|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-2349 |
0e+00 |
|
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: 1532.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 10 EIFIPLVLFFILLGLRQKKPTISVKEAFYTAAPLTSAGILPVMQSL-C----PDGQRDEFG-----FLQYANStvtqLLE 79
Cdd:TIGR01257 28 ELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIfCnvnnPCFQSPTPGespgiVSNYNNS----ILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 80 RLHRVVEEGNLFDPVRPSLG---SELEALRQRLEALssgpgtwESHSARPAVSSFSLDSVARDQRELWRFLMQNLSLPNS 156
Cdd:TIGR01257 104 RVYRDFQELLMDAPESQHLGqvwAELRTLSQFMDTL-------RTHPERIAGRGIRIRDILKDEEALTLFLMKNIGLSDS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 157 TAQALLAARVDPSEVYRllfgPLPDLDGKlgflrkqepwsrlgsnpllqmeelllapalleqlTCAPGSGELGRILTMPE 236
Cdd:TIGR01257 177 VVYLLVNSQVRPEQFAY----GVPDLELK----------------------------------DIACSEALLERFIIFSQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 237 GHQVdlQGYRDAVCS-GQATAraQRFSDlaaELRNQLDTAKIAQQLgfdvPNGSDPQPQAPSPQSLPALLGDLLD-AQKL 314
Cdd:TIGR01257 219 RRGA--QTVRDALCSlSQGTL--QWIED---TLYANVDFFKLFHVL----PTLLDSRSQGINLRSWGGILSDMSPrIQEF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 315 LQDVDVLSALALLLPqgacagqasapqasslngLANSTGigansgsnttveegtqspvspasPDTlqgqcsaFVQLWAGL 394
Cdd:TIGR01257 288 IHRPSVQDLLWVTRP------------------LLQNGG-----------------------PET-------FTQLMGIL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 395 QPILCGnnrtiEPEAlrrGNMSSLGFTSKEQRN----LGL---------------------LVHLMTSNP---------- 439
Cdd:TIGR01257 320 SDLLCG-----YPEG---GGSRVFSFNWYEDNNykafLGIdstrkdpiysydkrttsfcnaLIQSLESNPltkiawraak 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 440 -----KILYAPVGSEADRVILKANETFAFVGNVTHYAQVWLNISTEIRSFLEQGrlqqhlqWLQQYVADLQLHPEA---M 511
Cdd:TIGR01257 392 pllmgKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKS-------TQMTMIRDTLQNPTVkdfI 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 512 NLSLEELPPALRQDFSLPNGTALLQQLDTIDNAACGWI------------QFMSKVSVDIFKGFPDEESIVNYTLNQAYQ 579
Cdd:TIGR01257 465 NRQLGEEGITAEAVLNFLYNGPREKQADDMTNFDWRDIfnitdrflrlanQYLECLVLDKFESYDDEVQLTQRALSLLEE 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 580 DNVtvFASVIFQTRK--DGSLPPHVHYKIRQNSSFTEKTNEIRRAYWRPGPNTGGRFYFLY---GFVWIQDMMERAIINT 654
Cdd:TIGR01257 545 NRF--WAGVVFPDMYpwTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYiwgGFAYLQDMVEQGITRS 622
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 655 FVGHDVvEPGNYVQMFPYPCYTRDDFLFVIEHMMPLCMVISWVYSVAMTIQHIVAEKEHRLKEVMKTMGLNNAVHWVAWF 734
Cdd:TIGR01257 623 QMQAEP-PVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWF 701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 735 ITGFVQLSISVTALTAILKYGQVLMHSHVLIIWLFLAVYAVATIMFCFLVSVLYSKAKLASACGGIIYFLSYVPYMYVAI 814
Cdd:TIGR01257 702 LDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFA 781
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 815 REevahDKITAFEKCIASLMSTTAFGLGSKYFALYEVAGVGIQWHTFSQSPVEGDDFNLLLAVTMLMVDTVVYGVLTWYI 894
Cdd:TIGR01257 782 WQ----DRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYL 857
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 895 EAVHPGMYGLPRPWYFPLQKSYWLG----SGRTEawewswpwahtprlSVMEEDQACAMESRHFEETRGMEE---EPTHL 967
Cdd:TIGR01257 858 DQVFPGDYGTPLPWYFLLQESYWLGgegcSTREE--------------RALEKTEPLTEEMEDPEHPEGINDsffERELP 923
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 968 PLV--VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRK 1045
Cdd:TIGR01257 924 GLVpgVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQ 1003
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1046 NLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1125
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1126 ILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGAYGDGYRLTLV--- 1202
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVrkm 1163
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1203 KQPAEPGTSQEPGLASSPSG----CP-RLSSCSEPQV--------SQFIRKHVASSLLVSDTSTELSYILPSEAVKKGAF 1269
Cdd:TIGR01257 1164 KNIQSQRGGCEGTCSCTSKGfstrCPaRVDEITPEQVldgdvnelMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAY 1243
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1270 ERLFQQLEHSLDALHLSSFGLMDTTLEEVFLKVSEEDQSLENSEADVKESRKDVLPgAEGLTAVGGQAGNLARCSELaqs 1349
Cdd:TIGR01257 1244 ASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKRENANL-RHPCSGPTEKAGQTPQASHT--- 1319
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1350 qaslqsassvgSARGEEGTgysdgygdyrplfdnlqDPDNVSLQEAEmealaqvGQGSRKLEGWWLKMRQFHGLLVKRFH 1429
Cdd:TIGR01257 1320 -----------CSPGQPAA-----------------HPEGQPPPEPE-------DPGVPLNTGARLILQHVQALLVKRFQ 1364
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1430 CARRNSKALCSQILLPAFFVCVAMTVALSVPEIGDLPPLVLSPSQY-HNYTqprgnfipyaneerqeyrlRLSPDASPQQ 1508
Cdd:TIGR01257 1365 HTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYgQQYT-------------------FFSMDEPNSE 1425
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1509 LVSTFrlpsgvgATCVLKSPAngslgpmlnlssgesrllaarfFDSMCL-ESFTQGLPLSNfvppppspapsdspvspde 1587
Cdd:TIGR01257 1426 HLEVL-------ADVLLNKPG----------------------FGNRCLkEEWLPEYPCGN------------------- 1457
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1588 dsLQAWNMslpPTAGP--------ETWTSAPSLPRlvhepVRCTCSAQGTGF-SCPSSVGGHPPQMRVV-TGDILTDITG 1657
Cdd:TIGR01257 1458 --STPWKT---PSVSPnithlfqkQKWTAAHPSPS-----CRCSTREKLTMLpECPEGAGGLPPPQRTQrSTEILQDLTD 1527
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1658 HNVSEYLLFT---------SDRFRLH--RYGAITFGNVQKSIPASFGARVP--------------PMVRKIAVRRVA--- 1709
Cdd:TIGR01257 1528 RNISDFLVKTypalirsslKSKFWVNeqRYGGISIGGKLPAIPITGEALVGflsdlgqmmnvsggPVTREASKEMPDflk 1607
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1710 --------QVLYNNKGYHSMPTYLNSLNNAILRANLPKSKgNPAAYGITVTNHPMNKTSASLS-LDYLLQGTDVVIAIFI 1780
Cdd:TIGR01257 1608 hletedniKVWFNNKGWHALVSFLNVAHNAILRASLPKDR-DPEEYGITVISQPLNLTKEQLSeITVLTTSVDAVVAICV 1686
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1781 IVAMSFVPASFVVFLVAEKSTKAKHLQFVSGCNPVIYWLANYVWDMLNYLVPATCCVIILFVFDLPAYTSPTNFPAVLSL 1860
Cdd:TIGR01257 1687 IFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVAL 1766
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1861 FLLYGWSITPIMYPASFWFEVPSSAYVFLIVINLFIGITATVATFLLQLFEHDKDLKVVNSYLKSCFLIFPNYNLGHGLM 1940
Cdd:TIGR01257 1767 LMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFCLGRGLI 1846
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1941 EMAYNEYINEYYAKIGQfDKMKSPFEWDIVTRGLVAMTVEGFVGFFLTIMCQYNF-----LRQPQRLPVstkpVEDDVDV 2015
Cdd:TIGR01257 1847 DLALSQAVTDVYAQFGE-EHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFflsrwIAEPAKEPI----FDEDDDV 1921
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2016 ASERQRVLRGDADNDMVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFV 2095
Cdd:TIGR01257 1922 AEERQRIISGGNKTDILRLNELTKVYSGTSSP---AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV 1998
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2096 NGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRK 2175
Cdd:TIGR01257 1999 AGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRK 2078
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2176 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2255
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK 2158
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2256 NRFGDGYMITVRTKSSQ-----NVKDVVRFFNRNFPEAMLKERHHTKVQYQLKSEhiSLAQVFSKMEQVVGVLGIEDYSV 2330
Cdd:TIGR01257 2159 SKFGDGYIVTMKIKSPKddllpDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSS--SLARIFQLLISHKDSLLIEEYSV 2236
|
2490
....*....|....*....
gi 568912802 2331 SQTTLDNVFVNFAKKQSDN 2349
Cdd:TIGR01257 2237 TQTTLDQVFVNFAKQQTET 2255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2032-2255 |
5.61e-119 |
|
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: 374.92 E-value: 5.61e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2111
Cdd:cd03263 1 LQIRNLTKTYKK---GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDlIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2255
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
971-1190 |
4.19e-113 |
|
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: 358.36 E-value: 4.19e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC 1050
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1131 TAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLK 1190
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2032-2258 |
1.45e-85 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 280.03 E-value: 1.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2111
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRF 2258
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
973-1186 |
6.42e-85 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 278.10 E-value: 6.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1052
Cdd:COG1131 3 VRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1133 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:COG1131 161 GLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2032-2255 |
2.57e-68 |
|
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: 229.95 E-value: 2.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2111
Cdd:cd03265 1 IEVENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2255
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
2039-2342 |
5.05e-68 |
|
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: 232.28 E-value: 5.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2039 KVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFD 2118
Cdd:TIGR01188 1 KVY-----GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2119 ALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2198
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2199 DPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYmITVRTKSSQNVKDVV 2278
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEV 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2279 RFFNRNFPEAMLkERHHTKVQYQLKSEHISLAQvfskmEQVVGVLG--------IEDYSVSQTTLDNVFVNF 2342
Cdd:TIGR01188 235 SMLIAELGETGL-GLLAVTVDSDRIKILVPDGD-----ETVPEIVEaairngirIRSISTERPSLDDVFLKL 300
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
973-1181 |
4.19e-67 |
|
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: 227.43 E-value: 4.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1052
Cdd:COG4555 4 VENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1133 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLK 1181
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
973-1190 |
1.08e-65 |
|
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: 222.25 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1052
Cdd:cd03265 3 VENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1133 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLK 1190
Cdd:cd03265 161 GLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
973-1180 |
1.14e-65 |
|
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: 220.35 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1052
Cdd:cd03230 3 VRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLwfysrlksmaqeeirketdkmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568912802 1133 GVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03230 125 GLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
978-1302 |
4.03e-65 |
|
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: 224.19 E-value: 4.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 978 KVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLF 1057
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1137
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1138 ARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGAYGDgyRLTLVKQPAEPGTSQEPGL 1216
Cdd:TIGR01188 159 TRRAIWDYIRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGK--DTLESRPRDIQSLKVEVSM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1217 ASSPSGCPRLSSCSEPQVSQFIRkhvassLLVSDTSTELSYILpSEAVKKGaferlfqqlehsldaLHLSSFGLMDTTLE 1296
Cdd:TIGR01188 237 LIAELGETGLGLLAVTVDSDRIK------ILVPDGDETVPEIV-EAAIRNG---------------IRIRSISTERPSLD 294
|
....*.
gi 568912802 1297 EVFLKV 1302
Cdd:TIGR01188 295 DVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2032-2245 |
6.71e-64 |
|
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: 215.34 E-value: 6.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2111
Cdd:cd03230 1 IEVRNLSKRYGKKT-----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQlytrlrgipwkdeaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2031-2260 |
1.65e-61 |
|
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: 211.25 E-value: 1.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQS 2110
Cdd:COG4555 1 MIEVENLSKKYGKVP-----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2191 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGD 2260
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
973-1184 |
5.36e-55 |
|
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: 191.25 E-value: 5.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLyENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1052
Cdd:cd03264 3 LENLTKRYG--KKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1133 GVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1184
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2031-2249 |
2.45e-51 |
|
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: 181.03 E-value: 2.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQS 2110
Cdd:cd03266 1 MITADALTKRFRDVK-KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2191 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2249
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
973-1306 |
7.24e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 182.62 E-value: 7.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemDEIRKNLGMCPQ 1052
Cdd:COG4152 4 LKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1133 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGAYGdGYRLTLVKQPAEPGTS 1211
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEADGDAGWLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1212 QEPGLASspsgcprlsscsepqvsqfirkhvassllVSDTSTELSYILPSEAVKkgafERLFQQLehsLDALHLSSFGLM 1291
Cdd:COG4152 238 ALPGVTV-----------------------------VEEDGDGAELKLEDGADA----QELLRAL---LARGPVREFEEV 281
|
330
....*....|....*
gi 568912802 1292 DTTLEEVFLKVSEED 1306
Cdd:COG4152 282 RPSLNEIFIEVVGEK 296
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2031-2348 |
1.43e-50 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 181.85 E-value: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllqVQQS 2110
Cdd:COG4152 1 MLELKGLTKRFGDKT-----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKD-EAQVVKWaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2189
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEaKRRADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2190 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGdGYMITVRTK 2269
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEAD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2270 SSQNvkdvvrfFNRNFPEAMLKERHHTKVQYQLKSEHiSLAQVFSkmeQVVGVLGIEDYSVSQTTLDNVFVNFAKKQSD 2348
Cdd:COG4152 231 GDAG-------WLRALPGVTVVEEDGDGAELKLEDGA-DAQELLR---ALLARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2032-2246 |
1.16e-49 |
|
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: 175.87 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQsL 2111
Cdd:cd03268 1 LKTNDLTKTYGKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVvkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2246
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2032-2246 |
1.06e-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: 173.15 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKigrilAVDRLCLGVRPGeCFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2111
Cdd:cd03264 1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2192 DEPTTGMDPKAR-RFLwNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2246
Cdd:cd03264 155 DEPTAGLDPEERiRFR-NLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
973-1179 |
1.26e-48 |
|
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: 173.04 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGMCP 1051
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1131 TAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
973-1186 |
4.14e-48 |
|
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: 172.13 E-value: 4.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYkNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCP 1051
Cdd:COG1122 3 LENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QH--NVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:COG1122 82 QNpdDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1130 PTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2032-2244 |
3.21e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 172.68 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2111
Cdd:PRK13537 8 IDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2031-2225 |
1.48e-46 |
|
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: 166.89 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQS 2110
Cdd:COG4133 2 MLEAENLSCRRGERLL-----FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAqvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 568912802 2191 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2225
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2032-2249 |
3.51e-46 |
|
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: 165.92 E-value: 3.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllqVQQSL 2111
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2249
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
976-1180 |
7.99e-46 |
|
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: 165.08 E-value: 7.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNV 1055
Cdd:cd03268 6 LTKTYG--KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1056 LFDRLTVEEHLWFYSRLKSMAQEEIrketDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568912802 1136 PYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03268 159 PDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
973-1180 |
2.10e-45 |
|
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: 164.08 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKK--MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC 1050
Cdd:cd03266 4 ADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1131 TAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
973-1179 |
8.21e-44 |
|
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: 159.37 E-value: 8.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemDEIRKNLGMCPQ 1052
Cdd:cd03269 3 VENVTKRFG--RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568912802 1133 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2031-2244 |
1.25e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 163.46 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIE--NLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQ 2108
Cdd:PRK13536 39 TVAIDlaGVSKSYGDKAV-----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2188
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2189 IFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
970-1186 |
2.11e-42 |
|
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: 156.29 E-value: 2.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 970 VVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRK 1045
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1046 NLGMCPQHNVLFDRLTVEEHLWFYSR-LKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA 1124
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR--VALA-----RA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1125 IIL-------DEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:COG1127 156 LALdpeillyDEPTAGLDPITSAVIDELIreLRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
973-1186 |
2.35e-42 |
|
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: 156.12 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLG 1048
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1049 MCPQHNVLFDRLTVEEHLWFYSRLKS-MAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRAIIL 1127
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKR--VALA-----RALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1128 -------DEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:cd03261 154 dpelllyDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
988-1132 |
1.85e-41 |
|
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: 150.11 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-RKNLGMCPQHNVLFDRLTVEEHL 1066
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1067 WFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
973-1176 |
4.33e-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: 148.77 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVY--KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdirTEMDEIRKNLGMC 1050
Cdd:cd03293 3 VRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568912802 1131 TAGVDPYARRAIWDLILK--YKPGRTILLSTHHMDEADLLGDRIAIIS 1176
Cdd:cd03293 159 FSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2032-2250 |
1.55e-39 |
|
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: 147.69 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLL--QVQQ 2109
Cdd:cd03218 1 LRAENLSKRYGKRKV-----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 SLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2189
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2190 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
973-1180 |
2.60e-39 |
|
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: 146.51 E-value: 2.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1052
Cdd:cd03259 3 LKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1133 GVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
973-1186 |
7.65e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 148.41 E-value: 7.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1052
Cdd:PRK13537 10 FRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1133 GVDPYARRAIWD-LILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13537 168 GLDPQARHLMWErLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
973-1186 |
1.18e-38 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 145.49 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDE-IRKNLGMC 1050
Cdd:TIGR04406 4 AENLIKSYK--KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlPMHErARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLW-FYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1130 PTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
973-1172 |
2.77e-38 |
|
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: 143.00 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1052
Cdd:COG4133 5 AENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRkeTDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568912802 1133 GVDPYARRAIWDLILKYKP-GRTILLSTHhmDEADLLGDRI 1172
Cdd:COG4133 161 ALDAAGVALLAELIAAHLArGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
987-1186 |
3.33e-38 |
|
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: 144.12 E-value: 3.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1064
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHEIaRLGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 ------------HLWFYSRLKSMAqeEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03219 95 nvmvaaqartgsGLLLARARREER--EARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1133 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:cd03219 173 GLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
973-1186 |
6.38e-38 |
|
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: 143.07 E-value: 6.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEiRKNLGMC- 1050
Cdd:cd03218 3 AENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK-RARLGIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 -PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:cd03218 80 lPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1130 PTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIkiLKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
976-1186 |
6.77e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.51 E-value: 6.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNV 1055
Cdd:PRK13536 47 VSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1056 LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1136 PYARRAIWD----LILKykpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13536 205 PHARHLIWErlrsLLAR---GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2033-2256 |
9.61e-38 |
|
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: 142.58 E-value: 9.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQQS 2110
Cdd:cd03219 2 EVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQL-------YTRLRGIPWKDEAQVVKWA---LEKLELTKYADKPAGTYSGGNKRKLSTAI 2180
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVMVaaqartgSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2181 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2256
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
972-1179 |
1.68e-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: 138.92 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 972 CVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGMC 1050
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQhnvlfdrltveehlwfysrlksmaqeeirketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1131 TAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:cd00267 108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2032-2245 |
1.73e-37 |
|
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: 141.12 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLkDLLQVQQSL 2111
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQReLGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2032-2250 |
1.93e-37 |
|
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: 141.70 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL-KDLLQVQQS 2110
Cdd:COG1122 1 IELENLSFSYP----GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQF--DALFDElTAREHLQLYTRLRGIPwKDEA-QVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:COG1122 77 VGLVFQNpdDQLFAP-TVEEDVAFGPENLGLP-REEIrERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2188 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
965-1178 |
7.56e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.00 E-value: 7.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 965 THLPLVVCVDKLTKVY--KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemdE 1042
Cdd:COG1116 2 SAAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1043 IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1122
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1123 RAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1178
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
973-1180 |
8.91e-37 |
|
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: 139.16 E-value: 8.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIR-K 1045
Cdd:cd03255 3 LKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFRrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1046 NLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1125
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 1126 ILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1180
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2033-2244 |
9.48e-37 |
|
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: 138.75 E-value: 9.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSL 2111
Cdd:cd03225 1 ELKNLSFSYPDGAR---PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:cd03225 78 GLVFQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2191 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2031-2338 |
1.10e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 142.53 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYK----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAF 2094
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2095 VNGHSVLKD---LL--------QVQQslgycpqfdaLFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADK 2163
Cdd:COG4586 81 VLGYVPFKRrkeFArrigvvfgQRSQ----------LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2164 PAgtysggnkRKLS--------TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALC 2234
Cdd:COG4586 151 PV--------RQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2235 TRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQNVKDVVRFfnrnfpeAMLKERHHTKVQYQLKSEhISLAQVFS 2314
Cdd:COG4586 223 DRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRG-------GEVIEREGNRVRLEVDPR-ESLAEVLA 294
|
330 340
....*....|....*....|....
