644 177 ERIKK-LHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1316-1499 |
1.22e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1316 ILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREG-----DTPGFLGYCPQENALWPNLTVkehlEIFAAVR 1385
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldySKRGllalrQQVATVFQDPEQQIFYTDIDS----DIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1386 GLRKSHAAVAiTRLADALKLQDQL---KSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAII 1462
Cdd:PRK13638 105 NLGVPEAEIT-RRVDEALTLVDAQhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 254911033 1463 KNTDRgALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:PRK13638 184 AQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
471-696 |
1.43e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 68.91 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 471 PEFHgkesIRIRNISkeYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMa 550
Cdd:TIGR01842 313 PEGH----LSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 551 DLENILRIAGVCPQaNVQFDFLTVRENLRLF------------AKIRGippqdvekeVQRVLLELEMKNIQNILA--QNL 616
Cdd:TIGR01842 386 DRETFGKHIGYLPQ-DVELFPGTVAENIARFgenadpekiieaAKLAG---------VHELILRLPDGYDTVIGPggATL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 617 SGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQfMDEADILADRKVFISNGRLKCA 695
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGItVVVITH-RPSLLGCVDKILVLQDGRIARF 534
|
.
gi 254911033 696 G 696
Cdd:TIGR01842 535 G 535
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1305-1494 |
1.78e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsRE--GDTPGF-----LGYCP---QENAL------ 1368
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG-KEinALSTAQrlargLVYLPedrQSSGLyldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1369 -WPNLTVKEHLEIF-------AAVrgLRKSHAAVAItRLADAlklqDQlksPVKTLSEGVKRKLCFVLSILGNPSILLLD 1440
Cdd:PRK15439 359 aWNVCALTHNRRGFwikpareNAV--LERYRRALNI-KFNHA----EQ---AARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1441 EPSTGLDPEGQQQIWQAIRAIIK-NTdrGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAqNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
488-654 |
2.04e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 488 YKGKPNKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADlENILRIAGVCPQANV 567
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 568 QF-DflTVRENLRLFAKIRGIPPQdvEKEVQRVLLELEMKniQNILAQN---LSGGQKRKltfgIAILGDSQ----IFLL 639
Cdd:PRK10247 92 LFgD--TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALP--DTILTKNiaeLSGGEKQR----ISLIRNLQfmpkVLLL 161
|
170
....*....|....*
gi 254911033 640 DEPTAGLDPFSRHRV 654
Cdd:PRK10247 162 DEITSALDESNKHNV 176
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1305-1513 |
2.05e-11 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 65.64 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQENALWPNlTVKEHLE 1379
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdiRDLNLRWLrsqIGLVSQEPVLFDG-TIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 IfaavrGLRKSHA--AVAITRLADA----LKLQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:cd03249 99 Y-----GKPDATDeeVEEAAKKANIhdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1450 GQQQIWQAIRAIIKNtdRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDYLL 1513
Cdd:cd03249 174 SEKLVQEALDRAMKG--RTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1565 |
2.22e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSRegdtpgflgyCPQENALW-----------PN 1371
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE----------VNAENEKWvrskvglvfqdPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 -----LTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGL 1446
Cdd:PRK13647 90 dqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1447 DPEGQQQIwQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGsiqhlkskfGKDYLLEMKVktLEQVE-- 1524
Cdd:PRK13647 170 DPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG---------DKSLLTDEDI--VEQAGlr 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 254911033 1525 -PLNTEILRLFPQASRQerysslmayKLPV---EAVQPLSQAFFK 1565
Cdd:PRK13647 238 lPLVAQIFEDLPELGQS---------KLPLtvkEAVQIIRKLLTK 273
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1306-1501 |
2.39e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTPGFLGYCPQENALWPNLTVKEHLEIFA 1382
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1383 AV--RGLRKSHAAV--AITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 1458
Cdd:PRK10851 100 TVlpRRERPNAAAIkaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 1459 RAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQ 1501
Cdd:PRK10851 180 RQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
491-660 |
2.72e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 491 KPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMA---------DLENILR--IA 559
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewravrsDIQMIFQdpLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 560 GVCPQANVQfDFLTvrENLRLFAKirGIPPQDVEKEVQRVLLELEM-KNIQNILAQNLSGGQKRKLtfGIA---ILgDSQ 635
Cdd:PRK15079 110 SLNPRMTIG-EIIA--EPLRTYHP--KLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRI--GIAralIL-EPK 181
|
170 180
....*....|....*....|....*
gi 254911033 636 IFLLDEPTAGLDPFSRHRVWNLLKE 660
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQ 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1305-1449 |
2.74e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.99 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllKGSREGDtpgfLGYCPQENALW--PNLTVKEHLEIFA 1382
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWSENAN----IGYYAQDHAYDfeNDLTLFDWMSQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1383 -------AVRGlrkshaavAITRLadaLKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:PRK15064 410 qegddeqAVRG--------TLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1311-1476 |
2.74e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.27 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1311 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdtpgfLGYCPQENALWPNLTVKEHLEifaavrglrkS 1390
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------ISYKPQYISPDYDGTVEEFLR----------S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1391 HAAVAI------TRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKN 1464
Cdd:COG1245 425 ANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170
....*....|....
gi 254911033 1465 TDRGALLTTH--YM 1476
Cdd:COG1245 505 RGKTAMVVDHdiYL 518
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1303-1507 |
2.83e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG--SREGDTPGFLGYCPQ-ENALWPNLTVKEHLE 1379
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQALQKNLVAYVPQsEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 I---FAAVRGLR--KSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 1454
Cdd:PRK15056 102 MmgrYGHMGWLRraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1455 WQAIRAiIKNTDRGALLTTHYMAEAEALCD-----RVAILVSGRLRCIGSIQHLKSKF 1507
Cdd:PRK15056 182 ISLLRE-LRDEGKTMLVSTHNLGSVTEFCDytvmvKGTVLASGPTETTFTAENLELAF 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
498-647 |
2.92e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMaDLENILRIAGVCPQANVQFDFLTVREn 577
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW-SSKAFARKVAYLPQQLPAAEGMTVRE- 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 578 lrLFAKIR-------GIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:PRK10575 105 --LVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1269-1474 |
3.04e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 67.77 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1269 STSFDEKPVIIASCLRKEYAGKQkhclskkkakIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLK 1348
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGAP----------PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1349 G-----SREGDTPGFLGYCPQENALWpNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALK-LQDQLKSPV----KTLSE 1418
Cdd:TIGR02868 396 GvpvssLDQDEVRRRVSVCAQDAHLF-DTTVRENLRLARPDATDEELWAALERVGLADWLRaLPDGLDTVLgeggARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1419 GVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRGALLTTH 1474
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1301-1511 |
3.57e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWPNLTVKEHLEI 1380
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1381 FAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 1460
Cdd:PRK11248 94 GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1461 IIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCigsIQHLKSKFGKDY 1511
Cdd:PRK11248 174 LWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRF 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
479-685 |
3.85e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYK-----GKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMA--- 550
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 551 ------DLENILR--IAGVCPQANVQFdflTVRENLRlfaKIRGIPPQDVEKEVQRVLLELEMK-NIQNILAQNLSGGQK 621
Cdd:PRK10419 84 rkafrrDIQMVFQdsISAVNPRKTVRE---IIREPLR---HLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 622 RKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLK--------------------ERRADRVVLfstqfMDEADILA 681
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKklqqqfgtaclfithdlrlvERFCQRVMV-----MDNGQIVE 232
|
....
gi 254911033 682 DRKV 685
Cdd:PRK10419 233 TQPV 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
507-668 |
3.99e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 507 EGQITAVLGHSGAGKSTLLNILSGLSVPTKGSvtiYNNNLS-----------EMAD-----LENILRIAgVCPQanvQFD 570
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YEEEPSwdevlkrfrgtELQNyfkklYNGEIKVV-HKPQ---YVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 571 FL------TVRENLRlfaKI--RGIPPQDVEkevqrvllELEMKNI--QNIlaQNLSGGQKRKLTFGIAILGDSQIFLLD 640
Cdd:PRK13409 171 LIpkvfkgKVRELLK---KVdeRGKLDEVVE--------RLGLENIldRDI--SELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180
....*....|....*....|....*...
gi 254911033 641 EPTAGLDPFSRHRVWNLLKERRADRVVL 668
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGKYVL 265
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
477-693 |
4.65e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.22 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 477 ESIRIRNISKEY----------------KGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVT 540
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 541 IYnnnlsemADLENILRIAGVCPQanvqfdfLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQ 620
Cdd:PRK13546 83 RN-------GEVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 621 KRKLTFGIAILGDSQIFLLDEP-TAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRLK 693
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
498-647 |
6.09e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSvPTKGSVTIYNNNLSEMaDLENILRIAGVCPQANVQFDFLTVREN 577
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDW-SAAELARHRAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 578 LRLFAkirgiPPQDVEKEVQRVLLEL-EMKNIQNILAQN---LSGG--QKRKLTfgiAIL--------GDSQIFLLDEPT 643
Cdd:COG4138 90 LALHQ-----PAGASSEAVEQLLAQLaEALGLEDKLSRPltqLSGGewQRVRLA---AVLlqvwptinPEGQLLLLDEPM 161
|
....