gi 568912802 2315 KmeqVVGVLGIEDYSVSQTTLDNV 2338
Cdd:COG4586 295 R---LLARYPVRDLTIEEPPIEEV 315
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
987-1186 |
3.13e-36 |
|
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: 139.02 E-value: 3.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKnLGMCP--QHNVLFDRLTVE 1063
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItGLPPHRIAR-LGIARtfQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1064 EHL-----------WFYS--RLKSMAQEE--IRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:COG0411 98 ENVlvaaharlgrgLLAAllRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1129 EPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2027-2253 |
4.30e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 138.30 E-value: 4.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2027 ADNDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ 2106
Cdd:COG1121 2 MMMPAIELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VqqslGYCPQ---FDALFdELTARE----HLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA 2179
Cdd:COG1121 77 I----GYVPQraeVDWDF-PITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2180 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLaIMVNGRLRCLGSIQH 2253
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
974-1186 |
5.44e-36 |
|
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: 137.82 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 974 DKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMD--EIRKNLGMCP 1051
Cdd:cd03295 4 ENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-EQDpvELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIE--DLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1130 PTAGVDPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1709-1956 |
1.34e-35 |
|
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: 140.22 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1709 AQVLYNNKGYHSMPTYLNSLNNaILRANLPKSKGNPAAYGITVTNHPMNKTSASLSLDYLLQgtdVVIAIFIIVAMSFVP 1788
Cdd:pfam12698 101 VTVYINSSNLLVSKLILNALQS-LLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAY---YLVGLILMIIILIGA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1789 ASFVVFLVAEKSTKAKHLQFVSGCNPVIYWLANYVWDMLNYLVPATCCVIILFVFDLPaytsPTNFPAVLSLFLLYGWSI 1868
Cdd:pfam12698 177 AIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIP----FGNLGLLLLLFLLYGLAY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1869 TPIMYPASFWFEVPSSAYVFLIVINLFIGItATVATFLLQLFehdkdlkvvNSYLKSCFLIFPNYNLGHGLMEMAYNEYI 1948
Cdd:pfam12698 253 IALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDP---------PSFLQWIFSIIPFFSPIDGLLRLIYGDSL 322
|
....*...
gi 568912802 1949 NEYYAKIG 1956
Cdd:pfam12698 323 WEIAPSLI 330
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
987-1179 |
2.14e-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: 135.25 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1064
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHERaRAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLwfysRLKSMAQ-EEIRKETDKMIEDL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1141
Cdd:cd03224 95 NL----LLGAYARrRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 568912802 1142 IWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:cd03224 171 IFEAIRELRDeGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
973-1186 |
2.20e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 135.93 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTE--MDE-IRKNLGM 1049
Cdd:COG1137 6 AENLVKSYG--KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THlpMHKrARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1130 PTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMDEAdlLG--DRIAIISHGKLKCCGSP 1186
Cdd:COG1137 163 PFAGVDPIAVADIQKIIrhLKER-GIGVLITDHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
971-1179 |
2.27e-35 |
|
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: 133.66 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGM 1049
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQHNVLFDRlTVEEHLwfysrlksmaqeeirketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1130 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGK 1179
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2031-2245 |
2.77e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 135.93 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdlLQV--- 2107
Cdd:COG1137 3 TLEAENLVKSYGKRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH--LPMhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 -QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2186
Cdd:COG1137 76 aRLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2187 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
973-1186 |
3.95e-35 |
|
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: 135.94 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMD--EIRKNLGMC 1050
Cdd:COG1120 4 AENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSrrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEE--------HLwfySRLKSMAQEEIRKeTDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1122
Cdd:COG1120 81 PQEPPAPFGLTVRElvalgrypHL---GLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1123 RAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
948-1186 |
7.73e-35 |
|
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: 141.96 E-value: 7.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 948 AMESRHFEETRGMEEEPTHLPLVVcVDKLTKVY---KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP 1024
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPLLE-VRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1025 TSGSATIYGHDIRT----EMDEIRKNLGMCPQH--NVLFDRLTVEEHLWF-YSRLKSMAQEEIRKETDKMIEDLELSNK- 1096
Cdd:COG1123 318 TSGSILFDGKDLTKlsrrSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPPDl 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1097 RHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAI 1174
Cdd:COG1123 398 ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYIADRVAV 477
|
250
....*....|..
gi 568912802 1175 ISHGKLKCCGSP 1186
Cdd:COG1123 478 MYDGRIVEDGPT 489
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
976-1181 |
2.13e-34 |
|
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: 132.52 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHD-IRTEMdeirKNLGMCPQHN 1054
Cdd:TIGR03740 6 LSKRFG--KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKDL----HKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1055 VLFDRLTVEEHLWFYSRLKSMAQEEIrketDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1134
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568912802 1135 DPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1181
Cdd:TIGR03740 156 DPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2033-2244 |
2.27e-34 |
|
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: 130.06 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSL 2111
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLT-----LKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFdalfdeltarehlqlytrlrgipwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd00267 76 GYVPQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1003-1186 |
2.99e-34 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 144.11 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1003 FLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtEMD----EIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQE 1078
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ----PVDagdiATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1079 EIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTIL 1156
Cdd:NF033858 373 EIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLieLSREDGVTIF 452
|
170 180 190
....*....|....*....|....*....|
gi 568912802 1157 LSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1186
Cdd:NF033858 453 ISTHFMNEA-ERCDRISLMHAGRVLASDTP 481
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
960-1186 |
3.93e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 3.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 960 MEEEPthlplVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE 1039
Cdd:COG1121 1 MMMMP-----AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1040 mdeiRKNLGMCPQHnVLFDR---LTVEE--------HLWFYSRLKSmaqeEIRKETDKMIEDLELSNKRHSLVQTLSGGM 1108
Cdd:COG1121 74 ----RRRIGYVPQR-AEVDWdfpITVRDvvlmgrygRRGLFRRPSR----ADREAVDEALERVGLEDLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1109 KRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLkCCGSP 1186
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPP 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
973-1180 |
4.29e-34 |
|
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: 131.86 E-value: 4.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKN 1046
Cdd:cd03257 4 VKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1047 LGMCPQH--NVLFDRLTVEEHLW--FYSRLKSMAQEEIRKETDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIAFVGG 1121
Cdd:cd03257 84 IQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1122 SRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2033-2256 |
1.90e-33 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 130.47 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLG 2112
Cdd:TIGR04406 3 VAENLIKSYKKRKV-----VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2113 --YCPQFDALFDELTAREHLQLYTRLRGIPWKDE-AQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2189
Cdd:TIGR04406 78 igYLPQEASIFRKLTVEENIMAVLEIRKDLDRAErEERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2190 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2256
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
973-1187 |
2.67e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.27 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCP 1051
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSN--KRHSlvQTLSGGMKRKlsVAIAFVGG--SRAII 1126
Cdd:PRK13632 90 QNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDylDKEP--QNLSGGQKQR--VAIASVLAlnPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1127 LDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPL 1187
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
973-1180 |
3.53e-33 |
|
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: 129.62 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKN 1046
Cdd:cd03258 4 LKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1047 LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAII 1126
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1127 LDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
968-1180 |
3.57e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 129.39 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 968 PLVVCVDkLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMD 1041
Cdd:COG1136 3 PLLELRN-LTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1042 EIR-KNLGMCPQ-HNvLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFV 1119
Cdd:COG1136 82 RLRrRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1120 GGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1180
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
970-1180 |
4.62e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 4.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 970 VVCVDKLTKVYKNDKKmALNKLSLNLYENQVVsFL-GHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIR 1044
Cdd:COG2884 1 MIRFENVSKRYPGGRE-ALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1045 KNLGMCPQ-HNVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGG-MKRklsVAIAfvggs 1122
Cdd:COG2884 79 RRIGVVFQdFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGeQQR---VAIA----- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1123 RAI-------ILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:COG2884 150 RALvnrpellLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
970-1186 |
5.67e-33 |
|
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: 136.19 E-value: 5.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 970 VVCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT---SGSATIYGHDIRTEMDEIR-K 1045
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1046 NLGMCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1124
Cdd:COG1123 84 RIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1125 IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1995-2254 |
9.22e-33 |
|
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: 135.42 E-value: 9.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1995 FLRQPQRL---PVSTKPVEDDVDVASERQRVLRgdadndmvkIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVN 2071
Cdd:COG1123 230 ILAAPQALaavPRLGAARGRAAPAAAAAEPLLE---------VRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGES 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2072 GAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQVQQSLGYCPQ--FDALFDELTAREHLQLYTRLRGIPWKDEA 2145
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAER 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2146 -QVVKWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVL 2222
Cdd:COG1123 381 rERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLF 460
|
250 260 270
....*....|....*....|....*....|..
gi 568912802 2223 TSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2254
Cdd:COG1123 461 ISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
973-1179 |
9.78e-33 |
|
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: 126.15 E-value: 9.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI---RKNLGM 1049
Cdd:cd03229 3 LKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQHNVLFDRLTVEEHLWFysrlksmaqeeirketdkmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1130 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2032-2245 |
2.77e-32 |
|
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: 126.45 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK------DLL 2105
Cdd:cd03255 1 IELKNLSKTYGGGGE-KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQQsLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:cd03255 80 RRRH-IGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEEcEALCTRLAIMVNGRL 2245
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2033-2245 |
3.57e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 3.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSL 2111
Cdd:COG4619 2 ELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDElTAREHLQLYTRLRGIPWkDEAQVVKWaLEKLELTK-YADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKF-DRERALEL-LERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2191 LDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2031-2245 |
5.49e-32 |
|
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: 126.69 E-value: 5.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdlLQVQQ- 2109
Cdd:COG0411 4 LLEVRGLTKRF-----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 -SLG----YcpQFDALFDELTAREHLQL--YTRLRGIPW----------KDEAQVVKWA---LEKLELTKYADKPAGTYS 2169
Cdd:COG0411 77 aRLGiartF--QNPRLFPELTVLENVLVaaHARLGRGLLaallrlprarREEREARERAeelLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2170 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2031-2250 |
8.64e-32 |
|
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: 126.31 E-value: 8.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQ 2109
Cdd:COG1120 1 MLEAENLSVGYGGRPV-----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 SLGYCPQFDALFDELTARE--------HLQLYTRLRgipwKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2181
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRElvalgrypHLGLFGRPS----AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2182 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2033-2249 |
1.17e-31 |
|
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: 124.57 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQVQQSLG 2112
Cdd:cd03235 1 EVEDLTVSYGGHPV-----LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2113 YCPQ---FDALFdELTARE--HLQLYTRLRGIPW--KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:cd03235 72 YVPQrrsIDRDF-PISVRDvvLMGLYGHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRlAIMVNGRLRCLG 2249
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2027-2256 |
1.74e-31 |
|
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: 124.71 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2027 ADNDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----K 2102
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVV-----LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2103 DLLQVQQSLGYCPQFDALFDELTAREHLQL----YTRLrgipwkDEAQVVKWALEKLE---LTKYADKPAGTYSGGNKRK 2175
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFDSLTVFENVAFplreHTDL------SEAEIRELVLEKLElvgLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2176 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2254
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
..
gi 568912802 2255 KN 2256
Cdd:COG1127 230 LA 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
2052-2196 |
2.58e-31 |
|
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: 121.22 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2052 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKD-LLQVQQSLGYCPQFDALFDELTAREHL 2130
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2131 QLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAG----TYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2196
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
973-1179 |
3.42e-31 |
|
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: 123.83 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIRKNLG 1048
Cdd:cd03256 3 VENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1049 MCPQHNVLFDRLTVEEH-----LWFYSRLKSMAQEEIRKETDKMIEDLE---LSNKRHSLVQTLSGGMKRKLSVAIAFVG 1120
Cdd:cd03256 82 MIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1121 GSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
980-1184 |
4.31e-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: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTeMD--EIRKNLGMCPQhnvlf 1057
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-LSpkELARKIAYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 drltveehlwfysrlksmaqeeirketdkMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1137
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568912802 1138 ARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1184
Cdd:cd03214 132 HQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
973-1180 |
4.71e-31 |
|
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: 123.60 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVY-------------------KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG 1033
Cdd:cd03267 3 VSNLSKSYrvyskepgligslkslfkrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1034 HDIRTEMDEIRKNLG-MCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKL 1112
Cdd:cd03267 83 LVPWKRRKKFLRRIGvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1113 SVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
980-1180 |
5.71e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.23 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKNLGMCPQHNVLF 1057
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPppEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DRlTVEEHL--WFYSRLKSMAQEEIRKetdkMIEDLELS----NKRhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:COG4619 87 GG-TVRDNLpfPFQLRERKFDRERALE----LLERLGLPpdilDKP---VERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1132 AGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:COG4619 159 SALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
961-1199 |
8.25e-31 |
|
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: 130.66 E-value: 8.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 961 EEEPTHLPLVVCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-E 1039
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1040 MDEIRKNLGMCPQHNVLFDRlTVEEHLwfysRL-KSMAQEEirketdKMIEDLE----------LSNKRHSLV----QTL 1104
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDT-TLRENL----RLaRPDATDE------ELWAALErvglgdwlaaLPDGLDTWLgeggRRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1105 SGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCG 1184
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQG 551
|
250
....*....|....*
gi 568912802 1185 SPLFLKGAYGDGYRL 1199
Cdd:COG4987 552 THEELLAQNGRYRQL 566
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
973-1178 |
1.12e-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: 121.49 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEmdeiRKNLGMCPQ 1052
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 H-NVLFD-RLTVEE--------HLWFYSRLKsmaqEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1122
Cdd:cd03235 76 RrSIDRDfPISVRDvvlmglygHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1123 RAIILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIA-----IISHG 1178
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLllnrtVVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2032-2256 |
2.50e-30 |
|
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: 121.45 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQV 2107
Cdd:cd03261 1 IELRGLTKSFGGRTV-----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQFDALFDELTAREHLQL----YTRLrgipwkDEAQVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAI 2180
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFplreHTRL------SEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2181 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2256
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2031-2254 |
2.85e-30 |
|
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: 121.15 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQ 2106
Cdd:cd03258 1 MIELKNVSKVFGDTG-GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPwkdEAQVVKWALEKLELTKYADKpAGTY----SGGNKRKLSTAIAL 2182
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVP---KAEIEERVLELLELVGLEDK-ADAYpaqlSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2183 IGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2254
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
973-1186 |
3.60e-30 |
|
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: 120.80 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1052
Cdd:cd03300 3 LENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1133 GVDPYARRaiwDLILKYKP-----GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:cd03300 160 ALDLKLRK---DMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2032-2245 |
6.29e-30 |
|
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: 120.13 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYK----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFV 2095
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2096 NGhsvlkdLLQVQQSLGYCPQFDALFDE-------LTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTY 2168
Cdd:cd03267 81 AG------LVPWKRRKKFLRRIGVVFGQktqlwwdLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2169 SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
973-1186 |
7.48e-30 |
|
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: 120.13 E-value: 7.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKkmaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1052
Cdd:cd03299 3 VENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1133 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:cd03299 159 ALDVRTKEKLREELkkIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
973-1180 |
9.89e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 122.12 E-value: 9.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKK-------------------MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG 1033
Cdd:COG4586 4 VENLSKTYRVYEKepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1034 HDIRTEMDEIRKNLGmcpqhnVLF--------DrLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLS 1105
Cdd:COG4586 84 YVPFKRRKEFARRIG------VVFgqrsqlwwD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 1106 GGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
973-1186 |
3.24e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKND---KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKN 1046
Cdd:PRK13637 5 IENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1047 LGMC---PQHNvLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSN---KRHSLVQtLSGGMKRKLSVAIAFVG 1120
Cdd:PRK13637 85 VGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedyKDKSPFE-LSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1121 GSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2033-2256 |
3.33e-29 |
|
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: 117.54 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQQS 2110
Cdd:cd03224 2 EVENLNAGY-----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQLYTRLRGIpwkdeaQVVKWALEKL-----ELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRR------AKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2256
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2031-2262 |
3.59e-29 |
|
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: 118.37 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLL- 2105
Cdd:COG1124 1 MLEVRNLSVSYGQGG-RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrrrRKAFRr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQqslgYCPQ--FDALFDELTAREHLQLYTRLRGIPwKDEAQVVKwALEKLELTK-YADKPAGTYSGGNKRKLSTAIAL 2182
Cdd:COG1124 80 RVQ----MVFQdpYASLHPRHTVDRILAEPLRIHGLP-DREERIAE-LLEQVGLPPsFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2183 IGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDG 2261
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
.
gi 568912802 2262 Y 2262
Cdd:COG1124 234 Y 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2032-2240 |
3.80e-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: 117.19 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQVQQSL 2111
Cdd:cd03293 1 LEVRNVSKTYGGGG-GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIM 2240
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
987-1186 |
4.69e-29 |
|
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: 118.90 E-value: 4.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIR-KNLGMCPQHNVLFDRLT 1061
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRrKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1062 VEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1141
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568912802 1142 IWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:cd03294 199 MQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2024-2244 |
4.74e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 127.16 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2024 RGDADNDMVKIE--NLTkvyksRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL 2101
Cdd:NF033858 257 RPADDDDEPAIEarGLT-----MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2102 KDLLQVQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2181
Cdd:NF033858 332 AGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2182 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEaLCTRLAIMVNGR 2244
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
974-1199 |
5.67e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.69 E-value: 5.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 974 DKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCP 1051
Cdd:PRK10895 7 KNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKE-TDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 1131 TAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL------KGAY-GDGYRL 1199
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlqdehvKRVYlGEDFRL 241
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2031-2245 |
6.37e-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: 116.84 E-value: 6.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdLLQVQQS 2110
Cdd:cd03257 1 LLEVKNLSVSFPTGG-GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK-LSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 L-----GYCPQ--FDALFDELTAREHLQLYTRLRGIPWKDEAQ--VVKWALEKLELTK-YADKPAGTYSGGNKRKLSTAI 2180
Cdd:cd03257 79 IrrkeiQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARkeAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2181 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
976-1180 |
3.65e-28 |
|
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: 114.97 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP-----PTSGSATIYGHDIRTEMD---EIRKNL 1047
Cdd:cd03260 6 LNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVdvlELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1048 GMCPQHNVLFdRLTVEEHLWFYSRLKSMAQeeiRKETDKMIEDL--------ELSNKRHSLvqTLSGGMKRKLSVAIAFV 1119
Cdd:cd03260 84 GMVFQKPNPF-PGSIYDNVAYGLRLHGIKL---KEELDERVEEAlrkaalwdEVKDRLHAL--GLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1120 GGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
949-1186 |
3.97e-28 |
|
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: 122.17 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 949 MESRHFEETRGMEEEPTHLPLVVCVDKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGS 1028
Cdd:COG4988 315 LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1029 ATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDrLTVEEHLWFYSRLKSMAQ-EEIRKET--DKMIEDLElsNKRHSLV--- 1101
Cdd:COG4988 394 ILINGVDLSDlDPASWRRQIAWVPQNPYLFA-GTIRENLRLGRPDASDEElEAALEAAglDEFVAALP--DGLDTPLgeg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1102 -QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1180
Cdd:COG4988 471 gRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRI 549
|
....*.
gi 568912802 1181 KCCGSP 1186
Cdd:COG4988 550 VEQGTH 555
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
973-1181 |
4.73e-28 |
|
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: 113.89 E-value: 4.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKnDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEmdEIRKNLGMCPQ 1052
Cdd:cd03226 2 IENISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 ---HNVLFDrlTVEEHLWFYSRLKSMAQEEIRKetdkMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:cd03226 79 dvdYQLFTD--SVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1130 PTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1181
Cdd:cd03226 153 PTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2029-2245 |
4.89e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 114.37 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDL 2104
Cdd:COG1136 2 SPLLELRNLTKSYGTGE-GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2105 LQV-QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2183
Cdd:COG1136 81 ARLrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2184 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSmEECEALCTRLAIMVNGRL 2245
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
987-1179 |
5.23e-28 |
|
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: 114.69 E-value: 5.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1064
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHRIaRLGIGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HL--WFYSRLKSMAQEEIRKEtdkmIEDL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1140
Cdd:COG0410 98 NLllGAYARRDRAEVRADLER----VYELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568912802 1141 AIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:COG0410 174 EIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2031-2254 |
6.96e-28 |
|
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: 120.78 E-value: 6.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKDLLQV 2107
Cdd:COG1123 4 LLEVRDLSVRYPG---GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 Q-QSLGYCPQ-FDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:COG1123 81 RgRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2254
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
980-1186 |
1.59e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.80 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDK----KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD--EIRKNLGMCPQH 1053
Cdd:PRK13633 14 YESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 --NVLFDRLtVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSR--AIILDE 1129
Cdd:PRK13633 94 pdNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR--VAIAGILAMRpeCIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1130 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
979-1164 |
3.24e-27 |
|
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: 112.87 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 979 VYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSG-SATIYGHDI-RTEMDEIRKNLGMCpqHNVL 1056
Cdd:COG1119 11 VRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLV--SPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1057 FDRLTVEEHLW------FYSrlkSM-----AQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1125
Cdd:COG1119 88 QLRFPRDETVLdvvlsgFFD---SIglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568912802 1126 ILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDE 1164
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2031-2244 |
3.88e-27 |
|
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: 112.00 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLlq 2106
Cdd:COG0410 3 MLEVENLHAGY-----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQFDALFDELTAREHLQL--YTRlrgipwKDEAQVvKWALEKL-----ELTKYADKPAGTYSGGNKRKLSTA 2179
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSLTVEENLLLgaYAR------RDRAEV-RADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2180 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2032-2250 |
3.99e-27 |
|
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: 112.39 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQS 2110
Cdd:cd03295 1 IEFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQLYTRLRGipWKdEAQVVKWALEKLEL-----TKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLK--WP-KEKIRERADELLALvgldpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
975-1180 |
6.31e-27 |
|
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: 110.96 E-value: 6.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 975 KLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMC 1050
Cdd:cd03292 5 NVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1131 TAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
971-1180 |
9.94e-27 |
|
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: 110.04 E-value: 9.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMC 1050
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1131 TAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03301 158 LSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
971-1180 |
1.05e-26 |
|
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: 118.78 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGM 1049
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQHNVLFDRlTVEEHLWFYSRLKSMaqEEIRK-----ETDKMIEdlELSNKRHSLV----QTLSGGMKRKLSVAIAFVG 1120
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGDPDATD--EEIIEaarlaGLHDFIE--ALPMGYDTVVgeggSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1121 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLgDRIAIISHGKL 1180
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2033-2249 |
1.78e-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: 108.29 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSL 2111
Cdd:cd03214 1 EVENLSVGYGGRTV-----LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQfdalfdeltarehlqlytrlrgipwkdeaqvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03214 76 AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2249
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2035-2250 |
1.82e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 110.37 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2035 ENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH--SVLKDLLQVQQSLG 2112
Cdd:PRK10895 7 KNLAKAYKGRRV-----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2113 YCPQFDALFDELTAREHLQLYTRLR-GIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2032-2258 |
3.80e-26 |
|
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: 109.25 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLkDLLQVQQSL 2111
Cdd:cd03300 1 IELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2192 DEPTTGMDPKARRflwNLILDLI----KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRF 2258
Cdd:cd03300 155 DEPLGALDLKLRK---DMQLELKrlqkELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRF 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2034-2243 |
5.28e-26 |
|
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: 107.73 E-value: 5.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2034 IENLTkvYKSRKIGRILAVDRLCLgvRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLlqvQQSLG 2112
Cdd:cd03226 2 IENIS--FSYKKGTEILDDLSLDL--YAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKER---RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2113 YCPQ--FDALFDELTAREhlqLYTRLRGIPwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:cd03226 75 YVMQdvDYQLFTDSVREE---LLLGLKELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2191 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2243
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
981-1184 |
5.66e-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: 5.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 981 KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIRTemDEIRKNLGMCPQHNVLF 1057
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP--DQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DRLTVEEHLWFYSRLKS---MAQEEIRKETDKM-IEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1133
Cdd:cd03234 94 PGLTVRETLTYTAILRLprkSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1134 VDP------------YARRaiwdlilkykpGRTILLSTHHmDEADL--LGDRIAIISHGKLKCCG 1184
Cdd:cd03234 174 LDSftalnlvstlsqLARR-----------NRIVILTIHQ-PRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
980-1165 |
5.97e-26 |
|
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: 107.12 E-value: 5.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMCPQH--N 1054
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1055 VLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1134
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 568912802 1135 DPYARRAIWDLILKYKP-GRTILLSTHHMDEA 1165
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAeGMTVVISTHDVDLA 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
971-1187 |
6.51e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 111.70 E-value: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMC 1050
Cdd:COG3839 4 LELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRAII---- 1126
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR--VALG-----RALVrepk 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1127 ---LDEPTAGVDP----YARRAIWDLILKYkpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPL 1187
Cdd:COG3839 154 vflLDEPLSNLDAklrvEMRAEIKRLHRRL--GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2044-2278 |
6.86e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 111.75 E-value: 6.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2044 RKIGRILAVDRLCLGVRPGECFGLLGVNGAG--KTSTFKMLTGDESTTGGEAFVNGHSVLKDLlqvQQSLG-YCPQFDAL 2120
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRAL---RRTIG*HRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2121 FDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2200
Cdd:NF000106 98 RESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2201 KARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGdGYMITVRTKSSQNVKDVV 2278
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPAHAAELDRMV 254
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2059-2245 |
6.99e-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: 108.13 E-value: 6.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKDllQVQQSLGYCPQFDALFDELTAREHLQLYTR 2135
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2136 LRGIPWKDEAQVVKWAlEKLELTKYADKPAGTY-----SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPkarrFLWNLI 2210
Cdd:cd03234 108 LRLPRKSSDAIRKKRV-EDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568912802 2211 L----DLIKTGRSVVLTSHS-MEECEALCTRLAIMVNGRL 2245
Cdd:cd03234 183 VstlsQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
980-1180 |
1.23e-25 |
|
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: 107.29 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLF- 1057
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 ----DRLTV------EEHLWFYSRLkSMAQEEIRKETDKMieDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIIL 1127
Cdd:cd03245 92 gtlrDNITLgapladDERILRAAEL-AGVTDFVNKHPNGL--DLQIGERG----RGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1128 DEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLgDRIAIISHGKL 1180
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2029-2251 |
2.64e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.09 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYK-----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGG 2091
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2092 EAFVNGH-SVLKDLlqvqqSLGycpqFDAlfdELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSG 2170
Cdd:COG1134 82 RVEVNGRvSALLEL-----GAG----FHP---ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2171 GNKRKLSTAIALIGYPAFIFLDEPTTGMDP----KARRFlwnlILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2246
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLAR----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
....*
gi 568912802 2247 CLGSI 2251
Cdd:COG1134 226 MDGDP 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
968-1180 |
2.77e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.43 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 968 PLVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRK 1045
Cdd:COG3845 3 PPALELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1046 NLGMCPQHNVLFDRLTVEEHL---------WFYSRlksmaqEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAI 1116
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIvlgleptkgGRLDR------KAARARIRELSERYGLDVDPDAKVEDLSVGEQQR--VEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1117 --AFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:COG3845 153 lkALYRGARILILDEPTAVLTPQEADELFEILrrLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2031-2245 |
2.80e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.80 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQV--- 2107
Cdd:COG3842 5 ALELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNK-RklsTAIA--LIG 2184
Cdd:COG3842 76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VALAraLAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2185 YPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQReLGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2032-2249 |
3.48e-25 |
|
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: 105.80 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK------DLL 2105
Cdd:cd03301 1 VELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQQSLgycpqfdALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:cd03301 76 MVFQNY-------ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2249
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
984-1180 |
5.63e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 107.22 E-value: 5.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 984 KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-----MDEIRKNLGMCPQ--HNVL 1056
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1057 FDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNK--RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1134
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDliSKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568912802 1135 DPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK13641 177 DPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2035-2245 |
1.03e-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: 103.78 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2035 ENLTK-VYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVlkDLLQVQQSL 2111
Cdd:cd03213 7 RNLTVtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL--DKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIpwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03213 85 GYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHS-MEECEALCTRLAIMVNGRL 2245
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
973-1180 |
1.59e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.47 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKK--MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE-----IRK 1045
Cdd:COG1135 4 LENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSErelraARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1046 NLGMCPQH-NvLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA 1124
Cdd:COG1135 83 KIGMIFQHfN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR--VGIA-----RA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1125 I-----IL--DEPTAGVDPYARRAIWDLILK--YKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:COG1135 155 LannpkVLlcDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
985-1192 |
1.72e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.87 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 985 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDE-----IRKNLGMC---PQHNvL 1056
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkpLRKKVGIVfqfPEHQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1057 FDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSnkrHSLVQ----TLSGG-MKRklsVAIAFVGG--SRAIILDE 1129