gi 254911033 644 AGLD 647
Cdd:COG4138 162 NSLD 165
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1306-1503 |
7.30e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP--------GFLGYcpqenALWPNLTVKEH 1377
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqrdicmVFQSY-----ALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1378 LEIFAAVRGLRKSHAAvaiTRLADALKLQDQL---KSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 1454
Cdd:PRK11432 99 VGYGLKMLGVPKEERK---QRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 1455 WQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1314-1447 |
7.64e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1314 GEILGLLGHNGAGKSTSLKMISGDTKVT--AGQVLLKGSR-EGDTPGFLGYCPQENALWPNLTVKEHLeIFAAVRGLRKS 1390
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKpTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLLRLPKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1391 HAAVAITRLADAL-------KLQDQL--KSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 1447
Cdd:PLN03211 173 LTKQEKILVAESViselgltKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1280-1509 |
8.20e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1280 ASCLRKEYAGKQkhCLSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREG 1353
Cdd:PRK10419 6 VSGLSHHYAHGG--LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1354 -------------DTPGflgycpqenALWPNLTVKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQDQL--KSPvKTLS 1417
Cdd:PRK10419 84 rkafrrdiqmvfqDSIS---------AVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDSVldKRP-PQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1418 EGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL--- 1494
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvet 233
|
250
....*....|....*
gi 254911033 1495 RCIGSIQHLKSKFGK 1509
Cdd:PRK10419 234 QPVGDKLTFSSPAGR 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
501-647 |
9.09e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 501 LTLDIYEGQITAVLGHSGAGKSTLLNILSGLSvPTKGSVTIYNNNLSEMADLENILRIAGVCPQANVQFDfLTVRENLRL 580
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFA-MPVFQYLTL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 581 FakirgIPPQDVEKEVQRVLLEL-EMKNIQNILA---QNLSGGQKRKLTFGIAILG-------DSQIFLLDEPTAGLD 647
Cdd:PRK03695 93 H-----QPDKTRTEAVASALNEVaEALGLDDKLGrsvNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
178-417 |
1.04e-10 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 65.10 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 178 ALQAAINAAIIETTTNHSVMEELLSVSGKFMKIHP---FVRQEGILTDFFIFTCIISFSPITYYVSINVARERKRMKGLM 254
Cdd:pfam12698 115 LILNALQSLLQQLNASALVLLLEALSTSAPIPVEStplFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 255 MMMGLRDP-AFWLSWGLLYAGFVFIMALSLALVIKSVQFFIlTSFMVVFSLFLLYGLSMITLAFLMSALVRKSVLTGLSV 333
Cdd:pfam12698 195 LLVSGVSPlQYWLGKILGDFLVGLLQLLIILLLLFGIGIPF-GNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSII 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 334 FLLT-IFWGSLGFTSLYRYLPAPVEWTLSLFSPFAFTLGMaqllrvdYDLNSNAPpdpasGSNLIIATNFMLVFdAFLYL 412
Cdd:pfam12698 274 GIVIlLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGL-------LRLIYGDS-----LWEIAPSLIILLLF-AVVLL 340
|
....*
gi 254911033 413 ALMMY 417
Cdd:pfam12698 341 LLALL 345
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1296-1494 |
1.14e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.64 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1296 SKKKAkiaTRNVSFCVRKGEILGLLGHNGAGKSTSLKMIS--GD---TKVTAGQVLLKG----SREGDTPGF---LGYCP 1363
Cdd:PRK14239 16 NKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGhniySPRTDTVDLrkeIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1364 QENALWPnLTVKEHLEIFAAVRGLRKSH---AAVAITRLADAL--KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILL 1438
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQvldEAVEKSLKGASIwdEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1439 LDEPSTGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1303-1499 |
1.14e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKM------------ISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWP 1370
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 NlTVKEHLEIFAAVRGLRKSHAAVAITRLADALKL-QDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1450 GQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
479-670 |
1.14e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.11 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLsVPTKGSVTIYNNNLSEMAdLENILRI 558
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFlTVRENLRLFAKIRgippqdvEKEVQRVLLELEMKNIQNILAQNL-----------SGGQKRKLTFG 627
Cdd:cd03289 79 FGVIPQKVFIFSG-TFRKNLDPYGKWS-------DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 628 IAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFS 670
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILS 193
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
492-683 |
1.16e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.58 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 492 PNKIEALKDLTL-----DIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMadlenilriagvcPQaN 566
Cdd:cd03237 4 PTMKKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------PQ-Y 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 567 VQFDF-LTVRENLRLFAKIRGIPPQ---DVEKEVQrvllelemknIQNILAQ---NLSGGQKRKLTFGIAILGDSQIFLL 639
Cdd:cd03237 70 IKADYeGTVRDLLSSITKDFYTHPYfktEIAKPLQ----------IEQILDRevpELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 640 DEPTAGLDPFSRHRVWNLLKerradRVVLF--STQFMDEADI-----LADR 683
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIR-----RFAENneKTAFVVEHDIimidyLADR 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1277-1477 |
1.33e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.11 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1277 VIIASCLRKEYAGKqkhclskkkakIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsreGDTP 1356
Cdd:TIGR03719 322 VIEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----GETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1357 GfLGYCPQE-NALWPNLTVKE-------HLEIfaavrGLRKSHAAVAITRLadALKLQDQLKsPVKTLSEGVKRKLCFVL 1428
Cdd:TIGR03719 386 K-LAYVDQSrDALDPNKTVWEeisggldIIKL-----GKREIPSRAYVGRF--NFKGSDQQK-KVGQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1429 SILGNPSILLLDEPSTGLDPEGQQQIWQAIR-----AIIKNTDRGAL--LTTHYMA 1477
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLnfagcAVVISHDRWFLdrIATHILA 512
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1306-1493 |
1.60e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKS-TSLKMI-----------SGDTKVtAGQVLLKGSrEGDTPGFLG----YCPQEN--A 1367
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIRF-HGESLLHAS-EQTLRGVRGnkiaMIFQEPmvS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1368 LWPNLTVKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQD---QLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:PRK15134 105 LNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1444 TGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
478-647 |
1.74e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.51 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEY-KGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdlENIL 556
Cdd:PRK10790 340 RIDIDNVSFAYrDDNL----VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS--HSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RiAGVcpqANVQFDFL----TVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKN-IQNILAQ---NLSGGQKRKLTFGI 628
Cdd:PRK10790 414 R-QGV---AMVQQDPVvladTFLANVTLGRDISEEQVWQALETVQLAELARSLPDgLYTPLGEqgnNLSVGQKQLLALAR 489
|
170
....*....|....*....
gi 254911033 629 AILGDSQIFLLDEPTAGLD 647
Cdd:PRK10790 490 VLVQTPQILILDEATANID 508
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
498-668 |
1.74e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 65.61 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdLENILRIAGVCPQANVQF-DflTVRE 576
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT-QASLRAAIGIVPQDTVLFnD--TIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 577 NLRlFAKirgipPQDVEKEVQRVlleLEMKNIQNILAQ--------------NLSGGQKRKLtfGIA--ILGDSQIFLLD 640
Cdd:COG5265 451 NIA-YGR-----PDASEEEVEAA---ARAAQIHDFIESlpdgydtrvgerglKLSGGEKQRV--AIArtLLKNPPILIFD 519
|
170 180
....*....|....*....|....*...
gi 254911033 641 EPTAGLDPFSRHRVWNLLKERRADRVVL 668
Cdd:COG5265 520 EATSALDSRTERAIQAALREVARGRTTL 547
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
468-692 |
1.82e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 468 PVSPEFHGKESIRIRNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNnnls 547
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG---- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 548 EMADLENilriagvcPQANVQFdFLTVRENLRLFAKIRGIPPQDVEKE-VQRVLLELEMKN---IQN--ILAQNLSGGQK 621
Cdd:PRK10522 385 KPVTAEQ--------PEDYRKL-FSAVFTDFHLFDQLLGPEGKPANPAlVEKWLERLKMAHkleLEDgrISNLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 622 RKLTFGIAILGDSQIFLLDEPTAGLDP-FSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPhFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1303-1493 |
1.86e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG-------DTKVT-AGQVL-LKGSREGDTPGfLGYCPQENALWPNLT 1373
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyEGEIIfEGEELqASNIRDTERAG-IAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 VKEHL----EIfaaVRGLRKSHAAVaitrLADALKLQDQLK------SPVKTLSEGvKRKLCFVLSILG-NPSILLLDEP 1442
Cdd:PRK13549 99 VLENIflgnEI---TPGGIMDYDAM----YLRAQKLLAQLKldinpaTPVGNLGLG-QQQLVEIAKALNkQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1443 STGLDpEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:PRK13549 171 TASLT-ESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
479-697 |
1.94e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLS--VPTKGSVTIYNNNLSEMADLENIL 556
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQANVQFDFLTVRENLRlfakirgippqDVEKevqrvllelemkniqnilaqNLSGGQKRKLTFGIAILGDSQI 636
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLR-----------YVNE--------------------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254911033 637 FLLDEPTAGLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEAD-ILADRKVFISNGRLKCAGS 697
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
481-647 |
2.17e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYkGKPNKIEalkDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdLENilRIAG 560
Cdd:PRK11432 9 LKNITKRF-GSNTVID---NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS-IQQ--RDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 561 VCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLD 640
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
....*..
gi 254911033 641 EPTAGLD 647
Cdd:PRK11432 162 EPLSNLD 168
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
507-660 |
2.19e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 507 EGQITAVLGHSGAGKSTLLNILSGLSVPTKGsvtiynnNLSEMADLENIL-RIAGvcpqaNVQFDFLT-VRENlrlfaKI 584
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSWDEVLkRFRG-----TELQDYFKkLANG-----EI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 585 R-GIPPQDVEKeVQRV-------LLE--------------LEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEP 642
Cdd:COG1245 161 KvAHKPQYVDL-IPKVfkgtvreLLEkvdergkldelaekLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170
....*....|....*...
gi 254911033 643 TAGLDPFSRHRVWNLLKE 660
Cdd:COG1245 240 SSYLDIYQRLNVARLIRE 257
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1307-1494 |
2.26e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP--------GFLGYCPQENALwpNLTVKEHL 1378
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrrkiGMVFQNPDNQFV--GATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 EIFAAVRGLRKSHAavaITRLADAL----KLQDQLKSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 1454
Cdd:PRK13642 104 AFGMENQGIPREEM---IKRVDEALlavnMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1455 WQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRL 1494
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
464-647 |
2.28e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.74 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 464 DSFE--PVSPefHGKESIRIRNISKEY-KGKPnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILsglsvptkgsvt 540
Cdd:TIGR00957 622 DSIErrTIKP--GEGNSITVHNATFTWaRDLP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL------------ 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 541 iynnnLSEMADLENILRIAG----VCPQANVQFDflTVRENLrLFAKIRGIPPQDVEKEVQRVLLELEM--KNIQNILAQ 614
Cdd:TIGR00957 685 -----LAEMDKVEGHVHMKGsvayVPQQAWIQND--SLRENI-LFGKALNEKYYQQVLEACALLPDLEIlpSGDRTEIGE 756
|
170 180 190
....*....|....*....|....*....|....*.
gi 254911033 615 ---NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:TIGR00957 757 kgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1283-1499 |
2.81e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.09 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1283 LRKEYAGKQKhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGD-TPG---- 1357
Cdd:PRK11650 9 VRKSYDGKTQ----------VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElEPAdrdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1358 ---FLGYcpqenALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNP 1434
Cdd:PRK11650 79 amvFQNY-----ALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 1435 SILLLDEPSTGLDPEGQQQiwqaIRAIIKNTDR----GALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQ----MRLEIQRLHRrlktTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1303-1493 |
2.91e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGS-------REGDTPGfLGYCPQENALWPNLT 1373
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasniRDTERAG-IVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 VKEHL----EIfaAVRGLRKSHAavAITRLADALKLQDQLKS-----PVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 1444
Cdd:TIGR02633 95 VAENIflgnEI--TLPGGRMAYN--AMYLRAKNLLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 1445 GLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:TIGR02633 171 SLTEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
500-648 |
2.91e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 500 DLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMA--DLENILRIAGVCPQANVQFDFLTVREN 577
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 578 ----LRLFAKirgIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDP 648
Cdd:PRK11831 105 vaypLREHTQ---LPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1305-1474 |
3.20e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGdtkvtagqvllkgsREGDTPGFLGYCPQENALWPNLTVKEHLeifaav 1384
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCVDVPDNQFGREASLIDAI------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1385 rgLRKSHAAVAITRLADAlKLQDQ--LKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAII 1462
Cdd:COG2401 107 --GRKGDFKDAVELLNAV-GLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLA 183
|
170
....*....|..
gi 254911033 1463 KNTDRGALLTTH 1474
Cdd:COG2401 184 RRAGITLVVATH 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1305-1486 |
3.32e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.07 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKgSREG-----------------DTpgfLGYCPQ-EN 1366
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGwvdlaqaspreilalrrRT---IGYVSQfLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1367 ALwPNLTVkehLEIFAA---VRGLRKSHAAVAITRLADALKLQDQLKS-PVKTLSEGVKRKLCFVLSILGNPSILLLDEP 1442
Cdd:COG4778 104 VI-PRVSA---LDVVAEpllERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1443 STGLDPEGQQQIWQAIRAIIkntDRG-ALLT-THYMAEAEALCDRV 1486
Cdd:COG4778 180 TASLDAANRAVVVELIEEAK---ARGtAIIGiFHDEEVREAVADRV 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
481-670 |
3.86e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 65.32 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGKPNKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLsVPTKGSVTIYNNNLSEMAdLENILRIAG 560
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 561 VCPQANVQFDFlTVRENLRLFAkirgippQDVEKEVQRVLLELEMKNIQNILAQNL-----------SGGQKRKLTFGIA 629
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYE-------QWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 630 ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFS 670
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1305-1493 |
3.86e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 61.33 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdtpgfLGYCPQENalW-PNLTVKEHLeIFaa 1383
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP--WiQNGTIRENI-LF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1384 vrGLRKSHAavaitRLADALK---LQDQLKSPVK-----------TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 1449
Cdd:cd03250 89 --GKPFDEE-----RYEKVIKacaLEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254911033 1450 GQQQIWQ-AIRAIIKNtDRGALLTTHYMAEAEAlCDRVAILVSGR 1493
Cdd:cd03250 162 VGRHIFEnCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
478-647 |
4.36e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEM--ADLENI 555
Cdd:PLN03130 1237 SIKFEDVVLRYR--PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LriaGVCPQANVQFDFlTVRENLRLFAKIRGIppqDVEKEVQRV-LLELEMKNIQNILAQ------NLSGGQKRKLTFGI 628
Cdd:PLN03130 1315 L---GIIPQAPVLFSG-TVRFNLDPFNEHNDA---DLWESLERAhLKDVIRRNSLGLDAEvseageNFSVGQRQLLSLAR 1387
|
170
....*....|....*....