Cdd:PRK13634 99 FEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP---EELLArspfELSGGqMRR---VAIAGVLAmePEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 1130 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGA 1192
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPreIFADPD 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
973-1180 |
1.98e-24 |
|
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: 103.38 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGM 1049
Cdd:cd03262 3 IKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQHNVLFDRLTVEEHLWFYSR-LKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA---- 1124
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQR--VAIA-----RAlamn 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1125 ---IILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03262 154 pkvMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
970-1186 |
2.72e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 970 VVCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLG 1048
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1049 MCPQH-NVLFDRLTVEEHLWFysrlksmAQEEIRKETDKMIEDLELSNKRHSLVQ-------TLSGGMKRKlsVAIAFVG 1120
Cdd:PRK13635 85 MVFQNpDNQFVGATVQDDVAF-------GLENIGVPREEMVERVDQALRQVGMEDflnrephRLSGGQKQR--VAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1121 GSRA--IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13635 156 ALQPdiIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
975-1180 |
3.30e-24 |
|
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: 102.96 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 975 KLTKVYKNDKKMALNkLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHN 1054
Cdd:cd03298 2 RLDKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1055 VLFDRLTVEEH--LWFYSRLKSMAQEeiRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03298 80 NLFAHLTVEQNvgLGLSPGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1133 GVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03298 158 ALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
979-1186 |
3.91e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 979 VYK-NDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---TEMDEIRKNLGMCPQH- 1053
Cdd:PRK13639 8 KYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 -NVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:PRK13639 88 dDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1133 GVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2031-2228 |
4.63e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.82 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKsrkiGRILAVDRLCLGVRPGE-CFgLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLL 2105
Cdd:COG2884 1 MIRFENVSKRYP----GGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQQSLGYCPQfDA-LFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIG 2184
Cdd:COG2884 76 YLRRRIGVVFQ-DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568912802 2185 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2228
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2029-2244 |
4.69e-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: 103.63 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDES-TTGGEAFVNGHSVLK-DLLQ 2106
Cdd:COG1119 1 DPLLELRNVTVRRGGKTI-----LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRGGeDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYC-PQFDALFDE-LTARE--------HLQLYtrlRGIPWKDEAQVVKWaLEKLELTKYADKPAGTYSGGNKRKL 2176
Cdd:COG1119 76 LRKRIGLVsPALQLRFPRdETVLDvvlsgffdSIGLY---REPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2177 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTG-RSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
969-1189 |
4.71e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 4.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 969 LVVCVDKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNL 1047
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1048 GMCPQ--HNVLFDrLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1125
Cdd:PRK13647 82 GLVFQdpDDQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1126 ILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1189
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
980-1186 |
4.89e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.48 E-value: 4.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1058
Cdd:COG1132 349 YPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 RlTVEEHLwFYSRLKSmAQEEIRK-----ETDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:COG1132 428 G-TIRENI-RYGRPDA-TDEEVEEaakaaQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1130 PTAGVDPYARRAIWDLILKYKPGRTILLSTH------HMdeadllgDRIAIISHGKLKCCGSP 1186
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA-------DRILVLDDGRIVEQGTH 558
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
973-1180 |
5.03e-24 |
|
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: 103.34 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVY--KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGM 1049
Cdd:COG1124 4 VRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQH--NVLFDRLTVEEHLwfySR-LKSMAQEEIRKETDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1125
Cdd:COG1124 84 VFQDpyASLHPRHTVDRIL---AEpLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 1126 ILDEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
973-1186 |
5.64e-24 |
|
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: 103.19 E-value: 5.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1052
Cdd:cd03296 5 VRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSMAQE----EIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1129 EPTAGVDPYARRAI--WDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:cd03296 162 EPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2032-2249 |
6.42e-24 |
|
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: 102.23 E-value: 6.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRK-----------------IGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAF 2094
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2095 VNGhsvlkdllQVQQSLGycpqFDALFD-ELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNK 2173
Cdd:cd03220 81 VRG--------RVSSLLG----LGGGFNpELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2174 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2249
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2031-2245 |
8.10e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MV--KIENLTKvYKSRKIGR-ILAVDRLCLG---------VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH 2098
Cdd:COG1129 236 MVgrELEDLFP-KRAAAPGEvVLEVEGLSVGgvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2099 SV-LKDLLQ-VQQSLGYCP---QFDALFDELTARE-----HLQLYTRLRGIPWKDEAQVVKWALEKLEL-TKYADKPAGT 2167
Cdd:COG1129 315 PVrIRSPRDaIRAGIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGN 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2168 YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
975-1184 |
8.24e-24 |
|
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: 102.23 E-value: 8.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 975 KLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhDIRTEMDEirkNLGMCPQhn 1054
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGL---GGGFNPE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1055 vlfdrLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKL--SVAIAFvgGSRAIILDEPTA 1132
Cdd:cd03220 99 -----LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1133 GVDPY----ARRAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1184
Cdd:cd03220 172 VGDAAfqekCQRRLRELL---KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2032-2245 |
8.67e-24 |
|
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: 102.26 E-value: 8.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-----DESTTGGEAFVNGHSVLK---D 2103
Cdd:cd03260 1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldvD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2104 LLQVQQSLGYCPQFDALFDeLTAREHLQLYTRLRGIPWKDE-AQVVKWALEKLELTKY-ADKPAGTY-SGGNKRKLSTAI 2180
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEvKDRLHALGlSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2181 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
971-1180 |
9.20e-24 |
|
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: 99.81 E-value: 9.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLG 1048
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1049 MCPQhnvlfdrltveehlwfysrlksmaqeeirketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1129 EPTAGVDPYARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03216 108 EPTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2031-2244 |
9.76e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 9.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLtkvykSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQ 2108
Cdd:PRK11300 5 LLSVSGL-----MMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDALFDELTARE------HLQLYTR-LRGI---PW--KDEAQVVKWA---LEKLELTKYADKPAGTYSGGNK 2173
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIEnllvaqHQQLKTGlFSGLlktPAfrRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2174 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2032-2244 |
1.81e-23 |
|
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: 99.57 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQ--- 2108
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDALFDELTAREHLQLytrlrgipwkdeaqvvkwALekleltkyadkpagtySGGNKRKLSTAIALIGYPAF 2188
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIAL------------------GL----------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2189 IFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
979-1180 |
3.19e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.39 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 979 VYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTT---TMSILTGLFP--PTSGSATIYGHDI---RTEMDEIRKNLGMC 1050
Cdd:PRK14239 13 VYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTDTVDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDrLTVEEHLWFYSRLKSMAQEEIrkeTDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1122
Cdd:PRK14239 92 FQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1123 RAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
985-1180 |
3.96e-23 |
|
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: 98.66 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 985 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCP---QHNVLFDR 1059
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 LTVEEHLwfysrlksmaqeeirketdkmiedlelsnkrhSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1139
Cdd:cd03215 93 LSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568912802 1140 RAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03215 141 AEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
976-1180 |
4.94e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 102.96 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYKNDKK--MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGM 1049
Cdd:PRK11153 7 ISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQH-NVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRAIIL- 1127
Cdd:PRK11153 87 IFQHfNLLSSR-TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR--VAIARALASNPKVLl 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1128 -DEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK11153 164 cDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
983-1186 |
6.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.46 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 983 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMCPQH--NVLF 1057
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1137
Cdd:PRK13636 97 SA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1138 ARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13636 176 GVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
987-1175 |
6.86e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG--HDIRTEMDEIRKNLGMCPQHNVLFDRLTVEE 1064
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLWF---YSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGmKRKLsVAI--AFVGGSRAIILDEPTAGVDPYAR 1139
Cdd:COG1129 99 NIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-QQQL-VEIarALSRDARVLILDEPTASLTEREV 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 568912802 1140 RAIWDLI--LKYKpGRTILLSTHHMDEADLLGDRIAII 1175
Cdd:COG1129 177 ERLFRIIrrLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
975-1180 |
8.62e-23 |
|
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: 98.01 E-value: 8.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 975 KLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGL--FPPTSGSATIYGHDIRteMDEIRKNLGMCPQ 1052
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD--KRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSmaqeeirketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03213 90 DDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1133 GVDPYARRAIWDLILKY-KPGRTILLSTHH-MDEADLLGDRIAIISHGKL 1180
Cdd:cd03213 141 GLDSSSALQVMSLLRRLaDTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2032-2252 |
2.11e-22 |
|
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: 98.56 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKigrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKDLLQVQQSL 2111
Cdd:cd03299 1 LKVENLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKTGRSVVL-TSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2252
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2049-2245 |
3.30e-22 |
|
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: 95.96 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2049 ILAVDRLCLG---------VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLLQ-VQQSLGYCP-- 2115
Cdd:cd03215 4 VLEVRGLSVKgavrdvsfeVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDaIRAGIAYVPed 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2116 -QFDALFDELTAREHLQLYTRLrgipwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEP 2194
Cdd:cd03215 84 rKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2195 TTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2031-2245 |
3.43e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.54 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVL----KDLL 2105
Cdd:COG1135 1 MIELENLSKTFPTKG-GPVTALDDVSLTIEKGEIFGIIGYSGAGK-STLiRCINLLERPTSGSVLVDGVDLTalseRELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPwKDEAQvvKWALEKLELTKYADKpAGTY----SGGNKRKLSTAIA 2181
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVP-KAEIR--KRVAELLELVGLSDK-ADAYpsqlSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2182 LIGYPAFIFLDEPTTGMDPKARRflwnLILDLIK-----TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTR----SILDLLKdinreLGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
976-1217 |
3.89e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.72 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQH- 1053
Cdd:PRK13652 9 LCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVGLVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 -NVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:PRK13652 88 dDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1133 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGAYGDGYRLTLVKQPAEP 1208
Cdd:PRK13652 167 GLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDLPSLPKLI 246
|
....*....
gi 568912802 1209 GTSQEPGLA 1217
Cdd:PRK13652 247 RSLQAQGIA 255
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
973-1179 |
4.30e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVY---KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKN--- 1046
Cdd:COG1101 4 LKNLSKTFnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKRAkyi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1047 --------LGMCPqhnvlfdRLTVEEHL----------WFYSRLKSMAQEEIRKETDKMieDLELSNKRHSLVQTLSGGM 1108
Cdd:COG1101 83 grvfqdpmMGTAP-------SMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLATL--GLGLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 1109 KRKLSVAIAFVGGSRAIILDEPTAGVDPyaRRAiwDLILKY------KPGRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDP--KTA--ALVLELtekiveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
981-1186 |
5.31e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 5.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 981 KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMDEIR-KNLGMCPQHNV 1055
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1056 LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1136 PYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK10070 197 PLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
980-1186 |
6.13e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsaTIYGHDIRTEMD---EIRKNLGMCPQH-NV 1055
Cdd:PRK13648 17 YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAITDDnfeKLRKHIGIVFQNpDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1056 LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:PRK13648 95 QFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1136 PYARRAIWDLILKYKPGR--TILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTP 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2029-2245 |
6.21e-22 |
|
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: 102.57 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ-- 2106
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 ------VQQSLGYCPQFDALFDELTAREHLqlyTRLRGIPWKDEAQVVKwALEKLELTKYADKPA--------GTYSGGN 2172
Cdd:TIGR03269 357 pdgrgrAKRYIGILHQEYDLYPHRTVLDNL---TEAIGLELPDELARMK-AVITLKMVGFDEEKAeeildkypDELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2173 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKArEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
987-1186 |
6.98e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.28 E-value: 6.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-----EMDEIRKNLGMCPQ--HNVLFDR 1059
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 lTVEEHLWFYSRLKSMAQEEIRKETDkmiEDLELSNKRHSLVQT----LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAR---EKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1136 PYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13649 178 PKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
980-1186 |
8.32e-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: 96.02 E-value: 8.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1058
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 ---RLTV-------EEHLWfySRLKSMAQEEIRKETDKMIEDLELSNKRHslvqtLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:cd03244 92 gtiRSNLdpfgeysDEELW--QALERVGLKEFVESLPGGLDTVVEEGGEN-----LSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1129 EPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDE-ADLlgDRIAIISHGKLKCCGSP 1186
Cdd:cd03244 165 EATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
970-1186 |
8.69e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 970 VVCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSA---TIYGHDIRTE-MDEIRK 1045
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNskiTVDGITLTAKtVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1046 NLGMCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1124
Cdd:PRK13640 85 KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1125 IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2032-2250 |
1.01e-21 |
|
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: 96.64 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQvQQSL 2111
Cdd:cd03296 3 IEVRNVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGI---PWKDE-AQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRserPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2188 FIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2054-2225 |
1.21e-21 |
|
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: 95.12 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2054 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLY 2133
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 TRLRGipwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA-IALIGYPAFIfLDEPTTGMDPKARRFLWNLILD 2212
Cdd:TIGR01189 98 AAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALArLWLSRRPLWI-LDEPTTALDKAGVALLAGLLRA 172
|
170
....*....|...
gi 568912802 2213 LIKTGRSVVLTSH 2225
Cdd:TIGR01189 173 HLARGGIVLLTTH 185
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2032-2245 |
1.29e-21 |
|
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: 96.94 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSR-------------------KIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2092
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2093 AFVNGHSVL----KDLLQVQ-QSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGT 2167
Cdd:cd03294 81 VLIDGQDIAamsrKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2168 YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
984-1197 |
1.61e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.72 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 984 KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE---IRKNLGMCPQHNVLFDRL 1060
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTakiMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1061 TVEEHL----WFYSRlkSMAQEEIRKetdkmIEDL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1134
Cdd:PRK11614 96 TVEENLamggFFAER--DQFQERIKW-----VYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1135 DPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK--LKCCGSPLFLKGAYGDGY 1197
Cdd:PRK11614 169 APIIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDALLANEAVRSAY 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
986-1186 |
1.69e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.21 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 986 MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCP--QHNVLFDRLTVE 1063
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1064 EHL-----------WFYSRLKSMAQEeiRKETDKM---------IEDLELSNKRHSlvqTLSGGMKRKLSVAIAFVGGSR 1123
Cdd:PRK11300 99 ENLlvaqhqqlktgLFSGLLKTPAFR--RAESEALdraatwlerVGLLEHANRQAG---NLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1124 AIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2028-2245 |
2.83e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2028 DNDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSV-LKDLL 2105
Cdd:COG1129 1 AEPLLEMRGISKSF-----GGVKALDGVSLELRPGEVHALLGENGAGK-STLmKILSGVYQPDSGEILLDGEPVrFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 Q--------VQQSLgycpqfdALFDELTAREHL---QLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKR 2174
Cdd:COG1129 75 DaqaagiaiIHQEL-------NLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2175 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
987-1185 |
2.89e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.57 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIR-KNLGMC-----PqhNVlFDRL 1060
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDEHEiARLGIGrkfqkP--TV-FEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1061 TVEEHL---------WFysrlKSMAQEEIRKETDKMIEDLE---LSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:COG4674 101 TVFENLelalkgdrgVF----ASLFARLTAEERDRIEEVLEtigLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 1129 EPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS 1185
Cdd:COG4674 177 EPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
982-1193 |
3.36e-21 |
|
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: 94.99 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 982 NDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1060
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1061 TVEEHLwFYSRLkSMAQEEIRKETDK-MIED--LELSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1133
Cdd:cd03253 90 TIGYNI-RYGRP-DATDEEVIEAAKAaQIHDkiMRFPDGYDTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1134 VDPYARRAIWDLILKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPLFL---KGAY 1193
Cdd:cd03253 168 LDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELlakGGLY 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
987-1161 |
3.54e-21 |
|
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: 100.13 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEH 1065
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1066 LwfysRL--KSMAQEEIRKETDKM-----IEDLE--LSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1136
Cdd:TIGR02868 429 L----RLarPDATDEELWAALERVgladwLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*
gi 568912802 1137 YARRAIWDLILKYKPGRTILLSTHH 1161
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITHH 529
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2031-2294 |
3.66e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.98 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkDLLQV--- 2107
Cdd:PRK11607 19 LLEIRNLTKSFDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV----DLSHVppy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2188 FIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS----IQHLKNRFGDGY 2262
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEF 249
|
250 260 270
....*....|....*....|....*....|..
gi 568912802 2263 MITVrtkssqnvkdvvrffnrNFPEAMLKERH 2294
Cdd:PRK11607 250 IGSV-----------------NVFEGVLKERQ 264
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2032-2245 |
3.89e-21 |
|
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: 92.49 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkdllqvqqsl 2111
Cdd:cd03216 1 LELRGITKRF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 gycpQFDALFDeltAREHlqlytrlrGIpwkdeaQVVkwalekleltkyadkpagtY--SGGNKRKLSTAIALIGYPAFI 2189
Cdd:cd03216 65 ----SFASPRD---ARRA--------GI------AMV-------------------YqlSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2190 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
983-1186 |
3.95e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.82 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 983 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQH-NVLFDR 1059
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNpETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 LTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1139
Cdd:PRK13644 93 RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568912802 1140 RAIWDLILK-YKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13644 173 IAVLERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEP 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
973-1191 |
5.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDK-KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKNLGM 1049
Cdd:PRK13650 7 VKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENvwDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRA--II 1126
Cdd:PRK13650 86 VFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR--VAIAGAVAMRPkiII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1127 LDEPTAGVDPYARRaiwDLI-----LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP--LFLKG 1191
Cdd:PRK13650 164 LDEATSMLDPEGRL---ELIktikgIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPreLFSRG 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
982-1191 |
6.65e-21 |
|
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: 93.83 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 982 NDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1060
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1061 TVEEHLwFYSRLKSMAQEEIR--KET--DKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03254 92 TIMENI-RLGRPNATDEEVIEaaKEAgaHDFIMKLP--NGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1133 GVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP--LFLKG 1191
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNA----DKILVLDDGKIIEEGTHdeLLAKK 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2033-2244 |
7.44e-21 |
|
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: 94.17 E-value: 7.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQVQ 2108
Cdd:cd03256 2 EVENLSKTYPNGKK----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDALFDELTAREHLqLYTRLRGIPW---------KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA 2179
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENV-LSGRLGRRSTwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2180 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2059-2225 |
8.77e-21 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 100.95 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTGDEST---TGGEAFVNGHSVLKDLlqvQQSLGYCPQFDALFDELTAREHLQLYTR 2135
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2136 LR---GIPWKDEAQVVKWALEKLELTKYADKPAGTYSGG----NKRKLSTAIALIGYPA-FIFLDEPTTGMDPKARRFLW 2207
Cdd:TIGR00956 863 LRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*...
gi 568912802 2208 NLILDLIKTGRSVVLTSH 2225
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIH 960
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
980-1181 |
1.07e-20 |
|
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: 91.61 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDr 1059
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 ltveehlwfysrlksmaqeeirketdkmiedlelSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1139
Cdd:cd03247 89 ----------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568912802 1140 RAIWDLILKYKPGRTILLSTHHmdeadLLG----DRIAIISHGKLK 1181
Cdd:cd03247 135 RQLLSLIFEVLKDKTLIWITHH-----LTGiehmDKILFLENGKII 175
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
987-1201 |
1.16e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-----EMDEIRKNLGMCPQ--HNVLFDR 1059
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 lTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSnkRHSLVQT---LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1136
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1137 YARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGAYGDGYRLTL 1201
Cdd:PRK13646 179 QSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPkeLFKDKKKLADWHIGL 247
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2032-2251 |
1.52e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.34 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---DLLQVQ 2108
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFD--ALFDElTAREHLQLYTRLRGIPWKDEAQVVKWALE--KLELTKYADKPAGTYSGGNKRKLSTAIALIG 2184
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2185 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2251
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
980-1185 |
1.71e-20 |
|
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: 92.93 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1058
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 RlTVEEHLWFYSRLKSMAQ-EEIRKETDKMIEDLELSNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1133
Cdd:cd03252 90 R-SIRDNIALADPGMSMERvIEAAKLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1134 VDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLKCCGS 1185
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2031-2225 |
2.19e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.40 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTkvykSRKIGRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQS 2110
Cdd:PRK13538 1 MLEARNLA----CERDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQLYTRLRGIPwkDEAQVVKwALEKLELTKYADKPAGTYSGGNKRKLSTA-IALIGYPAFI 2189
Cdd:PRK13538 76 LLYLGHQPGIKTELTALENLRFYQRLHGPG--DDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALArLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 568912802 2190 fLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2225
Cdd:PRK13538 153 -LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
2061-2246 |
3.21e-20 |
|
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: 91.59 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2061 PGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG----HSVLKDLLQVQQ-SLGYCPQFDALFDELTAREHLqLYTR 2135
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQrKIGLVFQQYALFPHLNVRENL-AFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2136 LRGIPWKDEAQVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK 2215
Cdd:cd03297 101 KRKRNREDRISVDE-LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|..
gi 568912802 2216 T-GRSVVLTSHSMEECEALCTRLAIMVNGRLR 2246
Cdd:cd03297 180 NlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
983-1186 |
3.26e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 983 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdiRT----EMdeirkNLGMCPQhnvlfd 1058
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVsallEL-----GAGFHPE------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 rLTVEEHLWFYSRLKSMAQEEIRKETDKmIEDL-ELSNKRHSLVQTLSGGMKRKLSVAIAFvggsrAI-----ILDEPTA 1132
Cdd:COG1134 103 -LTGRENIYLNGRLLGLSRKEIDEKFDE-IVEFaELGDFIDQPVKTYSSGMRARLAFAVAT-----AVdpdilLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1133 GVDPY----ARRAIWDLILKykpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:COG1134 176 VGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2031-2256 |
3.44e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQ 2108
Cdd:PRK09700 5 YISMAGIGK-----SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDALFDELTAREHL---QLYTR-LRGIP---WKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2181
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigRHLTKkVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2182 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2256
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2059-2225 |
3.44e-20 |
|
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: 90.77 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVLKDLlqvQQSLGYCPQFDALFDELTAREHLQLYTRL 2136
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2137 RGIpwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT 2216
Cdd:cd03232 107 RGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
....*....
gi 568912802 2217 GRSVVLTSH 2225
Cdd:cd03232 158 GQAILCTIH 166
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2029-2246 |
3.62e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkdllqvq 2108
Cdd:COG0488 313 KKVLELEGLSKSYGDKTL-----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETV-------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 qSLGYCPQ-FDALFDELTAREHLQlytrlRGIPWKDEAQVVKWaLEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYP 2186
Cdd:COG0488 379 -KIGYFDQhQEELDPDKTVLDELR-----DGAPGGTEQEVRGY-LGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2187 AFIFLDEPTTGMDPKARrflwNLILDLIKT--GrSVVLTSHSMEECEALCTRLAIMVNGRLR 2246
Cdd:COG0488 452 NVLLLDEPTNHLDIETL----EALEEALDDfpG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
987-1165 |
3.87e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtemdeirKNLGMCPQHNVLFDRL--TVEE 1064
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 ----HLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1140
Cdd:NF040873 77 lvamGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180
....*....|....*....|....*.
gi 568912802 1141 AIWDLILKY-KPGRTILLSTHHMDEA 1165
Cdd:NF040873 157 RIIALLAEEhARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2051-2245 |
4.21e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.83 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKDLLQVQQSLGYCPQF--DALF---- 2121
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKTVGIVFQNpdDQLFaptv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2122 DELTAREHLQLytrlrGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2201
Cdd:PRK13639 97 EEDVAFGPLNL-----GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568912802 2202 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
973-1176 |
4.64e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.23 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVY--KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEiRknlGMC 1050
Cdd:COG4525 6 VRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-R---GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568912802 1131 TAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIIS 1176
Cdd:COG4525 162 FGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
960-1186 |
5.87e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.63 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 960 MEEEPTHLPLVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTE 1039
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1040 MDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIR---KETDKMIEDLELSNKRhslVQTLSGGMKRKLSVAI 1116
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITprvMEALRMVQLEEFAQRK---PHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1117 AFVGGSRAIILDEPTAGVDpYARRAIWDLILKY---KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD-YKLRKQMQNELKAlqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2031-2245 |
6.67e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.71 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQ 2106
Cdd:PRK11153 1 MIELKNISKVFPQGG-RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPwkdEAQVVKWALEKLELTKYADKpAGTY----SGGNKRKLSTAIAL 2182
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTP---KAEIKARVTELLELVGLSDK-ADRYpaqlSGGQKQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2183 IGYPAFIFLDEPTTGMDPKARRflwnLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTR----SILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
976-1186 |
8.03e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNV 1055
Cdd:PRK11607 25 LTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1056 LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1136 PYARR----AIWDLILKYkpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK11607 182 KKLRDrmqlEVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
988-1186 |
8.90e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.37 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVL-FDrLTVEE- 1064
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAVLPQHSSLsFP-FTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 -HLWFYSRLKSMAQEEIrkETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFV--------GGSRAIILDEPTAGVD 1135
Cdd:PRK13548 97 vAMGRAPHGLSRAEDDA--LVAAALAQVDLAHLAGRDYPQLSGGEQQR--VQLARVlaqlwepdGPPRWLLLDEPTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1136 PY--------ARRaiwdliLKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13548 173 LAhqhhvlrlARQ------LAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
980-1161 |
9.38e-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: 89.73 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDR 1059
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 LTVEEHLWFYSRLKSMAQEEIrketDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1139
Cdd:TIGR01189 88 LSALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|...
gi 568912802 1140 RAIWDLILKY-KPGRTILLSTHH 1161
Cdd:TIGR01189 164 ALLAGLLRAHlARGGIVLLTTHQ 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
992-1180 |
1.23e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.09 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 992 SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLGMCP---QHNVLFDRLTVEE-- 1064
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYVPedrKGEGLVLDLSIREni 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 ---HLWFYSRLKSMAQEEIRKETDKMIEDLEL-SNKRHSLVQTLSGGMKRKlsVAIA--FVGGSRAIILDEPTAGVDPYA 1138
Cdd:COG1129 352 tlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPTRGIDVGA 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 1139 RRAIWDLILKY-KPGRTILLSTHHMDEadLLG--DRIAIISHGKL 1180
Cdd:COG1129 430 KAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
970-1186 |
1.27e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 96.73 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 970 VVCVDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNL 1047
Cdd:NF033858 1 VARLEGVSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1048 GMCPQ---HNvLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1124
Cdd:NF033858 79 AYMPQglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1125 IILDEPTAGVDPYARRAIWDLI---LKYKPGRTILLSTHHMDEADLLgDRIAIISHGKLKCCGSP 1186
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIdriRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
980-1179 |
1.37e-19 |
|
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: 89.98 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1058
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 RlTVEEHLwFYSRLKSmAQEEIRK-----ETDKMIEDLElsNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:cd03251 90 D-TVAENI-AYGRPGA-TREEVEEaaraaNAHEFIMELP--EGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1130 PTAGVDPYARRAIWDLILKYKPGRTIL-----LSThhMDEAdllgDRIAIISHGK 1179
Cdd:cd03251 165 ATSALDTESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
988-1178 |
1.50e-19 |
|
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: 89.83 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrtemDEIRKNLGMCPQHNVLFDRLTVEEH-- 1065
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRMVVFQNYSLLPWLTVRENia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1066 LWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1145
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 568912802 1146 ILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1178
Cdd:TIGR01184 157 LMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2051-2259 |
1.52e-19 |
|
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: 95.22 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLL--QVQQSLGYCPQFDALFDElTARE 2128
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD-LRDLDedDLRRRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2129 HLQLytrlrGIPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTG 2197
Cdd:COG4987 428 NLRL-----ARPDATDEELWA-ALERVGLGDWLAAlPDGldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2198 MDPKARRFLWNLILDLIKtGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2259
Cdd:COG4987 502 LDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2060-2264 |
1.92e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2060 RPGECFGLLGVNGAGKTS-----TFKMLTGdeSTTGGEAFVNGHSVlkDLLQVQQSLGYCPQFDALFDELTAREHLQLYT 2134
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2135 RLR---GIPWKDEAQVVKWALEKLELTKYADKPAGT------YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2205
Cdd:TIGR00955 125 HLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2206 LWNLILDLIKTGRSVVLTSH--SMEECEaLCTRLAIMVNGRLRCLGSIQHLKNRFGD-GYMI 2264
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDlGHPC 265
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
987-1186 |
2.01e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSA-----TIYGHDIRTEMDEIRKNLGMCPQ--HNVLFDR 1059
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 lTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNK--RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1137
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1138 ARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK13643 179 ARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
973-1186 |
3.05e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.07 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1052
Cdd:PRK10851 5 IANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWF----YSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:PRK10851 82 HYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1129 EPTAGVDPYARRAI--WDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK10851 162 EPFGALDAQVRKELrrWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
988-1209 |
3.10e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMC---PQHNVLFDrlT 1061
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYT--D 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1062 VEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1141
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1142 IWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGAYGDGYRLT---LVKQPAEPG 1209
Cdd:PRK13638 175 MIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPgeVFACTEAMEQAGLTqpwLVKLHTQLG 248
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
967-1186 |
4.22e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.34 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 967 LPLVVCVDKLTKVYkndkkmaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIrtEMDEI 1043
Cdd:TIGR00955 27 LRGCFCRERPRKHL-------LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1044 RKNLGMCPQHNVLFDRLTVEEHLWFYSRLK---SMAQEEIRKETDKMIEDLELSNKRHSLVQT------LSGGMKRKLSV 1114
Cdd:TIGR00955 98 RAISAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1115 AIAFVGGSRAIILDEPTAGVDPYAR----RAIWDLILKykpGRTILLSTHHmDEADL--LGDRIAIISHGKLKCCGSP 1186
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAysvvQVLKGLAQK---GKTIICTIHQ-PSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2032-2245 |
4.99e-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: 87.85 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKD--LLQV 2107
Cdd:cd03292 1 IEFINVTKTYP----NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdLRGraIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2188 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
973-1174 |
7.21e-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: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIRT----EMDEI 1043
Cdd:COG0444 4 VRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1044 R-KNLGMCPQhnvlfD-------RLTVEEHLW-FYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQ---TLSGGMKRK 1111
Cdd:COG0444 84 RgREIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1112 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAI 1174
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2049-2245 |
7.33e-19 |
|
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: 87.65 E-value: 7.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2049 ILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAR 2127
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2128 EHLQLytrlrGIPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2196
Cdd:cd03245 96 DNITL-----GAPLADDERILR-AAELAGVTDFVNKhPNGldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2197 GMDPKA-RRFLWNliLDLIKTGRSVVLTSH--SMEEceaLCTRLAIMVNGRL 2245
Cdd:cd03245 170 AMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGRI 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2034-2225 |
8.59e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2034 IENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkdllqvqQSLGY 2113
Cdd:COG0488 1 LENLSKSFGGRPL-----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2114 CPQFDALFDELTAREHL--------QLYTRLRGIP-------------------------WKDEAQVVKwALEKLELTK- 2159
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVldgdaelrALEAELEELEaklaepdedlerlaelqeefealggWEAEARAEE-ILSGLGFPEe 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2160 YADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLildLIKTGRSVVLTSH 2225
Cdd:COG0488 145 DLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LKNYPGTVLVVSH 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2031-2240 |
8.70e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.38 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdllqvqqs 2110
Cdd:COG4525 3 MLTVRHVSVRYPGGG-QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 lgycP--------QFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIAL 2182
Cdd:COG4525 74 ----PgadrgvvfQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2183 IGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIM 2240
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2000-2259 |
1.37e-18 |
|
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: 92.97 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2000 QRL-PVSTKPVEDDVDVASERQRVLRGDadndmVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTST 2078
Cdd:COG2274 446 ERLdDILDLPPEREEGRSKLSLPRLKGD-----IELENVSFRYPGDSP---PVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2079 FKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREHLQLytrlrGIPWKDEAQVVkWALEKLEL 2157
Cdd:COG2274 518 LKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITL-----GDPDATDEEII-EAARLAGL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2158 TKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHS 2226
Cdd:COG2274 591 HDFIEAlPMGydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHR 669
|
250 260 270
....*....|....*....|....*....|...
gi 568912802 2227 MeECEALCTRLAIMVNGRLRCLGSIQHLKNRFG 2259
Cdd:COG2274 670 L-STIRLADRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
987-1187 |
1.46e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT------EMDEIRKNLGMC---PQHNVLF 1057
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikEVKRLRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DrlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSN---KRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1134
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyvKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1135 DPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPL 1187
Cdd:PRK13645 182 DPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
987-1184 |
1.52e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.77 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCPQHNVLFDRLTVEE 1064
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLwFYSRL---KSMA-----QEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1136
Cdd:PRK09700 100 NL-YIGRHltkKVCGvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1137 YARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1184
Cdd:PRK09700 179 KEVDYLFLIMnqLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2031-2245 |
2.01e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.07 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL---KDLLQV 2107
Cdd:PRK09493 1 MIEFKNVSKHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQFDALFDELTAREHLQL-YTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2186
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2187 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
979-1180 |
2.28e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 979 VYKNDKKMALNKL---SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQH- 1053
Cdd:PRK13642 11 VFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1133
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568912802 1134 VDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKL 1180
Cdd:PRK13642 171 LDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
960-1186 |
2.32e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.75 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 960 MEEEPTHLPLVVCVDKLTKVY---KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI----Y 1032
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYCVFdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1033 GHDIRTEMD-------------EIRKNLGMC---PQHNVLFDrlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSN- 1095
Cdd:PRK13631 91 GDKKNNHELitnpyskkiknfkELRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDs 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1096 --KRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRI 1172
Cdd:PRK13631 169 ylERSPF--GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEVADEV 246
|
250
....*....|....
gi 568912802 1173 AIISHGKLKCCGSP 1186
Cdd:PRK13631 247 IVMDKGKILKTGTP 260
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
2051-2229 |
4.15e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.59 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvlkdllqvqqSLGYCPQFDALFDEL--TARE 2128
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2129 --------HLQLYTRLRgipwKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2200
Cdd:NF040873 77 lvamgrwaRRGLWRRLT----RDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*....