gi 254911033 629 AILGDSQIFLLDEPTAGLD 647
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVD 1406
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1303-1508 |
5.27e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.08 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPgflgycpqENALWPNLT-VKEHLEIF 1381
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--------EAALRQAISvVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1382 AAVrgLRKS--HAAVAIT--RLADALK---LQDQLKSPV----------KTLSEGVKRKLCFVLSILGNPSILLLDEPST 1444
Cdd:PRK11160 427 SAT--LRDNllLAAPNASdeALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1445 GLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALcDRVAILVSGRLRCIGSIQHLKSKFG 1508
Cdd:PRK11160 505 GLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1298-1494 |
6.15e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1298 KKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGD---------TKVTaGQVLLKGSREGDTPGFLGYC-----P 1363
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARVT-GDVTLNGEPLAAIDAPRLARlravlP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1364 QENALWPNLTVKEHLEIFA---AVRGLRKSHAAVAITRLADALKLQDQL-KSPVKTLSEGVKRKLCF--VLSIL------ 1431
Cdd:PRK13547 90 QAAQPAFAFSAREIVLLGRyphARRAGALTHRDGEIAWQALALAGATALvGRDVTTLSGGELARVQFarVLAQLwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1432 -GNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
480-691 |
6.94e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 480 RIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVtIYNNNLSEMADLENI---- 555
Cdd:PRK11701 8 SVRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-HYRMRDGQLRDLYALseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 -------------------LRIAgVCPQANVQFDFLTVREnlRLFAKIRgippQDVEKEVQRVllELEMKNIQNiLAQNL 616
Cdd:PRK11701 83 rrrllrtewgfvhqhprdgLRMQ-VSAGGNIGERLMAVGA--RHYGDIR----ATAGDWLERV--EIDAARIDD-LPTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 617 SGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGR 691
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1300-1541 |
7.44e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkGSREgDTPGF-----------LGYCPQ--EN 1366
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERV-ITAGKknkklkplrkkVGIVFQfpEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1367 ALW-----------P-NLTVKEHleifaavRGLRKSHAAVAITRLADALkLQdqlKSPVKtLSEGVKRKLCF--VLSIlg 1432
Cdd:PRK13634 97 QLFeetvekdicfgPmNFGVSEE-------DAKQKAREMIELVGLPEEL-LA---RSPFE-LSGGQMRRVAIagVLAM-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1433 NPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKfgKDYL 1512
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD--PDEL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1513 LEMKV---------KTLEQ------------VEPLNTEILRLFPQASRQE 1541
Cdd:PRK13634 241 EAIGLdlpetvkfkRALEEkfgisfpkpcltLEELAHEVVQLLRKGGHES 290
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
465-693 |
7.78e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 7.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 465 SFEPVSPEFHGKESIRIRNISKEYKGKPnKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGlSVPTKGSVTIYNN 544
Cdd:TIGR02633 244 SLYPHEPHEIGDVILEARNLTCWDVINP-HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFIN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 545 nlSEMADLENILRI--AGVC--PQANVQ---FDFLTVRENLRL-----FAKIRGIPPQDVEKEVQRVLLELEMKNIQNIL 612
Cdd:TIGR02633 322 --GKPVDIRNPAQAirAGIAmvPEDRKRhgiVPILGVGKNITLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 613 A-QNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQfMDEADILADRKVFISN 689
Cdd:TIGR02633 400 PiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGE 478
|
....
gi 254911033 690 GRLK 693
Cdd:TIGR02633 479 GKLK 482
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1273-1493 |
7.90e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1273 DEKPVIIASCLRKEYAGKqkhclskkkakIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsRE 1352
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPR-----------KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM-RD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1353 GDTPG----------FL-----GYCPQ--ENALWPNLT----VKEHL---------EIFA-AVRGLRKshaaVAItrlaD 1401
Cdd:PRK11701 70 GQLRDlyalseaerrRLlrtewGFVHQhpRDGLRMQVSaggnIGERLmavgarhygDIRAtAGDWLER----VEI----D 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1402 ALKLQDQlksPvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEA 1481
Cdd:PRK11701 142 AARIDDL---P-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARL 217
|
250
....*....|..
gi 254911033 1482 LCDRVAILVSGR 1493
Cdd:PRK11701 218 LAHRLLVMKQGR 229
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
481-647 |
8.67e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.37 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVtiynnNLSEMADLenilriaG 560
Cdd:PRK15064 322 VENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSENANI-------G 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 561 VCPQaNVQFDF---LTVRENLRLFAKirgipPQDVEKEVQRVLLEL-----EMKNiqniLAQNLSGGQKRKLTFGIAILG 632
Cdd:PRK15064 386 YYAQ-DHAYDFendLTLFDWMSQWRQ-----EGDDEQAVRGTLGRLlfsqdDIKK----SVKVLSGGEKGRMLFGKLMMQ 455
|
170
....*....|....*
gi 254911033 633 DSQIFLLDEPTAGLD 647
Cdd:PRK15064 456 KPNVLVMDEPTNHMD 470
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1305-1498 |
9.20e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.01 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKM------ISGDTKVTaGQVLLKG----SREGDTPGF---LGYCPQENALWPN 1371
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVE-GEVRLFGrniySPDVDPIEVrreVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKEHLEIFAAVRGLRKSHAAV------AITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTG 1445
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVKSKKELdervewALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1446 LDPEGQQQIWQAIRAIikNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 1498
Cdd:PRK14267 180 IDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
468-703 |
1.11e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 468 PVSPefhGKESIRIRNISKEYKGKPNKiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGlsvptkgsvtiynnNLS 547
Cdd:PLN03232 607 PLQP---GAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELS 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 548 EMADLENILR-IAGVCPQANVQFDfLTVRENLRLFAKI------RGIPPQDVEKEVQ----RVLLELEMKNIqnilaqNL 616
Cdd:PLN03232 669 HAETSSVVIRgSVAYVPQVSWIFN-ATVRENILFGSDFeserywRAIDVTALQHDLDllpgRDLTEIGERGV------NI 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 617 SGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWN--LLKERRADRVVLFSTQ--FMDeadiLADRKVFISNGRL 692
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTRVLVTNQlhFLP----LMDRIILVSEGMI 817
|
250
....*....|.
gi 254911033 693 KCAGSSLFLKK 703
Cdd:PLN03232 818 KEEGTFAELSK 828
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1305-1499 |
1.20e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 60.20 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKST---SL-KMISgdtkVTAGQVLLKG---SREG--DTPGFLGYCPQEnalwPNL--- 1372
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSlllALfRLVE----LSSGSILIDGvdiSKIGlhDLRSRISIIPQD----PVLfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHL---------EIFAAvrgLRKSHAAVAITRLADalKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:cd03244 93 TIRSNLdpfgeysdeELWQA---LERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1444 TGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMaEAEALCDRVAILVSGRLRCIGS 1499
Cdd:cd03244 168 ASVDPETDALIQKTIREAFK--DCTVLTIAHRL-DTIIDSDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1300-1499 |
1.31e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQV------LLKGSREGDTP------GFLGYCPqENA 1367
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivVSSTSKQKEIKpvrkkvGVVFQFP-ESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1368 LWPNLTVKEhLEIFAAVRGLRKSHAAVAITRLADALKLQDQL--KSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPSTG 1445
Cdd:PRK13643 97 LFEETVLKD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFweKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1446 LDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:PRK13643 175 LDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1305-1474 |
1.36e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.33 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGdtKVTAGQVllkgsrEGDT--PGF----------LGYCPQENALWPNL 1372
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI------EGDIriSGFpkkqetfariSGYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHLeIFAAVRGLRKSHAAVAITRLADA---LKLQDQLKSP------VKTLSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:PLN03140 969 TVRESL-IYSAFLRLPKEVSKEEKMMFVDEvmeLVELDNLKDAivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190
....*....|....*....|....*....|.
gi 254911033 1444 TGLDPEGQQQIWQAIRAIIkNTDRGALLTTH 1474
Cdd:PLN03140 1048 SGLDARAAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
498-682 |
1.75e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSG--------LSVPTKGSVTIYNNNLSEMaDLENILRIAGVCPQANVQ- 568
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAI-DAPRLARLRAVLPQAAQPa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 569 FDFlTVRENLRL----FAKIRGIPPQDVEKEVQRVlleLEMKNIQNILAQN---LSGGQKRKLTFGIAI---------LG 632
Cdd:PRK13547 96 FAF-SAREIVLLgrypHARRAGALTHRDGEIAWQA---LALAGATALVGRDvttLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 633 DSQIFLLDEPTAGLDPFSRHRV----------WNL----------LKERRADRVVLFStqfmdEADILAD 682
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLldtvrrlardWNLgvlaivhdpnLAARHADRIAMLA-----DGAIVAH 236
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
493-647 |
1.97e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 493 NKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSG---LSVpTKGSVTIYNNNLSEM-----ADL------ENILRI 558
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKI-LEGDILFKGESILDLepeerAHLgiflafQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQanvqfDFLTVRENLRLfaKIRGIPPQDVEKEVQRVLLELEMKNIQNI-LAQNL----SGGQKRKLTFGIAILGD 633
Cdd:CHL00131 97 PGVSNA-----DFLRLAYNSKR--KFQGLPELDPLEFLEIINEKLKLVGMDPSfLSRNVnegfSGGEKKRNEILQMALLD 169
|
170
....*....|....
gi 254911033 634 SQIFLLDEPTAGLD 647
Cdd:CHL00131 170 SELAILDETDSGLD 183
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1305-1494 |
2.54e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-------REGDTPGF-----------LGYCPQEN 1366
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKVAdknqlrllrtrLTMVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1367 ALWPNLTVKEH-LEIFAAVRGLRKSHAAVAITRLADALKLQD--QLKSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:PRK10619 102 NLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1444 TGLDPEgqqQIWQAIRAIIKNTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK10619 181 SALDPE---LVGEVLRIMQQLAEEGKtmVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
493-648 |
2.64e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 493 NKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIyNNNLSEMADLENILRIAGVCPQANVQFDFL 572
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 573 tvrENLRLFAKIRGIPPQDVEKEVqrvLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDP 648
Cdd:PRK13543 101 ---ENLHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1297-1473 |
2.99e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1297 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSREGDT--PGFLGYCPQENALWPNL 1372
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvTTGVITGGDRLVNGRPLDSsfQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 TVKEHLEIFAAVR---GLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGV----KRKLCFVLSILGNPSILL-LDEPST 1444
Cdd:TIGR00956 852 TVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190
....*....|....*....|....*....|
gi 254911033 1445 GLDpegQQQIWQAIRAIIKNTDRG-ALLTT 1473
Cdd:TIGR00956 932 GLD---SQTAWSICKLMRKLADHGqAILCT 958
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1305-1499 |
3.66e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.58 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP-----GFLGYCPQENALWPNlTVKEHLE 1379
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPledlrSSLTIIPQDPTLFSG-TIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1380 IFAavrglRKSHAavaitRLADALKLqdqlKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 1459
Cdd:cd03369 104 PFD-----EYSDE-----EIYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1460 AIIKNTdrgALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:cd03369 170 EEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1301-1499 |
4.29e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG-----DTKVTA-GQVLLKGSREGDTPGF-----LGYCPQENALW 1369
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKIKVdGKVLYFGKDIFQIDAIklrkeVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNLTVKEHLEIFAAVRGLRKSHAAVAIT-----RLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 1444
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVeeclrKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1445 GLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 1499
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1305-1546 |
5.27e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.10 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKST----SLKMIS--GDTK---VTAGQVLLKGSREGdtpgfLGYCPQENALWPNlTVK 1375
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNteGDIQidgVSWNSVPLQKWRKA-----FGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHLEIFAavrglrkSHAAVAITRLADAL-----------KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 1444
Cdd:cd03289 95 KNLDPYG-------KWSDEEIWKVAEEVglksvieqfpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1445 GLDPegqqQIWQAIRAIIKN--TDRGALLTTHYMaEAEALCDRVAILVSGRLRCIGSIQHLKSKfgkdyllemkvKTLEQ 1522
Cdd:cd03289 168 HLDP----ITYQVIRKTLKQafADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFK 231
|
250 260
....*....|....*....|....