gi 568912802 2201 KARRFLWNLILDLIKTGRSVVLTSHSMEE 2229
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2049-2245 |
4.51e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2049 ILAVDRLC--------LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQQSLGYCP--- 2115
Cdd:PRK15439 268 VLTVEDLTgegfrnisLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2116 QFDALFDELTAREHLQLYTRLRGIPWKDEAQvvkwalEKLELTKY----------ADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:PRK15439 348 QSSGLYLDAPLAWNVCALTHNRRGFWIKPAR------ENAVLERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
983-1161 |
4.63e-18 |
|
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: 84.85 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 983 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTV 1062
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1063 EEHLWFYSRLKSMAQEEirketdKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1142
Cdd:cd03231 91 LENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 568912802 1143 WDLILKY-KPGRTILLSTHH 1161
Cdd:cd03231 165 AEAMAGHcARGGMVVLTTHQ 184
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
987-1180 |
4.87e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.83 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDE-----IRKNLGMCPQHNVLFDR 1059
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairlLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 LTVEEHLWFYS-RLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1138
Cdd:COG4161 97 LTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568912802 1139 RRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:COG4161 177 TAQVVEIIRELSqTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
979-1185 |
5.07e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 979 VYKNDKKMaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP------PTSGSATIYGHDI-RTEMDEIRKNLGMCP 1051
Cdd:PRK14246 18 LYINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRLTVEEHLWFysRLKSMAQEEiRKETDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSR 1123
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAY--PLKSHGIKE-KREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1124 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS 1185
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2032-2245 |
5.37e-18 |
|
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: 84.89 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL---KDLLQVQ 2108
Cdd:cd03262 1 IEIKNLHKSFGDFHV-----LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDALFDELTAREHLQL-YTRLRGIPwKDEAQvvKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIG 2184
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMS-KAEAE--ERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2185 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
988-1193 |
5.96e-18 |
|
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: 85.67 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHL 1066
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1067 WF--YSRLKSMAQEEIRK-ETDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1139
Cdd:cd03249 98 RYgkPDATDEEVEEAAKKaNIHDFIMSLP--DGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1140 RAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP---LFLKGAY 1193
Cdd:cd03249 176 KLVQEALDRAMKGRTTIVIAHRLStirNA----DLIAVLQNGQVVEQGTHdelMAQKGVY 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2028-2245 |
1.14e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2028 DNDMVKIENLTKVYKSRKIG-RILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG--HSVLKDL 2104
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEStEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2105 LQVQQSLGYCPQ------FDALFDELTA--REHLqlytrlrGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKL 2176
Cdd:PRK13633 81 WDIRNKAGMVFQnpdnqiVATIVEEDVAfgPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2177 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECeALCTRLAIMVNGRL 2245
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
974-1181 |
1.17e-17 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 85.25 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 974 DKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdirtEMDEIRKNLGMCPQh 1053
Cdd:PRK13546 26 DALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 nvlfdrLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP-TA 1132
Cdd:PRK13546 100 ------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1133 GVDPYARRAIwDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLK 1181
Cdd:PRK13546 174 GDQTFAQKCL-DKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2052-2249 |
1.67e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2052 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLLQVQQSLGYCPQFDALFDELTAREHL 2130
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2131 QL-----YTRLRGIPWKDEAqVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD-PKARR 2204
Cdd:PRK09536 99 EMgrtphRSRFDTWTETDRA-AVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 2205 FLwNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2249
Cdd:PRK09536 178 TL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
973-1180 |
1.68e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKM-----ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-------- 1039
Cdd:PRK13651 5 VKNIVKIF--NKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1040 -----------------MDEIRKNLGMCPQ--HNVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIE--DLELSNKRH 1098
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIElvGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1099 SLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISH 1177
Cdd:PRK13651 162 SPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
...
gi 568912802 1178 GKL 1180
Cdd:PRK13651 241 GKI 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
974-1180 |
2.34e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.39 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 974 DKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGM 1049
Cdd:PRK10908 5 EHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQ-HNVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:PRK10908 84 IFQdHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1129 EPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
999-1180 |
2.48e-17 |
|
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: 83.11 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 999 QVVSFLGHNGAGKTTTMSILTGLFPPTSGsaTIYGHDirTEMDEIRKNLGMCP---------QHNVLFDRLTVEEHLWFy 1069
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGG--TIVLNG--TVLFDSRKKINLPPqqrkiglvfQQYALFPHLNVRENLAF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1070 sRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY 1149
Cdd:cd03297 99 -GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|...
gi 568912802 1150 KP--GRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:cd03297 178 KKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
970-1178 |
3.18e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.91 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 970 VVCVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP--PTSGS-ATIYGHDIRTE---MDEI 1043
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQREgrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1044 RKN---LGMCPQHNVLFDRLTVEEHLW--------FYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKL 1112
Cdd:PRK09984 82 RKSranTGYIFQQFNLVNRLSVLENVLigalgstpFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1113 SVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHG 1178
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
991-1160 |
3.24e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 991 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGmcpQHNVLFDRLTVEEHLWFY 1069
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG---HRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1070 SRLKSMAQEEIrketDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY 1149
Cdd:PRK13539 98 AAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|..
gi 568912802 1150 -KPGRTILLSTH 1160
Cdd:PRK13539 174 lAQGGIVIAATH 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
985-1178 |
3.80e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.60 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 985 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEirknLGMCPQHNVLFDRLTVEE 1064
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWD 1144
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 568912802 1145 LILK--YKPGRTILLSTHHMDEADLLGDRIAIISHG 1178
Cdd:PRK11248 170 LLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2032-2244 |
3.98e-17 |
|
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: 81.28 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQS 2110
Cdd:cd03228 1 IEFKNVSFSYPGRPK---PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDElTAREHLqlytrlrgipwkdeaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2191 LDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMEECEaLCTRLAIMVNGR 2244
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
973-1180 |
6.23e-17 |
|
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: 80.72 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1051
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDrltveehlwfysrlKSMAqEEIrketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:cd03246 83 QDDELFS--------------GSIA-ENI-----------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1132 AGVDPYARRAIWDLI--LKyKPGRTILLSTHHMdEADLLGDRIAIISHGKL 1180
Cdd:cd03246 125 SHLDVEGERALNQAIaaLK-AAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2031-2250 |
6.41e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLL--QVQ 2108
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKP-ISMLSsrQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDALFDELTARE--------HLQLYTRLRGipwKDEaQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAI 2180
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRElvaygrspWLSLWGRLSA---EDN-ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2181 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
973-1180 |
6.85e-17 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 82.96 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE------ 1042
Cdd:TIGR02323 6 VSGLSKSYGGGK--GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAElelyQLSEaerrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1043 IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQE---EIRKETDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIAF 1118
Cdd:TIGR02323 84 MRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1119 VGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
962-1181 |
1.12e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 962 EEPTHLP-LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIRtem 1040
Cdd:COG0488 306 PPPERLGkKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1041 deirknLGMCPQHNVLFD-RLTVEEHLWfysRLKSMAQE-EIRketdKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIA 1117
Cdd:COG0488 380 ------IGYFDQHQEELDpDKTVLDELR---DGAPGGTEqEVR----GYLGRFLFSGDDaFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1118 FVGGSRAIILDEPTAGVDPYARRAIWDLILKYkPGrTILLSTHHMDEADLLGDRIAIISHGKLK 1181
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
952-1180 |
1.19e-16 |
|
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: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 952 RHFEETRGMEEepthlplvvcVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI 1031
Cdd:TIGR02203 322 RAIERARGDVE----------FRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1032 YGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHLwFYSRLKSMAQEEIRkETDKMIEDLELSNKRHSLVQT------- 1103
Cdd:TIGR02203 392 DGHDLADyTLASLRRQVALVSQDVVLFND-TIANNI-AYGRTEQADRAEIE-RALAAAYAQDFVDKLPLGLDTpigengv 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1104 -LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1180
Cdd:TIGR02203 469 lLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2029-2254 |
1.22e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQvQ 2108
Cdd:PRK11432 4 KNFVVLKNITKRF-----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2188
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2189 IFLDEPTTGMDPKARRFLWNLILDLIKtgrSVVLTS----HSMEECEALCTRLAIMVNGRLRCLGSIQHL 2254
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQ---QFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2031-2244 |
1.33e-16 |
|
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: 81.33 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIG--RILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQV- 2107
Cdd:COG4778 4 LLEVENLSKTFTLHLQGgkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQAs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 --------QQSLGYCPQF-------DALfdELTArEHLqlytRLRGIPwKDEAQV-VKWALEKLEL-TKYADKPAGTYSG 2170
Cdd:COG4778 84 preilalrRRTIGYVSQFlrviprvSAL--DVVA-EPL----LERGVD-REEARArARELLARLNLpERLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2171 GNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
987-1186 |
1.45e-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: 85.62 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIR--------KNLGMCPQHNVLFD 1058
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGpdgrgrakRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 RLTVEEHLWFYSRLKSMAQEEIRKE--TDKMI--EDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1134
Cdd:TIGR03269 379 HRTVLDNLTEAIGLELPDELARMKAviTLKMVgfDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1135 DPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:TIGR03269 459 DPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
2031-2250 |
1.77e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTG----GEAFVNGHSVLKDLL 2105
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGkvtvGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQQSLGYCPQF--DALFDElTAREHLQLYTRLRGIPwKDEAQvvKWALEKLELT----KYADKPAGTYSGGNKRKLSTA 2179
Cdd:PRK13643 81 PVRKKVGVVFQFpeSQLFEE-TVLKDVAFGPQNFGIP-KEKAE--KIAAEKLEMVgladEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2180 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
987-1180 |
2.12e-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: 85.56 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEH 1065
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1066 LWFYSRLKSMAQE--------EIRKETDKMIEDLELSNKRHSlvQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1137
Cdd:TIGR01193 568 LLLGAKENVSQDEiwaaceiaEIKDDIENMPLGYQTELSEEG--SSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568912802 1138 ARRAIWDLILKYKPgRTILLSTHHMDEADLLgDRIAIISHGKL 1180
Cdd:TIGR01193 646 TEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
968-1166 |
2.51e-16 |
|
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: 85.03 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 968 PLVVCVDKLTKVYkNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKN 1046
Cdd:TIGR02857 319 ASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1047 LGMCPQHNVLFDRlTVEEHLWFYSRLKS---MAQEEIRKETDKMIEDLELSnkRHSLV----QTLSGGMKRKLSVAIAFV 1119
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIRLARPDASdaeIREALERAGLDEFVAALPQG--LDTPIgeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1120 GGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTH---HMDEAD 1166
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1064-1194 |
3.08e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.86 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1064 EHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1143
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1144 DLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGAYG 1194
Cdd:NF000106 185 DEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2031-2245 |
3.49e-16 |
|
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: 82.02 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVL----KD 2103
Cdd:COG0444 1 LLEVRNLKVYFPTRR-GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLklseKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2104 LLQV-QQSLGYCPQ--FDAL---------FDElTAREHlqlytrlRGIPWKDEAQVVKWALEKLELT---KYADKPAGTY 2168
Cdd:COG0444 80 LRKIrGREIQMIFQdpMTSLnpvmtvgdqIAE-PLRIH-------GGLSKAEARERAIELLERVGLPdpeRRLDRYPHEL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2169 SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
986-1180 |
3.51e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 986 MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLF-----PPTSGSATIYGHDIRTE-MD--EIRKNLGMCPQHNVLF 1057
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPdVDpiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DRLTVEEHLWFYSRLKSMAQEeiRKETDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKS--KKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1130 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2054-2225 |
4.66e-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: 79.07 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2054 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLY 2133
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 TRLRGipwkDEAqvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2213
Cdd:cd03231 98 HADHS----DEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|..
gi 568912802 2214 IKTGRSVVLTSH 2225
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
973-1186 |
4.72e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.44 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGMCP 1051
Cdd:PRK11231 5 TENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRLTVEE--------HLWFYSRLKSMAQEEIRKETDKMiEDLELSNKRhslVQTLSGGMKRKLSVAIAFVGGSR 1123
Cdd:PRK11231 83 QHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQT-RINHLADRR---LTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1124 AIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2031-2262 |
5.15e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrILAVDrlcLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSV------L 2101
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA--LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVqregrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2102 KDLLQVQQSLGYCPQFDALFDELTAREHLqLYTRLRGIP-WK--------DEAQVVKWALEKLELTKYADKPAGTYSGGN 2172
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPfWRtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2173 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2251
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
250
....*....|..
gi 568912802 2252 QHLKN-RFGDGY 2262
Cdd:PRK09984 238 QQFDNeRFDHLY 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2035-2279 |
5.97e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2035 ENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLLQVQ-Q 2109
Cdd:PRK10070 27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVRrK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 SLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2189
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2190 FLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMIT--- 2265
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTffr 266
|
250
....*....|....*
gi 568912802 2266 -VRTKSSQNVKDVVR 2279
Cdd:PRK10070 267 gVDISQVFSAKDIAR 281
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2032-2259 |
6.40e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.41 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--KDLLQVQQ 2109
Cdd:NF033858 2 ARLEGVSHRY-----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdaRHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 SLGYCPQF--DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:NF033858 77 RIAYMPQGlgKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2188 FIFLDEPTTGMDPKARRFLWNLIlDLIKTGR---SVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2259
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELI-DRIRAERpgmSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2028-2245 |
6.89e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.42 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2028 DNDMVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVLKD-LL 2105
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEN---NALKNVSFEINEGEYVAILGHNGSGK-STIsKILTGLLKPQSGEIKIDGITISKEnLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQQSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIG 2184
Cdd:PRK13632 80 EIRKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2185 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2245
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKL 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
988-1186 |
9.96e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.98 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---TEMDEIRKNLGMCPQHNVLFDRLTVEE 1064
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVFQQFYLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLWFYS-RLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR---- 1139
Cdd:PRK09493 97 NVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRhevl 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568912802 1140 RAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK09493 177 KVMQDLA---EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2066-2257 |
1.03e-15 |
|
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: 81.31 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2066 GLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhSVLKD------LLQVQQSLGYCPQFDALFDELTAREHLQL-YTRLRG 2138
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-RTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYgMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2139 ipwkdEAQVVKWA--LEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARR----FLWNLILD 2212
Cdd:TIGR02142 106 -----SERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYeilpYLERLHAE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 2213 LiktGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNR 2257
Cdd:TIGR02142 181 F---GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2031-2245 |
1.03e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQ 2106
Cdd:COG3845 5 ALELRGITKRF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 -----VQQslgycpQFdALFDELTAREHLQLY---TRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLST 2178
Cdd:COG3845 80 lgigmVHQ------HF-MLVPNLTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2179 AIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2051-2264 |
1.06e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKDLLQVQQSLGYCPQ------FDALF 2121
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQdpdnqlFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2122 DELTAREHLQLytrlrGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2201
Cdd:PRK13636 101 YQDVSFGAVNL-----KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2202 ARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLknrFGDGYMI 2264
Cdd:PRK13636 176 GVSEIMKLLVEMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV---FAEKEML 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
987-1186 |
2.31e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDE-----IRKNLGMCPQHNVLFDR 1059
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkaireLRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 LTVEEHLWFYS-RLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1138
Cdd:PRK11124 97 LTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1139 RRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIA------IISHGKLKCCGSP 1186
Cdd:PRK11124 177 TAQIVSIIRELaETGITQVIVTHEVEVARKTASRVVymenghIVEQGDASCFTQP 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2030-2293 |
2.37e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2030 DMVKIENLTKVYKSRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKD-LLQVQ 2108
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKYTL--NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2188 FIFLDEPTTGMDPKARrflwnliLDLIKTGRS--------VVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFG 2259
Cdd:PRK13650 161 IIILDEATSMLDPEGR-------LELIKTIKGirddyqmtVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
250 260 270
....*....|....*....|....*....|....