gi 254911033 1523 VEPLNTEILRLFPQASRQERYSSL 1546
Cdd:cd03289 232 QAISPSDRLKLFPRRNSSKSKRKP 255
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
478-647 |
6.84e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdLENILR 557
Cdd:PLN03232 1234 SIKFEDVHLRYR--PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANVQFDFlTVRENLRLFAKIRGippQDVEKEVQRVLLELEMKNIQNIL-------AQNLSGGQKRKLTFGIAI 630
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIDPFSEHND---ADLWEALERAHIKDVIDRNPFGLdaevsegGENFSVGQRQLLSLARAL 1386
|
170
....*....|....*..
gi 254911033 631 LGDSQIFLLDEPTAGLD 647
Cdd:PLN03232 1387 LRRSKILVLDEATASVD 1403
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1292-1497 |
7.30e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1292 KHCLSKKKAKIatRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------------------SRE 1352
Cdd:PRK10982 254 RNLTSLRQPSI--RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnhnaneainhgfalvTEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1353 GDTPGFLGYCPQE-NALWPNltVKEHLEIFAAVRGLR-KSHAAVAItrlaDALKLQD-QLKSPVKTLSEGVKRKLCFVLS 1429
Cdd:PRK10982 332 RRSTGIYAYLDIGfNSLISN--IRNYKNKVGLLDNSRmKSDTQWVI----DSMRVKTpGHRTQIGSLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1430 ILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNtDRGALLTTHYMAEAEALCDRVAILVSGRLRCI 1497
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
479-641 |
7.61e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.29 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDL----------------TLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIY 542
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDLffrskdgeyhyalnniSFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 543 NNnlsemADLenILRIAGVCPQanvqfdfLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKR 622
Cdd:PRK13545 85 GS-----AAL--IAISSGLNGQ-------LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKS 150
|
170
....*....|....*....
gi 254911033 623 KLTFGIAILGDSQIFLLDE 641
Cdd:PRK13545 151 RLGFAISVHINPDILVIDE 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1305-1475 |
8.03e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 8.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSREGDTPgflgycPQENAlwpnltvkeHLEIFA 1382
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE------PEERA---------HLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1383 AVRglrkshAAVAIT--------RLADALKLQDQLKSPVKTLS--EGVKRKLCFV------LS----------------- 1429
Cdd:CHL00131 89 AFQ------YPIEIPgvsnadflRLAYNSKRKFQGLPELDPLEflEIINEKLKLVgmdpsfLSrnvnegfsggekkrnei 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 1430 ---ILGNPSILLLDEPSTGLDPEGQQQIWQAIRaIIKNTDRGALLTTHY 1475
Cdd:CHL00131 163 lqmALLDSELAILDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHY 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
464-692 |
8.10e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 464 DSFEPVSPEFHGKESIRIRNISKEykgkpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYN 543
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 544 NNLsemaDLENI-----LRIA---------GVCPQanvqfdfLTVREN-----LRLFAKIRGIPPQDVEKEVQRVLLELE 604
Cdd:COG1129 314 KPV----RIRSPrdairAGIAyvpedrkgeGLVLD-------LSIRENitlasLDRLSRGGLLDRRRERALAEEYIKRLR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 605 MK--NIQNiLAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKErRADR---VVLFSTQfMDEADI 679
Cdd:COG1129 383 IKtpSPEQ-PVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE-LAAEgkaVIVISSE-LPELLG 459
|
250
....*....|...
gi 254911033 680 LADRKVFISNGRL 692
Cdd:COG1129 460 LSDRILVMREGRI 472
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1311-1494 |
8.43e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.22 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1311 VRKGEILGLLGHNGAGKSTSLKMI-------SGDTKVtaGQVLLKGSRE-GDTPGFL-------GYCPQENALWPNLTVK 1375
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTARSlSQQKGLIrqlrqhvGFVFQNFNLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EH-LEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 1454
Cdd:PRK11264 104 ENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1455 WQAIRAIIKNtDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK11264 184 LNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1300-1479 |
9.36e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.22 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTpgflgycpqenalwpNLT-VKEHL 1378
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD---------------NFEkLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 EI---------------FAAVRGLrKSHAAV---AITRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSIL 1437
Cdd:PRK13648 86 GIvfqnpdnqfvgsivkYDVAFGL-ENHAVPydeMHRRVSEALKqvdMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254911033 1438 LLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEA 1479
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
481-647 |
9.58e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGKPNKIeaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVT--IYNNNLSEmADLENILRI 558
Cdd:TIGR00956 62 FRKLKKFRDTKTFDI--LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEgvITYDGITP-EEIKKHYRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGV-CPQANVQFDFLTVRENLRLFAKIRGipPQD----VEKEVQRV-LLELEMK----------NIQNILAQNLSGGQKR 622
Cdd:TIGR00956 139 DVVyNAETDVHFPHLTVGETLDFAARCKT--PQNrpdgVSREEYAKhIADVYMAtyglshtrntKVGNDFVRGVSGGERK 216
|
170 180
....*....|....*....|....*
gi 254911033 623 KLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1306-1474 |
1.15e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP-----GFLGYCPQENALWPNlTVKEHLEI 1380
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiyrQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1381 FAAVRglrksHAAVAITRLADALKL----QDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:PRK10247 104 PWQIR-----NQQPDPAIFLDDLERfalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170
....*....|....*...
gi 254911033 1457 AIRAIIKNTDRGALLTTH 1474
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTH 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1300-1532 |
1.32e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.72 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1300 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------SRE-GDTPGFLgycPQENALWPN 1371
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlsSRQlARRLALL---PQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKE--------HLEIFAAVRGLRKSHAAVA-----ITRLADalklqdqlkSPVKTLSEGvKRKLCFVLSILG-NPSIL 1437
Cdd:PRK11231 91 ITVRElvaygrspWLSLWGRLSAEDNARVNQAmeqtrINHLAD---------RRLTDLSGG-QRQRAFLAMVLAqDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1438 LLDEPSTGLDPEGQQQIWQAIRaIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLkskfgkdylleMKV 1517
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV-----------MTP 228
|
250
....*....|....*
gi 254911033 1518 KTLEQVEPLNTEILR 1532
Cdd:PRK11231 229 GLLRTVFDVEAEIHP 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
477-647 |
1.36e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 477 ESIRIRN--I------SKEYKGKPNKIE------ALKDLTLD-----IYEGQITAVLGHSGAGKSTLLNILSGLSVPTKG 537
Cdd:COG1245 316 ENVRIRDepIefevhaPRREKEEETLVEypdltkSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 538 SVtiynnnlsemadlENILRIAgVCPQAnVQFDF-LTVRENLRLFAKiRGIPPQDVEKEVQRVLlelemkNIQNILAQN- 615
Cdd:COG1245 396 EV-------------DEDLKIS-YKPQY-ISPDYdGTVEEFLRSANT-DDFGSSYYKTEIIKPL------GLEKLLDKNv 453
|
170 180 190
....*....|....*....|....*....|....
gi 254911033 616 --LSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:COG1245 454 kdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1303-1503 |
1.49e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGdtkvtagqVLLKGSREGDTPGFLGY----CPQE------------- 1365
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG--------LLAANGRIGGSATFNGReilnLPEKelnklraeqismi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1366 -----NALWPNLTVKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQDQLKS----PvKTLSEGVKRKLCFVLSILGNPS 1435
Cdd:PRK09473 103 fqdpmTSLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1436 ILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1314-1494 |
1.60e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1314 GEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL-----LKGSREGDTPGFlgycpQENALWPNLTVKEHLEIfaavrGLR 1388
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtapLAEAREDTRLMF-----QDARLLPWKKVIDNVGL-----GLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1389 KSHAAVAITRLAdALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP----EGQQQI---WQairai 1461
Cdd:PRK11247 108 GQWRDAALQALA-AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIeslWQ----- 181
|
170 180 190
....*....|....*....|....*....|....*
gi 254911033 1462 ikntDRG--ALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK11247 182 ----QHGftVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1314-1458 |
2.02e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1314 GEILGLLGHNGAGKSTSLKMISGDTKVTAGQV-LLKGSRegdtpgfLGYCPQenalwpnltvkEHLEIfaavrgLRKSHA 1392
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIK-------LGYFAQ-----------HQLEF------LRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1393 AVA-ITRLADALKLQ-------------DQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 1458
Cdd:PRK10636 394 PLQhLARLAPQELEQklrdylggfgfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1311-1489 |
3.18e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1311 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTagqvllkgsregdtpgflgycpQENALWPNLTVkehleifaavrglrks 1390
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----------------------GDNDEWDGITP---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1391 haavaitrladalklqdQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGAL 1470
Cdd:cd03222 64 -----------------VYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170
....*....|....*....
gi 254911033 1471 LTTHYMAEAEALCDRVAIL 1489
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHVF 145
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1306-1494 |
3.79e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFL-------GYCPQENALWPNLTVKEHL 1378
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 eIFAA--VRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 1456
Cdd:PRK09493 99 -MFGPlrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 1457 AIRAIiknTDRG--ALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK09493 178 VMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
477-647 |
3.87e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 477 ESIRIRNISKEYKGKPNKIEA--------------LKDLTLD-----IYEGQITAVLGHSGAGKSTLLNILSGLSVPTKG 537
Cdd:PRK13409 315 ENMRIRPEPIEFEERPPRDESeretlveypdltkkLGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 538 SVTIynnnlsemadlenILRIAgVCPQAnVQFDF-LTVRENLRLFAKIRGIPPqdVEKEVQRVLlelemkNIQNILAQN- 615
Cdd:PRK13409 395 EVDP-------------ELKIS-YKPQY-IKPDYdGTVEDLLRSITDDLGSSY--YKSEIIKPL------QLERLLDKNv 451
|
170 180 190
....*....|....*....|....*....|....
gi 254911033 616 --LSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:PRK13409 452 kdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1303-1525 |
4.20e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAG-------QVLLKGSREGDTPGfLGYCPQENALWPNLTVK 1375
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkEVTFNGPKSSQEAG-IGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHL----EIFAAVRGL--RKSHAAVaiTRLADALKLQDQLKSPVKTLSEGVKR--KLCFVLSIlgNPSILLLDEPSTGLD 1447
Cdd:PRK10762 98 ENIflgrEFVNRFGRIdwKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQmvEIAKVLSF--ESKVIIMDEPTDALT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 1448 PEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLrcIGsiQHLKSKFGKDYLLEMKV-KTLEQVEP 1525
Cdd:PRK10762 174 DTETESLFRVIRE-LKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IA--EREVADLTEDSLIEMMVgRKLEDQYP 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1305-1503 |
4.35e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKST----SLKMISGDTK-----VTAGQVLLKGSREGdtpgfLGYCPQENALWPNlTVK 1375
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTllsaLLRLLSTEGEiqidgVSWNSVTLQTWRKA-----FGVIPQKVFIFSG-TFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHLEIFA--AVRGLRKSHAAVAITRLADAL--KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPegq 1451
Cdd:TIGR01271 1310 KNLDPYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP--- 1386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1452 qQIWQAIRAIIKNT--DRGALLTTHYMaEAEALCDRVAILVSGRLRCIGSIQHL 1503
Cdd:TIGR01271 1387 -VTLQIIRKTLKQSfsNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
510-692 |
4.59e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 510 ITAVLGHSGAGKSTLLNILSGLSVPTKG-----SVTIYNNNLSEMADLENILRIAGVCPQANVQFDfLTVRENLrlFAKI 584
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNV--LAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 585 RG---IPPQDVEKEVQRVLLELEMKN-IQNILAQN---LSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNL 657
Cdd:PRK14271 126 RAhklVPRKEFRGVAQARLTEVGLWDaVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190
....*....|....*....|....*....|....*.
gi 254911033 658 LKErRADRV-VLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK14271 206 IRS-LADRLtVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
502-692 |
4.68e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 502 TLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILriAGV--CPQANVQ---FDFLTVRE 576
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIR--AGImlCPEDRKAegiIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 577 NL-----RLFAKIRGIPPQDVEKE-VQRVLLELEMKNI---QNILaqNLSGGQKRKltfgiAILG-----DSQIFLLDEP 642
Cdd:PRK11288 351 NInisarRHHLRAGCLINNRWEAEnADRFIRSLNIKTPsreQLIM--NLSGGNQQK-----AILGrwlseDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 643 TAGLDPFSRHRVWNLLKERRAD-RVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1321-1474 |
4.77e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1321 GHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-FLGYCPQENALWPNLTVKEHLEIFAAVrglrkSHAAVAITRL 1399
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpYCTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1400 ADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIrAIIKNTDRGALLTTH 1474
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMKANSGGIVLLSSH 181
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
496-692 |
5.03e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 496 EALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILR----------IAG----- 560
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARglvylpedrqSSGlylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 561 -----VCPQANVQFDFL--TVRENLRL--FAKIRGIPPQDVEKEVQRvllelemkniqnilaqnLSGGQKRKLTFGIAIL 631
Cdd:PRK15439 357 plawnVCALTHNRRGFWikPARENAVLerYRRALNIKFNHAEQAART-----------------LSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 632 GDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
465-692 |
5.90e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 465 SFEPVSPEFHGKESIRIRNISKEYKGKpnkieaLKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNN 544
Cdd:PRK09700 252 AMKENVSNLAHETVFEVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 545 NLSEMADLENILRIAGVCPQA---NVQFDFLTVRENLRLFAKIR--------GIPPQDVEK---EVQRVLLELEMKNI-Q 609
Cdd:PRK09700 326 DISPRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKdggykgamGLFHEVDEQrtaENQRELLALKCHSVnQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 610 NIlaQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRAD-RVVLFSTQFMDEADILADRKVFIS 688
Cdd:PRK09700 406 NI--TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFC 483
|
....
gi 254911033 689 NGRL 692
Cdd:PRK09700 484 EGRL 487
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
479-692 |
5.92e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkiEALKDLTLDIYEGQITAVLGHSGAGKS----TLLNIL-SGLSVpTKGSVTIYNNNLSEmADLE 553
Cdd:PRK10418 5 IELRNIALQAAQ-----PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAP-CALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 554 NILrIAGVCPQANVQFDFL-TVRENLRLFAKIRGIPPQDveKEVQRVLLELEMKNIQNIL---AQNLSGGQKRKLTFGIA 629
Cdd:PRK10418 78 GRK-IATIMQNPRSAFNPLhTMHTHARETCLALGKPADD--ATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 630 ILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRV--VLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1306-1449 |
6.06e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsreGDTPGfLGYCPQE-NALWPNLTVKE-------H 1377
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-----GETVK-LAYVDQSrDALDPNKTVWEeisggldI 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1378 LEIfaavrGLRK--SHAAVAitrlADALKLQDQLKsPVKTLSEGVKRK--LCFVLSILGNpsILLLDEPSTGLDPE 1449
Cdd:PRK11819 416 IKV-----GNREipSRAYVG----RFNFKGGDQQK-KVGVLSGGERNRlhLAKTLKQGGN--VLLLDEPTNDLDVE 479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1306-1495 |
6.08e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMI--------SGDTKVTAGQVLLKGSREGDTPGfLGYCPQE---NALWPNLTV 1374
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypgrwEGEIFIDGKPVKIRNPQQAIAQG-IAMVPEDrkrDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1375 KEH-----LEIFAAVRGLRKSHAAVAITRLADALKLQ-DQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 1448
Cdd:PRK13549 359 GKNitlaaLDRFTGGSRIDDAAELKTILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 1449 EGQQQIWQAIRAIIKntdRGA--LLTTHYMAEAEALCDRVAILVSGRLR 1495
Cdd:PRK13549 439 GAKYEIYKLINQLVQ---QGVaiIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1305-1505 |
7.72e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 55.63 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllKGSregdtpGFLGYCPQENALWPNlTVKEHLeIFAAV 1384
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHS------GRISFSSQFSWIMPG-TIKENI-IFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1385 RGLRKSHAAVAITRL-ADALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQA-I 1458
Cdd:cd03291 124 YDEYRYKSVVKACQLeEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScV 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254911033 1459 RAIIKNTDRgaLLTTHYMaEAEALCDRVAILVSGRLRCIGSIQHLKS 1505
Cdd:cd03291 204 CKLMANKTR--ILVTSKM-EHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
489-647 |
7.97e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.87 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 489 KGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGsvtiynnnlsEMADLENIlrIAGVCPQANVQ 568
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQPGI--KVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 569 FDFLTVRENLRL-FAKIRGI-------------PPQDVEKevqrvLLElEMKNIQNILA--------------------- 613
Cdd:TIGR03719 80 DPTKTVRENVEEgVAEIKDAldrfneisakyaePDADFDK-----LAA-EQAELQEIIDaadawdldsqleiamdalrcp 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254911033 614 ------QNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:TIGR03719 154 pwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
498-690 |
8.41e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSG--LSVPTKGSVTIYNNNL-SEMADLENILRIAgvcpqanvqfDFLTV 574
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFgREASLIDAIGRKG----------DFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 575 REnlrlfakirgippqdvekevqrVLLELEMKNIQNILA--QNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRH 652
Cdd:COG2401 116 VE----------------------LLNAVGLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 653 RV-WNLLKE-RRADRVVLFSTQFMD-EADILADRKVFISNG 690
Cdd:COG2401 174 RVaRNLQKLaRRAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1303-1494 |
8.81e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.56 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGD--------TPGFLGYCPqENALWP 1370
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDkyirpvrkRIGMVFQFP-ESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 NlTVKEhlEIFAAVRGLRKSHAAVAitrlADALKLQDQL--------KSPVKtLSEGVKRKLCFVlSILG-NPSILLLDE 1441
Cdd:PRK13646 101 D-TVER--EIIFGPKNFKMNLDEVK----NYAHRLLMDLgfsrdvmsQSPFQ-MSGGQMRKIAIV-SILAmNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1442 PSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1306-1495 |
8.97e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTK-VTAGQVLLKGsREGDTPGFLGYCPQENALWP-------------- 1370
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFING-KPVDIRNPAQAIRAGIAMVPedrkrhgivpilgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1371 --NLTVKEhLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKS-PVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 1447
Cdd:TIGR02633 357 gkNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254911033 1448 PEGQQQIWQAIRAIIKntdRGA--LLTTHYMAEAEALCDRVAILVSGRLR 1495
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
507-682 |
9.81e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.07 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 507 EGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVT--------IYNNNLSEMADLENILRIAGVCPQANVQF-DFL----- 572
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPQYvDLIpkavk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 573 -TVRENLRlfakirgippQDVEKEVQRVLLE-LEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFS 650
Cdd:cd03236 105 gKVGELLK----------KKDERGKLDELVDqLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|...
gi 254911033 651 RHRVWNLLKER-RADRVVLFSTQFMDEADILAD 682
Cdd:cd03236 175 RLNAARLIRELaEDDNYVLVVEHDLAVLDYLSD 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1301-1511 |
1.14e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTS----LKMISGDTKVT-AGQVLLKGSREGDTPgflgYCPQ--------ENA 1367
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINSQGEIWfDGQPLHNLNRRQLLP----VRHRiqvvfqdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1368 LWPNLTVkehLEIFAavRGLRKSHAAV-AITRLADALKLQDQLKSPVKT-------LSEGVKRKLCFVLSILGNPSILLL 1439
Cdd:PRK15134 375 LNPRLNV---LQIIE--EGLRVHQPTLsAAQREQQVIAVMEEVGLDPETrhrypaeFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1440 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDY 1511
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
479-660 |
1.19e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.80 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKP-----NKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLsEMADL- 552
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 553 ---ENILRI-----AGVCPQANV-QFDFLTVRENLRLfakirgiPPQDVEKEVQRVLLELEMKNIQ-NILAQNLSGGQKR 622
Cdd:PRK15112 84 yrsQRIRMIfqdpsTSLNPRQRIsQILDFPLRLNTDL-------EPEQREKQIIETLRQVGLLPDHaSYYPHMLAPGQKQ 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 254911033 623 KLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE 660
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1311-1489 |
1.24e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1311 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQ-------ENALWPNLTVKEHLEIFAA 1383
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQnyftkllEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1384 VRG-----LRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 1458
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170 180 190
....*....|....*....|....*....|.
gi 254911033 1459 RAIIKNtDRGALLTTHYMAEAEALCDRVAIL 1489
Cdd:cd03236 183 RELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1305-1376 |
1.41e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.32 E-value: 1.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-----FLGYCPQENALWPNLTVKE 1376
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakRLAILRQENHINSRLTVRE 94
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
480-530 |
1.41e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 1.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 480 RIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSG 530
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1494 |
2.02e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.86 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENA--------------- 1367
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfkelrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1368 --LWPNLTV-KEHLE---IFAAVR-GLRKSHAAVAITRLADALKLQDQL--KSPVKtLSEGVKRKLCF--VLSIlgNPSI 1436
Cdd:PRK13631 121 vfQFPEYQLfKDTIEkdiMFGPVAlGVKKSEAKKLAKFYLNKMGLDDSYleRSPFG-LSGGQKRRVAIagILAI--QPEI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1437 LLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
479-646 |
2.27e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGS-------VTIYNNNLSEMAD 551
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkeVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 552 LENILRIAGVCPQanvqfdfLTVRENL---RLFAKIRG-IPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFG 627
Cdd:PRK10762 81 IGIIHQELNLIPQ-------LTIAENIflgREFVNRFGrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170
....*....|....*....
gi 254911033 628 IAILGDSQIFLLDEPTAGL 646
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDAL 172
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
498-658 |
2.50e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADleniLRIAGVCPQANVQFDfLTVREN 577
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK----PYCTYIGHNLGLKLE-MTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 578 LRLFAKIrgippQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNL 657
Cdd:PRK13541 91 LKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
.
gi 254911033 658 L 658
Cdd:PRK13541 166 I 166
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
497-692 |
2.54e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 497 ALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENIL----------RIAGVcpQAN 566
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINhgfalvteerRSTGI--YAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 567 VQFDFLTVRENLRLF-AKIRGIPPQDVEKEVQRVLLELEMKN-IQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTA 644
Cdd:PRK10982 341 LDIGFNSLISNIRNYkNKVGLLDNSRMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 645 GLDPFSRHRVWNLLKE-RRADRVVLFSTQFMDEADILADRKVFISNGRL 692
Cdd:PRK10982 421 GIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
498-655 |
3.00e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.09 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTiYNNNLSEMADL---------ENIlrIAGVCPQanvQ 568
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGRISFSSQFswimpgtikENI--IFGVSYD---E 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 569 FDFLTVRENLRLFAKIRGIPPQDvekevQRVLLELEMkniqnilaqNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDP 648
Cdd:cd03291 127 YRYKSVVKACQLEEDITKFPEKD-----NTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*..