gi 568912802 2260 DGYMITVRTKSSQNVKDVVRFFNRNFPEAMLKER 2293
Cdd:PRK13650 233 DLLQLGLDIPFTTSLVQSLRQNGYDLPEGYLTEK 266
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
2057-2251 |
4.14e-15 |
|
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: 77.12 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2057 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---DLLQVQQSLgycpqfdALFDELTAREHLQLY 2133
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNY-------SLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 TR--LRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2211
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568912802 2212 DLIKTGR-SVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2251
Cdd:TIGR01184 159 QIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
978-1197 |
4.16e-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: 76.03 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 978 KVYKNDKKMaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGlFP---PTSGSATIYGHDIrTEM--DEI-RKNLGMCP 1051
Cdd:cd03217 7 HVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLppEERaRLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRLTVEEHLwfysrlksmaqeeirketdkmiedlelsnkrHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:cd03217 84 QYPPEIPGVKNADFL-------------------------------RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1132 AGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLL-GDRIAIISHGKLKCCGSPLFLKGAYGDGY 1197
Cdd:cd03217 133 SGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2052-2245 |
4.45e-15 |
|
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: 75.33 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2052 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREHL 2130
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2131 qlytrlrgipwkdeaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2210
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*
gi 568912802 2211 LDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRL 2245
Cdd:cd03246 140 AALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
960-1180 |
4.58e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.38 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 960 MEEEPTHLPLVVCVDKLTkVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTT---TMSILTGLFPP--TSGSATIYGH 1034
Cdd:COG1117 1 MTAPASTLEPKIEVRNLN-VYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1035 DIRT-EMD--EIRKNLGMCPQH----------NVLFD-RLtveeHlwfysRLKSmaqeeiRKETDKMIEDL--------E 1092
Cdd:COG1117 79 DIYDpDVDvvELRRRVGMVFQKpnpfpksiydNVAYGlRL----H-----GIKS------KSELDEIVEESlrkaalwdE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1093 LSNKRHSLVQTLSGGMKRKLSVAiafvggsRAI------IL-DEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEA 1165
Cdd:COG1117 144 VKDRLKKSALGLSGGQQQRLCIA-------RALavepevLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQA 216
|
250
....*....|....*
gi 568912802 1166 DLLGDRIAIISHGKL 1180
Cdd:COG1117 217 ARVSDYTAFFYLGEL 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
984-1186 |
4.86e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.99 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 984 KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNVLFDRLTVE 1063
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1064 EHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1143
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 1144 DLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK11432 177 EKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
988-1180 |
4.87e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMD----------EIRKN----LGMCP 1051
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDglangivyisEDRKRdglvLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVlfdRLTVEEHLwfysrlkSMAQEEIRKETDKM-IED-LELSN-KRHSLVQT---LSGGMKRKLSVAIAFVGGSRAI 1125
Cdd:PRK10762 348 KENM---SLTALRYF-------SRAGGSLKHADEQQaVSDfIRLFNiKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1126 ILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEadLLG--DRIAIISHGKL 1180
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
980-1193 |
5.26e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE--IRKNLGMCPQHNVLF 1057
Cdd:PRK11160 348 YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DRlTVEEHLwfysrlkSMAQEEIRKEtdKMIEDLE---LSNkrhsLVQT--------------LSGGMKRKLSVAIAFVG 1120
Cdd:PRK11160 427 SA-TLRDNL-------LLAAPNASDE--ALIEVLQqvgLEK----LLEDdkglnawlgeggrqLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1121 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTH------HMdeadllgDRIAIISHGKLKCCGS---PLFLKG 1191
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltgleQF-------DRICVMDNGQIIEQGThqeLLAQQG 565
|
..
gi 568912802 1192 AY 1193
Cdd:PRK11160 566 RY 567
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2060-2225 |
6.56e-15 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 81.43 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2060 RPGECFGLLGVNGAGKTSTFKMLTGDEstTGGeaFVNGHSVLKDLLQVQQSL----GYCPQFDALFDELTAREHL--QLY 2133
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESLiySAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 TRLRGIPWKDEAQV-VKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLW 2207
Cdd:PLN03140 980 LRLPKEVSKEEKMMfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
170
....*....|....*...
gi 568912802 2208 NLILDLIKTGRSVVLTSH 2225
Cdd:PLN03140 1060 RTVRNTVDTGRTVVCTIH 1077
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2032-2258 |
7.12e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.84 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL------KDLL 2105
Cdd:PRK09452 15 VELRGISKSFDGKEV-----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvpaenRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQQSlgYcpqfdALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:PRK09452 90 TVFQS--Y-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRF 2258
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
973-1180 |
7.16e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTkVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKnLGMC 1050
Cdd:COG3845 260 VENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSprERRR-LGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 -----PQHNVLFDRLTVEEHLWF-------YSRLKSMAQEEIRKETDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIA 1117
Cdd:COG3845 337 yipedRLGRGLVPDMSVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDVRTPGpDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1118 FVGGSRAIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2031-2252 |
7.76e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.69 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLLQVQQS 2110
Cdd:COG4559 1 MLEAENLSVRLGGRTL-----LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP-LAAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 --LGYCPQFDAL-FDeLTAREHLqlytRLRGIPW----KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2183
Cdd:COG4559 75 rrRAVLPQHSSLaFP-FTVEEVV----ALGRAPHgssaAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2184 -------GYPAFIFLDEPTTGMDPK--------ARRFLwnlildliKTGRSVV-------LTSHsmeeceaLCTRLAIMV 2241
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAhqhavlrlARQLA--------RRGGGVVavlhdlnLAAQ-------YADRILLLH 214
|
250
....*....|.
gi 568912802 2242 NGRLRCLGSIQ 2252
Cdd:COG4559 215 QGRLVAQGTPE 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2041-2253 |
8.03e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2041 YKSRKIGRI-LAVDRL---------CLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDllQ 2106
Cdd:PRK11288 248 YRPRPLGEVrLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirspRD--A 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQ---FDALFDELTAREHLQLYTRLRGIPW------KDEAQVVKWALEKLEL-TKYADKPAGTYSGGNKRK- 2175
Cdd:PRK11288 326 IRAGIMLCPEdrkAEGIIPVHSVADNINISARRHHLRAgclinnRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKa 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2176 -----LSTAIALIgypafiFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRclGS 2250
Cdd:PRK11288 406 ilgrwLSEDMKVI------LLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GE 477
|
...
gi 568912802 2251 IQH 2253
Cdd:PRK11288 478 LAR 480
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2026-2254 |
8.16e-15 |
|
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: 80.19 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2026 DADNDMVKIENLTKVYKSRKigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DL 2104
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGR----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2105 LQVQQSLGYCPQFDALFdELTAREHLQLYTrlrgiPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNK 2173
Cdd:COG4988 407 ASWRRQIAWVPQNPYLF-AGTIRENLRLGR-----PDASDEELEA-ALEAAGLDEFVAAlPDGldtplgeggrGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2174 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQH 2253
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEE 557
|
.
gi 568912802 2254 L 2254
Cdd:COG4988 558 L 558
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
990-1186 |
1.08e-14 |
|
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: 78.23 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 990 KLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-----RKNLGMCPQHNVLFDRLTVEE 1064
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLwFYSRLKSMAqEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD--------P 1136
Cdd:TIGR02142 95 NL-RYGMKRARP-SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdprkyeilP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1137 YARRaiwdliLKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:TIGR02142 173 YLER------LHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
988-1180 |
1.29e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.10 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLF-----PPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVLFDRLT 1061
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1062 VEEHLWFYSRLKSMA------QEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:PRK14247 99 IFENVALGLKLNRLVkskkelQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 1136 PYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2009-2245 |
1.43e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2009 VEDDVDVASERQRVLRGDAdndMVKIENLTkVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDEST 2088
Cdd:COG3845 238 VGREVLLRVEKAPAEPGEV---VLEVENLS-VRDDRGV---PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2089 TGGEAFVNGHSVL-KDLLQVQQS-LGYCP---QFDALFDELTAREHLQLyTRLRGIP-----WKDEAQVVKWALEKLElt 2158
Cdd:COG3845 311 ASGSIRLDGEDITgLSPRERRRLgVAYIPedrLGRGLVPDMSVAENLIL-GRYRRPPfsrggFLDRKAIRAFAEELIE-- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2159 KY------ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEA 2232
Cdd:COG3845 388 EFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILA 467
|
250
....*....|...
gi 568912802 2233 LCTRLAIMVNGRL 2245
Cdd:COG3845 468 LSDRIAVMYEGRI 480
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2031-2252 |
1.44e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.96 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDL--LQVQ 2108
Cdd:PRK13548 2 MLEARNLSV-----RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWspAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQFDAL-FDeLTAREhlqlYTRLRGIPW----KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2183
Cdd:PRK13548 76 RRRAVLPQHSSLsFP-FTVEE----VVAMGRAPHglsrAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2184 ------GYPAFIFLDEPTTGMDPK--------ARRFLWnlildliKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2249
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAhqhhvlrlARQLAH-------ERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
...
gi 568912802 2250 SIQ 2252
Cdd:PRK13548 224 TPA 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2050-2245 |
1.62e-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: 73.89 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2050 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDElTAREH 2129
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2130 LqlytrlrGIPwkdeaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNL 2209
Cdd:cd03247 95 L-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 568912802 2210 ILDLIKtGRSVVLTSHSMEECEALcTRLAIMVNGRL 2245
Cdd:cd03247 141 IFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
964-1180 |
1.73e-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: 75.20 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 964 PTHLPLVVCVDKLTKVYKN-DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMD 1041
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1042 EIRKNLGMCPQHNVLFDRlTVEEHLWFysRLKSMAQEEIRKETDK-----MIEDLEL-----SNKRHSLvqtLSGGMKRK 1111
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAY--GLQSCSFECVKEAAQKahahsFISELASgydteVGEKGSQ---LSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1112 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1180
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2049-2245 |
1.81e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2049 ILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLLQ-----VQQSLGYCPqfda 2119
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAagvaiIYQELHLVP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2120 lfdELTAREHL---QLYTRLrGipWKDEAQVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDE 2193
Cdd:PRK11288 93 ---EMTVAENLylgQLPHKG-G--IVNRRLLNYEAREQLEhlgVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2194 PTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2057-2246 |
1.85e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2057 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLLQVQ------QSLGYCPQFDALFDELTAREHL 2130
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2131 QLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2210
Cdd:PRK10584 110 ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 568912802 2211 LDLIKT-GRSVVLTSHSmEECEALCTRLAIMVNGRLR 2246
Cdd:PRK10584 190 FSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2055-2226 |
2.18e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2055 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkDLLQVQQSLGYCPQFDALFDELTAREHLQLYT 2134
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2135 RLRGipwKDEAQVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY-PAFIfLDEPTTGMDPKARRFLWNLILDL 2213
Cdd:PRK13539 99 AFLG---GEELDIAA-ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNrPIWI-LDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|...
gi 568912802 2214 IKTGRSVVLTSHS 2226
Cdd:PRK13539 174 LAQGGIVIAATHI 186
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2057-2245 |
2.29e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2057 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG-----HSVLKDLLQVQQSLGYCPQF--DALFDElTAREH 2129
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitsTSKNKDIKQIRKKVGLVFQFpeSQLFEE-TVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2130 LQLYTRLRGIPwKDEAQvvKWALEKLELTKYA----DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2205
Cdd:PRK13649 107 VAFGPQNFGVS-QEEAE--ALAREKLALVGISeslfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568912802 2206 LWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2044-2244 |
2.63e-14 |
|
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: 78.33 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2044 RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVL---------KDLLQVQQSLg 2112
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKasnirdterAGIVIIHQEL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2113 ycpqfdALFDELTAREHLQLYTR--LRGIPWKDEAQVVKWA--LEKLELTKYAD-KPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:TIGR02633 88 ------TLVPELSVAENIFLGNEitLPGGRMAYNAMYLRAKnlLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2188 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2031-2232 |
2.74e-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: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDES---TTGGEAFVNGHSVlkDLLQV 2107
Cdd:COG4136 1 MLSLENLTITLGGRPL-----LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRL--TALPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQ-SLGYCPQFDALFDELTAREHLQLYTRlRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2186
Cdd:COG4136 74 EQrRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 2187 AFIFLDEPTTGMDP----KARRFLWNLILDLiktGRSVVLTSHSMEECEA 2232
Cdd:COG4136 153 RALLLDEPFSKLDAalraQFREFVFEQIRQR---GIPALLVTHDEEDAPA 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2032-2225 |
3.13e-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: 72.10 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILAvdrlcLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEafVNGHSVLKdllqvqqsL 2111
Cdd:cd03221 1 IELENLSKTYGGKLLLKDIS-----LTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--VTWGSTVK--------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFdalfdeltarehlqlytrlrgipwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03221 66 GYFEQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....
gi 568912802 2192 DEPTTGMDPKARRFLWNLildLIKTGRSVVLTSH 2225
Cdd:cd03221 95 DEPTNHLDLESIEALEEA---LKEYPGTVILVSH 125
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2031-2245 |
3.24e-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: 75.23 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKS----RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---- 2102
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2103 -------DLLQV-QQSLG-YCPQFDAlfdELTAREHLQLYTRLrgipwkDEAQVVKWALEKLEL----TKYADKPAGTYS 2169
Cdd:TIGR02769 82 qrrafrrDVQLVfQDSPSaVNPRMTV---RQIIGEPLRHLTSL------DESEQKARIAELLDMvglrSEDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2170 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDpkarRFLWNLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
.
gi 568912802 2245 L 2245
Cdd:TIGR02769 229 I 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
971-1179 |
3.26e-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: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsatiyghdirtemdeirknlgmc 1050
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG----------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 pqhnvlfdrlTVEEHlwfysrlksmaqeeirketdkmiedlelSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:cd03221 56 ----------IVTWG----------------------------STVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1131 TAGVDPYARRAIWDLILKYKpgRTILLSTHhmDEA--DLLGDRIAIISHGK 1179
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
991-1161 |
4.61e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 991 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYS 1070
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1071 RLKSMAQEeirketDKMIEDLE---LSNKRHSLVQTLSGGMKRKlsVAIA--FVGGSRAIILDEP-----TAGVDPYARR 1140
Cdd:PRK13538 100 RLHGPGDD------EALWEALAqvgLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPftaidKQGVARLEAL 171
|
170 180
....*....|....*....|.
gi 568912802 1141 aiwdLILKYKPGRTILLSTHH 1161
Cdd:PRK13538 172 ----LAQHAEQGGMVILTTHQ 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
987-1179 |
5.00e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE--MDEIRKNLGMCPQHNVLFDRLTVEE 1064
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLW----FYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1140
Cdd:PRK10762 99 NIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568912802 1141 AIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:PRK10762 179 SLFRVIRELKSqGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
991-1186 |
5.07e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.80 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 991 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMCPQHNVLFDRLTVEEHL 1066
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1067 WFYSRLKSMAQEEIRKETDKM-IEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1145
Cdd:PRK11831 106 AYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568912802 1146 I--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK11831 186 IseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
973-1199 |
8.20e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.98 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1051
Cdd:PRK11176 344 FRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRlTVEEHLwFYSRLKSMAQEEIRKETdKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSR 1123
Cdd:PRK11176 424 QNVHLFND-TIANNI-AYARTEQYSREQIEEAA-RMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1124 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP---LFLKGAYGDGYRL 1199
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGTHaelLAQNGVYAQLHKM 578
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
999-1160 |
9.08e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 9.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 999 QVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE-----IR-KNLGMCPQHNVLFDRLTVEEHLWFYSRL 1072
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-HQMDEearakLRaKHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1073 KSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYK 1150
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNRE 195
|
170
....*....|
gi 568912802 1151 PGRTILLSTH 1160
Cdd:PRK10584 196 HGTTLILVTH 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2026-2246 |
9.20e-14 |
|
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: 76.40 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2026 DADNDMVKIENLTKVY-KSRKIGRilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTGGEAFVNGHSV-LK 2102
Cdd:TIGR02633 252 EIGDVILEARNLTCWDvINPHRKR---VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2103 DLLQ-VQQSLGYCPQ---FDALFDELTAREH-----LQLYTRLRGIPWKDEAQVVKWALEKLEL-TKYADKPAGTYSGGN 2172
Cdd:TIGR02633 329 NPAQaIRAGIAMVPEdrkRHGIVPILGVGKNitlsvLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2173 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2246
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2062-2243 |
9.39e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2062 GECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLlqvQQSL-GYCPQ-------FDALFDELTAREHLQLY 2133
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAYVPQseevdwsFPVLVEDVVMMGRYGHM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 TRLRgIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2213
Cdd:PRK15056 110 GWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL 188
|
170 180 190
....*....|....*....|....*....|
gi 568912802 2214 IKTGRSVVLTSHSMEECEALCTrLAIMVNG 2243
Cdd:PRK15056 189 RDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
687-893 |
1.11e-13 |
|
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: 75.12 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 687 MMPLCMVISWVYSVAMTIQHIVAEKEHRLKEVMKTMGLNNAVHWVAWFITGFVqLSISVTALTAILKYGQVLMHSHVLII 766
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFL-VGLLQLLIILLLLFGIGIPFGNLGLL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 767 WLFLAVYAVATIMFCFLVSVLYSKAKLASACGGIIYFLSYVPYMYVAIREEVAHdkitaFEKCIASLMSTTAFGLGSKYF 846
Cdd:pfam12698 242 LLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPS-----FLQWIFSIIPFFSPIDGLLRL 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568912802 847 ALYEVAgvgiqwhtfsqspvegddFNLLLAVTMLMVDTVVYGVLTWY 893
Cdd:pfam12698 317 IYGDSL------------------WEIAPSLIILLLFAVVLLLLALL 345
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2047-2245 |
1.30e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2047 GRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-----DESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDAL 2120
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2121 FDELTAREHLQLYTRL-RGIPWKDEAQV-VKWALEKLEL----TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEP 2194
Cdd:PRK14247 94 IPNLSIFENVALGLKLnRLVKSKKELQErVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2195 TTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
986-1173 |
1.77e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 986 MALNKLSLNLYENQVVSFLGHNGAGKTTTMSI---LTGLFPP--TSGSATIYGHDIR-TEMD--EIRKNLGMCPQHNVLF 1057
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYaPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DRlTVEEHLWFYSRLKSMaqeeiRKETDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1129
Cdd:PRK14243 104 PK-SIYDNIAYGARINGY-----KGDMDELVERSlrqaalwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568912802 1130 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIA 1173
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2064-2245 |
2.42e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.18 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2064 CFGLLGVNGAGKTS---TFKMLT--GDESTTGGEAFVNGHSVLK---DLLQVQQSLGYCPQFDALFDELTAREHLQLYTR 2135
Cdd:PRK14267 32 VFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2136 LRGI--PWKDEAQVVKWALEKLEL-----TKYADKPaGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2208
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 568912802 2209 LILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK14267 191 LLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2029-2245 |
2.66e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.83 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQVQ 2108
Cdd:PRK11614 3 KVMLSFDKVSAHY-----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDITDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 ------QSLGYCPQFDALFDELTAREHLQLytrlrGIPWKDEAQV---VKWALEKL-ELTKYADKPAGTYSGGNKRKLST 2178
Cdd:PRK11614 74 takimrEAVAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFqerIKWVYELFpRLHERRIQRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2179 AIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
971-1162 |
3.15e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYKNDKkMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMdeiRKNL-GM 1049
Cdd:PRK15056 7 IVVNDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1050 CPQ-HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIED-----LELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSR 1123
Cdd:PRK15056 83 VPQsEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTaalarVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568912802 1124 AIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHM 1162
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNL 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2067-2254 |
3.42e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2067 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQF--DALFDElTAREHLQLYTRLRGIPWKD 2143
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRKFVGLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2144 EAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVL 2222
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIF 193
|
170 180 190
....*....|....*....|....*....|..