gi 254911033 649 FSRHRVW 655
Cdd:cd03291 193 FTEKEIF 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
468-647 |
3.01e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 468 PVSPEFhGKESIRIRNISKEYKGKPnkieALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTI------ 541
Cdd:TIGR03719 313 PPGPRL-GDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvkl 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 542 -Y----------NNNL-SEMADLENILRIAG--VCPQANV-QFDFltvrenlrlfakiRGippQDVEKEVqrvllelemk 606
Cdd:TIGR03719 388 aYvdqsrdaldpNKTVwEEISGGLDIIKLGKreIPSRAYVgRFNF-------------KG---SDQQKKV---------- 441
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 607 niqnilaQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:TIGR03719 442 -------GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1273-1349 |
4.04e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.97 E-value: 4.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 1273 DEKPVIIASCLRKEYAGKQKhCLSKKKAKI-ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG 1349
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGG-LFGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1301-1494 |
4.09e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.12 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLK-------MISGdTKVTaGQVLLKG----SREGDTPGF---LGYCPQ-- 1364
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPG-ARVE-GEILLDGediyDPDVDVVELrrrVGMVFQkp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1365 --------ENALWP----NLTVKEHLEifAAV-RGLRKshAAvaitrLADALKlqDQLKSPVKTLSEGVKRKLCFVLSIL 1431
Cdd:COG1117 102 npfpksiyDNVAYGlrlhGIKSKSELD--EIVeESLRK--AA-----LWDEVK--DRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 1432 GNPSILLLDEPSTGLDPEGQQQIWQAIR------AIIkntdrgalLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILelkkdyTIV--------IVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1307-1508 |
4.18e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdtpgfLGYCPQEnALWPNLTVKEHLEIFAAVRG 1386
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ-AWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1387 LRKSHAAVAITRLAD--ALKLQDQLKSPVK--TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI---R 1459
Cdd:TIGR00957 728 KYYQQVLEACALLPDleILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpE 807
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 1460 AIIKNTDRgaLLTTHYMAEAEALcDRVAILVSGRLRCIGSIQHLKSKFG 1508
Cdd:TIGR00957 808 GVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1307-1495 |
4.59e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTaGQVLLKGSREgdtpgFLGYC-------------------PQENa 1367
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVE-----FFNQNiyerrvnlnrlrrqvsmvhPKPN- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1368 LWPnLTVKEHLEIFAAVRGLRKSHAAVAITRLA-DALKLQDQLKSPVKT----LSEGVKRKLCFVLSILGNPSILLLDEP 1442
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESAlKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1443 STGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLR 1495
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
477-654 |
5.78e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 477 ESIRIRNISKEYKGKPNkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENIL 556
Cdd:PTZ00265 381 KKIQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQ----------ANVQFDFLTVR-----------------ENLRLFAKIRGIPPQDVEKEVQRV----LLELEm 605
Cdd:PTZ00265 460 SKIGVVSQdpllfsnsikNNIKYSLYSLKdlealsnyynedgndsqENKNKRNSCRAKCAGDLNDMSNTTdsneLIEMR- 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 606 KNIQNIL-------------------------------AQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRV 654
Cdd:PTZ00265 539 KNYQTIKdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1306-1494 |
9.16e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.44 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREGD------TPGFLGYCPqENALWPNlT 1373
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKNKDikqirkKVGLVFQFP-ESQLFEE-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 VKEHLEIFAAVRGLRKSHA-AVAITRLAdALKLQDQL--KSPVKtLSEGVKRKLCfVLSILG-NPSILLLDEPSTGLDPE 1449
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAeALAREKLA-LVGISESLfeKNPFE-LSGGQMRRVA-IAGILAmEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254911033 1450 GQQQIWQairaIIKNTDRGAL---LTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK13649 180 GRKELMT----LFKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1303-1493 |
9.20e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTK----VTAGQV------LLKGS-RE-----GDTPGFLGYCPQeN 1366
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMrfddidLLRLSpRErrklvGHNVSMIFQEPQ-S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1367 ALWPNLTVKEHLeiFAAVRG------------LRKSHAAVAITRLAdaLK-LQDQLKSPVKTLSEGVKRKLCFVLSILGN 1433
Cdd:PRK15093 101 CLDPSERVGRQL--MQNIPGwtykgrwwqrfgWRKRRAIELLHRVG--IKdHKDAMRSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1434 PSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
479-647 |
9.56e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMAdLENILRI 558
Cdd:TIGR00957 1285 VEFRNYCLRYR--EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG-LHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 559 AGVCPQANVQFDFlTVRENLRLFAkirgippQDVEKEVqrvLLELEMKNIQNILA--------------QNLSGGQKRKL 624
Cdd:TIGR00957 1362 ITIIPQDPVLFSG-SLRMNLDPFS-------QYSDEEV---WWALELAHLKTFVSalpdkldhecaeggENLSVGQRQLV 1430
|
170 180
....*....|....*....|...
gi 254911033 625 TFGIAILGDSQIFLLDEPTAGLD 647
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVD 1453
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1305-1506 |
1.30e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.38 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllKGSregdtpGFLGYCPQENALWPNlTVKEHLEIFAAV 1384
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHS------GRISFSPQTSWIMPG-TIKDNIIFGLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1385 RGLRKSHAAVAITRLADALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQA-IR 1459
Cdd:TIGR01271 514 DEYRYTSVIKACQLEEDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLC 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254911033 1460 AIIKNTDRgaLLTTHYMaEAEALCDRVAILVSGRLRCIGSIQHLKSK 1506
Cdd:TIGR01271 594 KLMSNKTR--ILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1306-1479 |
1.37e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGD-TKVTAGQVLLKGSREG------DTPGFLGYCpqENALwpnltvkeHL 1378
Cdd:PRK10938 278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhPQGYSNDLTLFGRRRGsgetiwDIKKHIGYV--SSSL--------HL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 E--IFAAVRGLRKS--------HAAV--AITRLA----DALKLQDQL-KSPVKTLSEGVKRKLCFVLSILGNPSILLLDE 1441
Cdd:PRK10938 348 DyrVSTSVRNVILSgffdsigiYQAVsdRQQKLAqqwlDILGIDKRTaDAPFHSLSWGQQRLALIVRALVKHPTLLILDE 427
|
170 180 190
....*....|....*....|....*....|....*...
gi 254911033 1442 PSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEA 1479
Cdd:PRK10938 428 PLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1301-1451 |
1.65e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------SRE-GDTPGFLGycpqENALWP-N 1371
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaSKEvARRIGLLA----QNATTPgD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKE--------HLEIFAAvrgLRKSHAAvAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPS 1443
Cdd:PRK10253 96 ITVQElvargrypHQPLFTR---WRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
....*...
gi 254911033 1444 TGLDPEGQ 1451
Cdd:PRK10253 172 TWLDISHQ 179
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1024-1215 |
2.02e-06 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 52.01 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1024 AFWLILTSAcppYIAMSSVTDYKNRAWFQLRVSGLFPSAYWVGQAMVDIPLYCFVFLFMSLM--DYLFRFPDTMFSIISH 1101
Cdd:pfam12698 169 MIIILIGAA---IIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLlfGIGIPFGNLGLLLLLF 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1102 VIqipcsvgYAISLIFLTYVISFISRKGKKNSGIWSLSFYIITVFSVAVILLAFDVDGTQyyIIFLIPPSTLVGCLILSL 1181
Cdd:pfam12698 246 LL-------YGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQ--WIFSIIPFFSPIDGLLRL 316
|
170 180 190
....*....|....*....|....*....|....
gi 254911033 1182 HLFIGQIfeegQVIEPFLVFLIPFLhVFIFIFTL 1215
Cdd:pfam12698 317 IYGDSLW----EIAPSLIILLLFAV-VLLLLALL 345
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1301-1499 |
2.30e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdtpgfLGYCPQEnALWPNLTVKEHLEI 1380
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--------IAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1381 FAAVRGLRkSHAAVAITRL-ADALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE-GQQQI 1454
Cdd:PTZ00243 744 FDEEDAAR-LADAVRVSQLeADLAQLGGGLETEIGekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVV 822
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254911033 1455 WQAIRAIIKNTDRgaLLTTHYMaEAEALCDRVAILVSGRLRCIGS 1499
Cdd:PTZ00243 823 EECFLGALAGKTR--VLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
491-692 |
2.83e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 491 KPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGL---SVPTKGSVTIYNNNLSEMADLENILRIAgvcpQANV 567
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKldpSLKVSGEITYNGYRLNEFVPRKTSAYIS----QNDV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 568 QFDFLTVRENLRLFA-------------------KIRGIPPqdvEKEVQRVLLELEMKNIQNIL---------------- 612
Cdd:PLN03140 250 HVGVMTVKETLDFSArcqgvgtrydllselarreKDAGIFP---EAEVDLFMKATAMEGVKSSLitdytlkilgldickd 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 613 -------AQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFS-TQFMDEADILAD 682
Cdd:PLN03140 327 tivgdemIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQivHLTEATVLMSlLQPAPETFDLFD 406
|
250
....*....|
gi 254911033 683 RKVFISNGRL 692
Cdd:PLN03140 407 DIILLSEGQI 416
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1303-1494 |
3.08e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 51.99 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKS-TSL---KMISGDTKVTAGQVLLKGS-------------REGDtpgfLGYCPQE 1365
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvTALsilRLLPDPAAHPSGSILFDGQdllglserelrriRGNR----IAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1366 --NALWPNLTVKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQD---QLKSPVKTLSEGVKRKLCFVLSILGNPSILLL 1439
Cdd:COG4172 101 pmTSLNPLHTIGKQIaEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1440 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:COG4172 181 DEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
498-663 |
3.37e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 48.69 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVtiynnnlsEMADLENILRIagvcPQANVqFDFLTVREN 577
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLFL----PQRPY-LPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 578 LRLfakirgiPPQDVekevqrvllelemkniqnilaqnLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNL 657
Cdd:cd03223 84 LIY-------PWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
....*.
gi 254911033 658 LKERRA 663
Cdd:cd03223 134 LKELGI 139
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
498-697 |
4.30e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGlsvptkgsvtiynnNLSEMADLENILR--IAGVcPQANVQFDfLTVR 575
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG--------------ELPPRSDASVVIRgtVAYV-PQVSWIFN-ATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 576 ENLrLFakirGIP--PQDVEKEV-----QRVLLELEMKNIQNILAQ--NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGL 646
Cdd:PLN03130 697 DNI-LF----GSPfdPERYERAIdvtalQHDLDLLPGGDLTEIGERgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 647 DPFSRHRVWN--LLKERRADRVVLFSTQ--FMDEadilADRKVFISNGRLKCAGS 697
Cdd:PLN03130 772 DAHVGRQVFDkcIKDELRGKTRVLVTNQlhFLSQ----VDRIILVHEGMIKEEGT 822
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1303-1494 |
4.42e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG----DTKVTAGQVLLKGS-----REGDTPGFLG------YCPQENA 1367
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQdlqriSEKERRNLVGaevamiFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1368 LWPNLTVKehLEIFAAVR----GLRKSHAAVAItrlaDALKL------QDQLKSPVKTLSEGVKRKLCFVLSILGNPSIL 1437
Cdd:PRK11022 102 LNPCYTVG--FQIMEAIKvhqgGNKKTRRQRAI----DLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1438 LLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 1494
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1303-1493 |
4.55e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGdtkvtagqVLLKGSREGD------TPGF--------LGYC--PQEN 1366
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG--------VYPHGSYEGEilfdgeVCRFkdirdseaLGIViiHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1367 ALWPNLTVKEHleIF----AAVRGLRKSHAavAITRLADALK---LQDQLKSPVKTLseGV-KRKLCFVLSILG-NPSIL 1437
Cdd:NF040905 88 ALIPYLSIAEN--IFlgneRAKRGVIDWNE--TNRRARELLAkvgLDESPDTLVTDI--GVgKQQLVEIAKALSkDVKLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1438 LLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
481-691 |
6.30e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKS-TLLNILSGLSVP----TKGSVTIYNNNLSEmADlENI 555
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH-AS-EQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LR------IAGVCPQANVQFDFL-TVRENL-RLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILA---QNLSGGQKRKL 624
Cdd:PRK15134 86 LRgvrgnkIAMIFQEPMVSLNPLhTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 625 TFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQFMDEADILADRKVFISNGR 691
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1303-1349 |
7.79e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 7.79e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG 1349
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1306-1506 |
9.19e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.52 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTK----VTA------GQVLLKGS---------REgdtpgfLGYCPQE- 1365
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTAdrfrwnGIDLLKLSprerrkiigRE------IAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1366 -NALWPNLTVKEHLE----------IFAAVRGLRKSHAA-----VAITrladalKLQDQLKSPVKTLSEGVKRKLCFVLS 1429
Cdd:COG4170 99 sSCLDPSAKIGDQLIeaipswtfkgKWWQRFKWRKKRAIellhrVGIK------DHKDIMNSYPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254911033 1430 ILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSK 1506
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1307-1531 |
9.89e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 9.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREG--DTPGFLGYCPQENALWPNlTVKEHLEIF 1381
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvAKFGltDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1382 AA------VRGLRKSHAAVAITRlaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIW 1455
Cdd:PLN03232 1334 SEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254911033 1456 QAIRAIIKNTdrgALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDYLlemkvKTLEQVEPLNTEIL 1531
Cdd:PLN03232 1412 RTIREEFKSC---TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFF-----RMVHSTGPANAQYL 1479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
468-693 |
1.40e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 468 PVSPEFHGKESIRIRNISKEYKGKPNkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGlSVPTKGSVTIYNNNls 547
Cdd:PRK13549 249 PREPHTIGEVILEVRNLTAWDPVNPH-IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRWEGEIFIDG-- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 548 EMADLENILR-----IA---------GVCPQANVQFDFLTVreNLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILA 613
Cdd:PRK13549 325 KPVKIRNPQQaiaqgIAmvpedrkrdGIVPVMGVGKNITLA--ALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 614 -QNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE--RRADRVVLFSTQfMDEADILADRKVFISNG 690
Cdd:PRK13549 403 iARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlvQQGVAIIVISSE-LPEVLGLSDRVLVMHEG 481
|
...
gi 254911033 691 RLK 693
Cdd:PRK13549 482 KLK 484
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
495-530 |
1.74e-05 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 48.57 E-value: 1.74e-05
10 20 30
....*....|....*....|....*....|....*.
gi 254911033 495 IEALKDLtLdiyEGQITAVLGHSGAGKSTLLNILSG 530
Cdd:COG1162 157 LDELREL-L---KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
405-672 |
1.83e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.54 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 405 VFDAFLYLALMMYFEKVLPNEYghqhSPLFFLKSSFWLQTRKPAHVILEDGIDPVPSSGDSFE--------------PVS 470
Cdd:pfam13304 15 LLEALRFLADFDALVIGLTDER----SRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRygldleredveeklSSK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 471 PEFHGKESIRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVL---GHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLS 547
Cdd:pfam13304 91 PTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSElsdLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 548 EMADLENILRIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLEleMKNIQNILAQNLSGGQKRKLTFG 627
Cdd:pfam13304 171 LAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLE--NGGGGELPAFELSDGTKRLLALL 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 254911033 628 IAILGDSQ---IFLLDEPTAGLDPFSRHRVWNLLKERRADRV-VLFSTQ 672
Cdd:pfam13304 249 AALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
482-646 |
1.98e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 482 RNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLsVPT---KGSVTIYNNNL-------SEMAD 551
Cdd:PRK13549 9 KNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqasnirdTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 552 LENILRIAGVCPQanvqfdfLTVRENLRLFAKIR--GIPPQD-VEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGI 628
Cdd:PRK13549 84 IAIIHQELALVKE-------LSVLENIFLGNEITpgGIMDYDaMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170
....*....|....*...
gi 254911033 629 AILGDSQIFLLDEPTAGL 646
Cdd:PRK13549 157 ALNKQARLLILDEPTASL 174
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
495-530 |
2.00e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 47.39 E-value: 2.00e-05
10 20 30
....*....|....*....|....*....|....*.
gi 254911033 495 IEALKDLtLdiyEGQITAVLGHSGAGKSTLLNILSG 530
Cdd:cd01854 76 LDELREL-L---KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
482-647 |
2.04e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 482 RNISKEYkgkPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNnlsemadleniLRIaGV 561
Cdd:PRK11819 10 NRVSKVV---PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG-----------IKV-GY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 562 CPQANVQFDFLTVRENLRL-FAKIRGI-------------PPQDVEKevqrvLLElEMKNIQNILAQ------------- 614
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEEgVAEVKAAldrfneiyaayaePDADFDA-----LAA-EQGELQEIIDAadawdldsqleia 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254911033 615 --------------NLSGGQKRKltfgIAI----LGDSQIFLLDEPTAGLD 647
Cdd:PRK11819 149 mdalrcppwdakvtKLSGGERRR----VALcrllLEKPDMLLLDEPTNHLD 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1312-1464 |
2.12e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1312 RKGEILGLLGHNGAGKSTSLKMISG---------DTKVTAGQVL-----------LKGSREGDTPgfLGYCPQENALWPN 1371
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGelkpnlgdyDEEPSWDEVLkrfrgtelqdyFKKLANGEIK--VAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 L---TVKEHLEIfAAVRGlrkshaavAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDp 1448
Cdd:COG1245 175 VfkgTVRELLEK-VDERG--------KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD- 244
|
170
....*....|....*...
gi 254911033 1449 egqqqIWQAIRA--IIKN 1464
Cdd:COG1245 245 -----IYQRLNVarLIRE 257
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
479-667 |
2.36e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.91 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKS-TLLNIL----SGLSVPTkGSVTIYNNNLSEM--AD 551
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQDLLGLseRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 552 LENI--LRIAGVcpqanvqfdF----------LTV----RENLRLfakIRGIPPQDVEKEVQRVLLELEMKNIQNILAQ- 614
Cdd:COG4172 86 LRRIrgNRIAMI---------FqepmtslnplHTIgkqiAEVLRL---HRGLSGAAARARALELLERVGIPDPERRLDAy 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 615 --NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKE-------------------RR-ADRVV 667
Cdd:COG4172 154 phQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDlqrelgmalllithdlgvvRRfADRVA 228
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1416-1474 |
2.48e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.15 E-value: 2.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254911033 1416 LSEGVKRKLCFVLSIL---GNPSILLLDEPSTGLDPEGQQQIWQAIRaIIKNTDRGALLTTH 1474
Cdd:pfam13304 237 LSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLK-ELSRNGAQLILTTH 297
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
477-666 |
2.68e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 477 ESIRIRNISKEYKgkPNKIEalkdltldiYEGQITAVLGHSGAGKSTllnILSGLSVPTKGSVTiynNNLSEMADLENIL 556
Cdd:cd03240 2 DKLSIRNIRSFHE--RSEIE---------FFSPLTLIVGQNGAGKTT---IIEALKYALTGELP---PNSKGGAHDPKLI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 557 RIAGVCPQANVQF-----DFLTVRENLRLFAKIRGIPPQDVEKevqrvLLELEMKniqnilaqNLSGGQKRKLTFGI--- 628
Cdd:cd03240 65 REGEVRAQVKLAFenangKKYTITRSLAILENVIFCHQGESNW-----PLLDMRG--------RCSGGEKVLASLIIrla 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254911033 629 ---AILGDSQIFLLDEPTAGLDPFSR-HRVWNLLKERRADRV 666
Cdd:cd03240 132 laeTFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKN 173
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
498-647 |
3.79e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 498 LKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVtiynnnlsemadlENILRIAgVCPqanvQFDFL---TV 574
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRIS-FSP----QTSWImpgTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 575 RENLRLFAKIRGIPPQDVEKEVQrvlLELEMKNIQN----ILAQ---NLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLD 647
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQ---LEEDIALFPEkdktVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
616-690 |
3.92e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.81 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 616 LSGGQKRKLT----FGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRA-DRVVLFST---QFMDEADILADRKVFI 687
Cdd:cd03227 78 LSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkGAQVIVIThlpELAELADKLIHIKKVI 157
|
...
gi 254911033 688 SNG 690
Cdd:cd03227 158 TGV 160
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
478-647 |
4.05e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 478 SIRIRNISKEYKgkpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLS--VPTKGSVTIYNNNLSEMADLENI 555
Cdd:PRK09580 3 SIKDLHVSVEDK------AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 -----------LRIAGVCPQANVQFDFLTVRenlrlfaKIRGIPPQD-------VEKEVQrvLLELEMKNIQNILAQNLS 617
Cdd:PRK09580 77 gegifmafqypVEIPGVSNQFFLQTALNAVR-------SYRGQEPLDrfdfqdlMEEKIA--LLKMPEDLLTRSVNVGFS 147
|
170 180 190
....*....|....*....|....*....|.
gi 254911033 618 GGQ-KRKLTFGIAILgDSQIFLLDEPTAGLD 647
Cdd:PRK09580 148 GGEkKRNDILQMAVL-EPELCILDESDSGLD 177
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
479-660 |
5.28e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 47.76 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGK-------PNKIEALKDLTLDIYEGQITAVLGHSGAGKSTL-LNILsGLsVPTKGSVTIYNNNLSEMA 550
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 551 DLEN-ILRiagvcpqANVQFDF----------LTVR----ENLRLFAkiRGIPPQDVEKEVQRVLLELEMK-NIQNILAQ 614
Cdd:COG4172 354 RRALrPLR-------RRMQVVFqdpfgslsprMTVGqiiaEGLRVHG--PGLSAAERRARVAEALEEVGLDpAARHRYPH 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254911033 615 NLSGGQKRKLtfGIA---ILgDSQIFLLDEPTAGLDPFSRHRVWNLLKE 660
Cdd:COG4172 425 EFSGGQRQRI--AIAralIL-EPKLLVLDEPTSALDVSVQAQILDLLRD 470
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
481-646 |
6.19e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 481 IRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NNLSEMADLENilR 557
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeiDFKSSKEALEN--G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 558 IAGVCPQANvQFDFLTVRENL---RLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDS 634
Cdd:PRK10982 75 ISMVHQELN-LVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170
....*....|..
gi 254911033 635 QIFLLDEPTAGL 646
Cdd:PRK10982 154 KIVIMDEPTSSL 165
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1301-1494 |
7.68e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 47.53 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1301 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTaGQVLLKGS--REGDTP------GFLGYCPQ-------E 1365
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIelRELDPEswrkhlSWVGQNPQlphgtlrD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1366 NAL--WPNLTVKEhleIFAAvrgLRKSHAAVAITRLADAL--KLQDQlkspVKTLSEGVKRKLCFVLSILGNPSILLLDE 1441
Cdd:PRK11174 442 NVLlgNPDASDEQ---LQQA---LENAWVSEFLPLLPQGLdtPIGDQ----AAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254911033 1442 PSTGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEAlCDRVAILVSGRL 1494
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1311-1489 |
8.59e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1311 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLG------------------YCPQENALWPNL 1372
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGtelqnyfkklyngeikvvHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1373 ---TVKEHLEIfAAVRGLRKShaavaitrLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDpe 1449
Cdd:PRK13409 176 fkgKVRELLKK-VDERGKLDE--------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-- 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254911033 1450 gqqqIWQ------AIRAIIKNtdRGALLTTHYMAEAEALCDRVAIL 1489
Cdd:PRK13409 245 ----IRQrlnvarLIRELAEG--KYVLVVEHDLAVLDYLADNVHIA 284
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1305-1494 |
1.10e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSregdtpGFLGYCPQENA--------LWPNLT- 1373
Cdd:PRK09580 18 RGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGK------DLLELSPEDRAgegifmafQYPVEIp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1374 -VKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQ---LKSPVKTLSEGV---------KRKLCFVLSILgNPSILLLD 1440
Cdd:PRK09580 92 gVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKialLKMPEDLLTRSVnvgfsggekKRNDILQMAVL-EPELCILD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 1441 EPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEAL-CDRVAILVSGRL 1494
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNS-LRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRI 224
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
495-530 |
1.21e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 44.45 E-value: 1.21e-04
10 20 30
....*....|....*....|....*....|....*.
gi 254911033 495 IEALKDLtldiYEGQITAVLGHSGAGKSTLLNILSG 530
Cdd:pfam03193 97 IEALKEL----LKGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1302-1487 |
1.45e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.54 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1302 IATRNVSFCVRKGEILGLLGHNGAGKSTSLK-------MISG---DTKVTAGQVLLKGSR--EGDTPGFLGYCPQENALW 1369
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGfrvEGKVTFHGKNLYAPDvdPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1370 PNlTVKEHLEIFAAVRGLRKSHAAVAITRLADAL---KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGL 1446
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGDMDELVERSLRQAAlwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 1447 DPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALCDRVA 1487
Cdd:PRK14243 183 DPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
468-541 |
1.83e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 468 PVSPEFhGKESIRIRNISKEYKGKpnkiEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTI 541
Cdd:PRK11819 315 PPGPRL-GDKVIEAENLSKSFGDR----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
495-535 |
2.11e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 45.20 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 254911033 495 IEALKDLTldiyEGQITAVLGHSGAGKSTLLN-ILSGLSVPT 535
Cdd:PRK00098 155 LDELKPLL----AGKVTVLAGQSGVGKSTLLNaLAPDLELKT 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
479-691 |
2.43e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.59 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 479 IRIRNISKEYKGkpnkIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNN----LSEMADLEN 554
Cdd:TIGR02633 2 LEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGsplkASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 555 ilriAGVC--PQANVQFDFLTVRENLRLFAKI--RGIPPQDVE--KEVQRVLLELEMKNIQNILA-QNLSGGQKRKLTFG 627
Cdd:TIGR02633 78 ----AGIViiHQELTLVPELSVAENIFLGNEItlPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254911033 628 IAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVV-LFSTQFMDEADILADRKVFISNGR 691
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1273-1351 |
3.26e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 45.06 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1273 DEKPVIIASCLRKEYAGKQKHCLSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTS----LKMISgdtkvTAGQVLLK 1348
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFD 345
|
...
gi 254911033 1349 GSR 1351
Cdd:COG4172 346 GQD 348
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1316-1500 |
3.50e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1316 ILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG--FL-------GYCPQENALWPNLTVKEHLEIfaavrG 1386
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLppekrriGYVFQDARLFPHYKVRGNLRY-----G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1387 LRKSHAAV--AITRLadaLKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD-PEGQ------QQIWQA 1457
Cdd:PRK11144 101 MAKSMVAQfdKIVAL---LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRellpylERLARE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254911033 1458 IRAIIkntdrgaLLTTHYMAEAEALCDRVAILVSGRLRCIGSI 1500
Cdd:PRK11144 178 INIPI-------LYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1303-1493 |
3.81e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1303 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------SREGDTPGfLGYCPQENALWPNLTVK 1375
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfksSKEALENG-ISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHLEIFA-AVRGLRKSHAAV--AITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:PRK10982 92 DNMWLGRyPTKGMFVDQDKMyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 254911033 1453 QIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 1493
Cdd:PRK10982 172 HLFTIIRK-LKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1305-1474 |
6.47e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 44.33 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR----EGDTPGFL-----GYCPQENALWPNLTVK 1375
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatlDADALAQLrrehfGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1376 EHLEIFAAVRGL----RKSHAAVAITRLAdalkLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 1451
Cdd:PRK10535 105 QNVEVPAVYAGLerkqRLLRAQELLQRLG----LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180
....*....|....*....|....*.
gi 254911033 1452 QQiwqaIRAIIKN-TDRG--ALLTTH 1474
Cdd:PRK10535 181 EE----VMAILHQlRDRGhtVIIVTH 202
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
263-348 |
1.21e-03 |
|
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 42.11 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 263 AFWLSWGLLYAgFVFIMALSLALVIKSVQFFILTSFMVVFSLFLLYGLSMITLAFLMSALVRKSVLT-GLSVFLLTIFWG 341
Cdd:COG1277 102 GALLVLLLALL-ITFLLALLLGLLLFGSPPPDLGAILGFYLGLLLLGLAFLAIGLFISALTRNQIVAaILAIALWLLLVI 180
|
....*..
gi 254911033 342 SLGFTSL 348
Cdd:COG1277 181 LLAWIVL 187
|
|
| MelB |
COG2211 |
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]; |
1046-1168 |
1.43e-03 |
|
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
Pssm-ID: 441813 [Multi-domain] Cd Length: 447 Bit Score: 42.97 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1046 KNRAWFQLRVSGLFpsaYWVGQAMVDiplycfvFLFMSLMDYLFRFPDTMFSIIShviqipcsVGYAISLIFLTYVISFI 1125
Cdd:COG2211 226 KNRPFLLLLLAYLL---FFLALALVA-------ALLLYYFKYVLGLSAALVGLLL--------ALYFLAALLGAPLWPRL 287
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 254911033 1126 SRK-GKKNSGIWSLSFYIItvfsvAVILLAFdVDGTQYYIIFLI 1168
Cdd:COG2211 288 AKRfGKKKAFIIGLLLAAL-----GLLLLFF-LGPGNLWLLLVL 325
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
482-688 |
1.66e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.64 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 482 RNISKEY---KG---KPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENI 555
Cdd:PRK11308 9 IDLKKHYpvkRGlfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 556 LRiagvcpQANVQFDF------LTVRE------------NLRLFAKIRgipPQDVEKEVQRVLLELE-------Mkniqn 610
Cdd:PRK11308 89 LL------RQKIQIVFqnpygsLNPRKkvgqileeplliNTSLSAAER---REKALAMMAKVGLRPEhydryphM----- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254911033 611 ilaqnLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLlkerradrvvlfstqFMDEADILADRKVFIS 688
Cdd:PRK11308 155 -----FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL---------------MMDLQQELGLSYVFIS 212
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
475-526 |
1.83e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 1.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 254911033 475 GKESIRIRniSKEYKGKPNKIEA-------LKDLTLDIYEGQITAVLGHSGAGKSTLLN 526
Cdd:TIGR00630 596 GRKKIEVP--AERRPGNGKFLTLkgarennLKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1307-1441 |
2.72e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 42.09 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDtpgflgycpqENALWpnltvkeHLEIFAAV-- 1384
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA----------DNREA-------YRQLFSAVfs 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254911033 1385 ------R--GLRKSHAAVAITRLADALKLQDQLK------SPVKtLSEGVKRKLCFVLSILGNPSILLLDE 1441
Cdd:COG4615 414 dfhlfdRllGLDGEADPARARELLERLELDHKVSvedgrfSTTD-LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1414-1477 |
2.89e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 2.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254911033 1414 KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMA 1477
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1420
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
508-691 |
3.51e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.66 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 508 GQITAVLGHSGAGKSTLLNILSGLSVPTKGSVtiynnnlsEMADLENILriagvcpqanvqfdfltvrenlrlfakirgi 587
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------IYIDGEDIL------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 588 ppqdvekevqRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLL-------KE 660
Cdd:smart00382 43 ----------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLK 112
|
170 180 190
....*....|....*....|....*....|....*.
gi 254911033 661 RRADRVVLFSTQFMDEAD-----ILADRKVFISNGR 691
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGpallrRRFDRRIVLLLIL 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1306-1347 |
4.61e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 4.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 254911033 1306 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLL 1347
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1307-1544 |
4.72e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1307 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREG--DTPGFLGYCPQENALWPNlTVKEHLEIF 1381
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiSKFGlmDLRKVLGIIPQAPVLFSG-TVRFNLDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1382 AA------VRGLRKSHAAVAITRlaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDpegqqqiw 1455
Cdd:PLN03130 1337 NEhndadlWESLERAHLKDVIRR--NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-------- 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1456 qaIR--AIIKNTDRGALLTTHYMAEAEAL-----CDRVAILVSGRLRCIGSIQHLKSKFGkdyllEMKVKTLEQVEPLNT 1528
Cdd:PLN03130 1407 --VRtdALIQKTIREEFKSCTMLIIAHRLntiidCDRILVLDAGRVVEFDTPENLLSNEG-----SAFSKMVQSTGAANA 1479
|
250
....*....|....*.
gi 254911033 1529 EILRLFPQASRQERYS 1544
Cdd:PLN03130 1480 QYLRSLVFGGDEDRLA 1495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
606-680 |
4.82e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 606 KNIQNIlaQNLSGGQKrKLT-----FGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADR---VVLFSTQFMDEA 677
Cdd:pfam02463 1070 KGVKNL--DLLSGGEK-TLValaliFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAqfiVISLREEMLEKA 1146
|
...
gi 254911033 678 DIL 680
Cdd:pfam02463 1147 DKL 1149
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1305-1459 |
5.98e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.47 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1305 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTpGF------LGYCPQENALWPNlTVKEHL 1378
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-GLhdlrfkITIIPQDPVLFSG-SLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1379 EIFAAVR------GLRKSHAAVAITRLADalKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 1452
Cdd:TIGR00957 1381 DPFSQYSdeevwwALELAHLKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
....*..
gi 254911033 1453 QIWQAIR 1459
Cdd:TIGR00957 1459 LIQSTIR 1465
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1308-1453 |
6.16e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1308 SFCVRKGEILGLLGHNGAGKSTSLKMISGDTkvtagqVLLKGSREGD--TPGFLGYCPQENAL---W-----------PN 1371
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGEL------PLLSGERQSQfsHITRLSFEQLQKLVsdeWqrnntdmlspgED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 1372 LTVKEHLEIFaavrgLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 1451
Cdd:PRK10938 97 DTGRTTAEII-----QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
..
gi 254911033 1452 QQ 1453
Cdd:PRK10938 172 QQ 173
|
|
| MFS |
cd06174 |
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ... |
260-373 |
9.88e-03 |
|
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.
Pssm-ID: 349949 [Multi-domain] Cd Length: 378 Bit Score: 40.10 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254911033 260 RDPAFW---LSWGLLYAGFVFIMALSLALVIKSVQFFILTSFMVVFSLFLLYGLSMITLAFLMSALVRKSVLTGLSVFLL 336
Cdd:cd06174 201 KNPGLWlllLAIFLVNLAYYSFSTLLPLFLLDLGGLSVAVAGLLLSLFGLAGALGSLLLGLLSDRLIGRKPLLLIGLLLM 280
|
90 100 110
....*....|....*....|....*....|....*..
gi 254911033 337 TIFWGSLGFTSlYRYLPAPVEWTLSLFSPFAFTLGMA 373
Cdd:cd06174 281 ALGLALLLLAP-SLLLLLLLLLLLGFGLGGLLPLSFA 316
|
|
| |