gi 568912802 2223 TSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2254
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
973-1180 |
4.42e-13 |
|
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: 71.76 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVY-------KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMD 1041
Cdd:TIGR02769 5 VRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1042 EIRKNLGMCPQ--HNVLFDRLTVE----EHLWFYSRLKSMAQEEirkETDKMIEDLEL-SNKRHSLVQTLSGGMKRKLSV 1114
Cdd:TIGR02769 85 AFRRDVQLVFQdsPSAVNPRMTVRqiigEPLRHLTSLDESEQKA---RIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1115 AIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2028-2245 |
5.06e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.58 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2028 DNDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFK----MLTGDESTTGGEAFVNGHSV--- 2100
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGDKKnnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2101 ----------LKDLLQVQQSLGYCPQFD--ALFDElTAREHLQLYTRLRGIPWKDEAQVVKWALEKLEL-TKYADKPAGT 2167
Cdd:PRK13631 98 elitnpyskkIKNFKELRRRVSMVFQFPeyQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2168 YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
987-1180 |
5.58e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCPQHNVLFDRLTVEE 1064
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLW---FYSRL----KSMAQEEIRKETDKMIEDLELSNKrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDpy 1137
Cdd:PRK11288 99 NLYlgqLPHKGgivnRRLLNYEAREQLEHLGVDIDPDTP----LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568912802 1138 AR------RAIWDLilkYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK11288 173 AReieqlfRVIREL---RAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
976-1189 |
5.60e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYKNDKKMALNK-LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatIYGHDIRteMDEI---RKNLGMCP 1051
Cdd:PRK11000 6 LRNVTKAYGDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD--LFIGEKR--MNDVppaERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1132 AGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1189
Cdd:PRK11000 162 SNLDAALRVQMRIEIsrLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2062-2256 |
6.31e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2062 GECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKDLLQVQQSLGYCPQFDALFDELTAREHL-QLY 2133
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNLiEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 TRLRGIpwkDEAQVVKWA---LEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2210
Cdd:PRK11124 108 CRVLGL---SKDQALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568912802 2211 LDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2256
Cdd:PRK11124 185 RELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2051-2226 |
6.85e-13 |
|
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: 73.93 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREH 2129
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2130 LQLytrlrGIPWKDEAQVVkWALEKLELTKY-ADKPAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2198
Cdd:TIGR02868 429 LRL-----ARPDATDEELW-AALERVGLADWlRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*...
gi 568912802 2199 DPKARRFLWNLILDlIKTGRSVVLTSHS 2226
Cdd:TIGR02868 503 DAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2031-2245 |
9.37e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYksrkIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLLQ 2106
Cdd:PRK10908 1 MIRFEHVSKAY----LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2186
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2187 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2031-2244 |
9.47e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--------K 2102
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2103 DLLQVQQ--SLGYCPqfdalfdELTAREHLQL-YTR--LRGIPW---KDEAQVVKWALEKLE--LTKYADKPAGTYSGGN 2172
Cdd:COG1101 81 YIGRVFQdpMMGTAP-------SMTIEENLALaYRRgkRRGLRRgltKKRRELFRELLATLGlgLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2173 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRsvvLTS----HSMEECEALCTRLAIMVNGR 2244
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEGR 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
983-1173 |
1.00e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 983 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTS-----GSATIYGHDI---RTEMDEIRKNLGMC-PQH 1053
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLNRLRRQVSMVhPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 NvLFDrLTVEEHLWFYSRLKSMAQE-EIRKETDKMIEDLEL----SNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:PRK14258 98 N-LFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568912802 1129 EPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIA 1173
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
979-1180 |
1.26e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 979 VYKNDKKMALNkLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQH--- 1053
Cdd:PRK09700 271 VTSRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrd 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 NVLFDRLTVEEHLWFYSRLKS---------MAQEEIRKETDKMIEDLELsnKRHSLVQT---LSGGMKRKLSVAIAFVGG 1121
Cdd:PRK09700 350 NGFFPNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELLAL--KCHSVNQNiteLSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1122 SRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
2055-2228 |
1.27e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2055 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKDLLQVQQSLGYC---PQFDALFDELTARE 2128
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2129 HLQLytRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2208
Cdd:PRK13638 100 AFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180
....*....|....*....|
gi 568912802 2209 LILDLIKTGRSVVLTSHSME 2228
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDID 197
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
991-1186 |
1.45e-12 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 69.70 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 991 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP----TSGSATIYGHDIrTEMDEIRKNLGMCPQH-----NVLFdrlT 1061
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL-LPLSIRGRHIATIMQNprtafNPLF---T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1062 VEEHLwfysRLKSMAQEEIRKE-TDKMIEDLELSNKRHS--LVQT----LSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1134
Cdd:TIGR02770 81 MGNHA----IETLRSLGKLSKQaRALILEALEAVGLPDPeeVLKKypfqLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1135 DPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:TIGR02770 157 DVVNQARVLKLLreLRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2032-2253 |
1.45e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL-----KDLLQ 2106
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQF--DALFDElTAREHLQLYTRLRGIPwKDEA--QVVKWaLEKLEL-TKYADKPAGTYSGGNKRKLSTAIA 2181
Cdd:PRK13641 83 LRKKVSLVFQFpeAQLFEN-TVLKDVEFGPKNFGFS-EDEAkeKALKW-LKKVGLsEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2182 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLrclgsIQH 2253
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL-----IKH 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2061-2245 |
1.61e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2061 PGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKDLLQVQQSLGYCPQFDALFDELTAREHL-QL 2132
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVFQQYNLWPHLTVMENLiEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2133 YTRLRGIPwKDEAQV-VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2211
Cdd:COG4161 107 PCKVLGLS-KEQAREkAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIR 185
|
170 180 190
....*....|....*....|....*....|....
gi 568912802 2212 DLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:COG4161 186 ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
962-1180 |
1.70e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 962 EEPTHL----PLVVcvDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsATIYGhdiR 1037
Cdd:PRK11247 2 MNTARLnqgtPLLL--NAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---T 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1038 TEMDEIRKNLGMCPQHNVLFDRLTVEEHL-------WfysrlksmaqeeiRKETDKMIEDLELSNKRHSLVQTLSGGMKR 1110
Cdd:PRK11247 74 APLAEAREDTRLMFQDARLLPWKKVIDNVglglkgqW-------------RDAALQALAAVGLADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1111 KLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
988-1186 |
1.90e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGMCPQHNVL---FD-RLTV 1062
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDTSLsfeFDvRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1063 E----EHLwfySRLKSMAQEEiRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDpyA 1138
Cdd:PRK09536 99 EmgrtPHR---SRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1139 RRAIWDLILKYK---PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK09536 173 NHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
973-1180 |
2.02e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.39 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE---------MDEI 1043
Cdd:PRK11264 6 VKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1044 RKNLGMCPQHNVLFDRLTVEEHLWFYSRL-KSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1122
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1123 RAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
982-1181 |
2.03e-12 |
|
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: 72.16 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 982 NDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT-SGSATIYGH--DIRTEMDEIRKNLGMCPQ------ 1052
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrhg 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 --------HNVlfdRLTVEEHLWFYSRLKSMAQEEIrkeTDKMIEDLELSNKRHSL-VQTLSGGMKRKLSVAIAFVGGSR 1123
Cdd:TIGR02633 350 ivpilgvgKNI---TLSVLKSFCFKMRIDAAAELQI---IGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1124 AIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1181
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2031-2250 |
2.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.02 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQ 2108
Cdd:PRK13644 1 MIRLENVSYSYPDGTP----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:PRK13644 77 KLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2188 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGS 2250
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2052-2245 |
2.43e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2052 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllQVQQSLGYCPQF-------DALFDEL 2124
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR--SPQDGLANGIVYisedrkrDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2125 TAREHLQLyTRLR-------GIPWKDEAQVVKWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2196
Cdd:PRK10762 346 SVKENMSL-TALRyfsraggSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568912802 2197 GMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
987-1179 |
2.54e-12 |
|
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: 71.78 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIY--GHDIRTE--MDEIRKNLGMCPQHNVLFDRLTV 1062
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLKASniRDTERAGIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1063 EEHLWFYSRL----KSMAQEEIRKETDKMIEDLELSNKRHSL-VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1137
Cdd:TIGR02633 96 AENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568912802 1138 ARRAIWDLI--LKYKPGRTILLStHHMDEADLLGDRIAIISHGK 1179
Cdd:TIGR02633 176 ETEILLDIIrdLKAHGVACVYIS-HKLNEVKAVCDTICVIRDGQ 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
968-1169 |
2.75e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 968 PLVVCvDKLTKVYKNDKKMA--LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMD 1041
Cdd:PRK11629 4 ILLQC-DNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1042 EIRKN-LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVG 1120
Cdd:PRK11629 83 ELRNQkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1121 GSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLG 1169
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2050-2242 |
3.98e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.01 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2050 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLLQ---------VQQSLGYCPQ 2116
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLRKhigivfqnpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2117 FDALFDeltAREHLqlytrlrgIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2196
Cdd:PRK13648 103 YDVAFG---LENHA--------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568912802 2197 GMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVN 2242
Cdd:PRK13648 172 MLDPDARQNLLDLVRKV-KSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
973-1181 |
4.83e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATiyghdirtemdeIRKNL--GMC 1050
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS------------IPKGLriGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDRLTVEEHLW--FYSRLKSMAQ-EEIRKETDKMIEDL----ELSNK--------------------------R 1097
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgDAELRALEAElEELEAKLAEPDEDLerlaELQEEfealggweaearaeeilsglgfpeedL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1098 HSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRaiW--DLILKYkPGrTILLSTH--H-MDEadlLGDRI 1172
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNY-PG-TVLVVSHdrYfLDR---VATRI 219
|
....*....
gi 568912802 1173 AIISHGKLK 1181
Cdd:COG0488 220 LELDRGKLT 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2019-2245 |
5.38e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2019 RQRVLRGDADNDMVKIENLTkvykSRKIGRilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH 2098
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT----SRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2099 --SVLKDLLQVQQSLGYCPQF---DALFDELTAREHLQLYTRLRGIPWK---------DEAQVVKWALEKLELTKYA-DK 2163
Cdd:PRK09700 326 diSPRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKDGGYKgamglfhevDEQRTAENQRELLALKCHSvNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2164 PAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2243
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
..
gi 568912802 2244 RL 2245
Cdd:PRK09700 486 RL 487
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
987-1178 |
7.92e-12 |
|
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: 67.46 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSaTIYGHDIRT---------EMDEIRKN-LGMCPQH-NV 1055
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS-ILVRHDGGWvdlaqasprEILALRRRtIGYVSQFlRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1056 LfDRLT----VEEHLwfysRLKSMAQEEIRKETDKMIEDLELSNKRHSLV-QTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:COG4778 105 I-PRVSaldvVAEPL----LERGVDREEARARARELLARLNLPERLWDLPpATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568912802 1131 TAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHG 1178
Cdd:COG4778 180 TASLDAANRAVVVELIEEAKArGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2029-2292 |
9.60e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.20 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLtkVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL-KDLLQV 2107
Cdd:PRK13642 2 NKILEVENL--VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2186
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2187 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMIT 2265
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSEDMVEIG 238
|
250 260
....*....|....*....|....*..
gi 568912802 2266 VRTKSSQNVKDVVRFFNRNFPEAMLKE 2292
Cdd:PRK13642 239 LDVPFSSNLMKDLRKNGFDLPEKYLSE 265
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2065-2264 |
1.04e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2065 FGLLGVNGAGKTSTFKMLT------GDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDELTAREHLQLYTRLR 2137
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2138 GIPWKDE-AQVVKWALEKLELTKYA----DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2212
Cdd:PRK14246 119 GIKEKREiKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2213 LiKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRFGDGYMI 2264
Cdd:PRK14246 199 L-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2032-2252 |
1.12e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdLLQVQQSL 2111
Cdd:PRK10851 3 IEIANIKKSF-----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-LHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLytRLRGIPWKDEA------QVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAF--GLTVLPRRERPnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2186 PAFIFLDEPTTGMDPKA----RRFLWNLILDLIKTGrsvVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2252
Cdd:PRK10851 155 PQILLLDEPFGALDAQVrkelRRWLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
956-1184 |
1.29e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 69.78 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 956 ETRGMEEEPTHLP-----LVVcvDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAT 1030
Cdd:COG4618 313 AAVPAEPERMPLPrpkgrLSV--ENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1031 IYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHLwfySRLKSMAQEEI-----RKETDKMIedLELSNKRHSLV--- 1101
Cdd:COG4618 391 LDGADLSQwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDADPEKVvaaakLAGVHEMI--LRLPDGYDTRIgeg 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1102 -QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMdeaDLLG--DRIAIIS 1176
Cdd:COG4618 465 gARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIraLKAR-GATVVVITHRP---SLLAavDKLLVLR 540
|
....*...
gi 568912802 1177 HGKLKCCG 1184
Cdd:COG4618 541 DGRVQAFG 548
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
987-1179 |
1.44e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQHNVLFDRLTVEE 1064
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLWF--YSrLKSM--AQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1140
Cdd:PRK10982 93 NMWLgrYP-TKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568912802 1141 AIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:PRK10982 172 HLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2025-2228 |
1.60e-11 |
|
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: 69.62 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2025 GDADNDMVKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDL 2104
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYP----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2105 LQ--VQQSLGYCPQFDALFdELTAREHLQLYTrlrgiPWKDEAQVVKwALEKLELTKY-ADKPAGTY----------SGG 2171
Cdd:TIGR02857 390 DAdsWRDQIAWVPQHPFLF-AGTIAENIRLAR-----PDASDAEIRE-ALERAGLDEFvAALPQGLDtpigeggaglSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2172 NKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSME 2228
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2034-2250 |
1.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2034 IENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV------LKDLLQV 2107
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQFD--ALFDELTARE------HLQlytrlrgipwKDEAQVVKWALEKLELTK----YADKPAGTYSGGNKRK 2175
Cdd:PRK13645 89 RKEIGLVFQFPeyQLFQETIEKDiafgpvNLG----------ENKQEAYKKVPELLKLVQlpedYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2176 LSTA--IALIGYPafIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:PRK13645 159 VALAgiIAMDGNT--LVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
960-1180 |
2.06e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 960 MEEEPTHLPLVVCVDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE 1039
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1040 MDEIRKNLG--MCPQHNVLFDRLTVEEHLWF--------YSRLKSMAQE-EIRKETDKMIEDLELSNKRhsLVQTLSGGM 1108
Cdd:PRK15439 79 TPAKAHQLGiyLVPQEPLLFPNLSVKENILFglpkrqasMQKMKQLLAAlGCQLDLDSSAGSLEVADRQ--IVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 1109 KRklsvaiafvggSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK15439 157 RD-----------SRILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
968-1179 |
2.19e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 968 PLVVcVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE- 1042
Cdd:PRK11701 5 PLLS-VRGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLrdlyALSEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1043 -----IRKNLGMCPQHNVLFDRLTVE------EHLwfysrlksMAQ-----EEIRKETDKMIEDLELSNKR-HSLVQTLS 1105
Cdd:PRK11701 82 errrlLRTEWGFVHQHPRDGLRMQVSaggnigERL--------MAVgarhyGDIRATAGDWLERVEIDAARiDDLPTTFS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1106 GGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1179
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
988-1180 |
2.27e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.37 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMDE--IRKNLGMCPQHNVLFDRlTVEEH 1065
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHhyLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1066 LWFysRLKSMAQEEIRKETDKMIED---LELSNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1138
Cdd:TIGR00958 575 IAY--GLTDTPDEEIMAAAKAANAHdfiMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568912802 1139 RRAIWDliLKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1180
Cdd:TIGR00958 653 EQLLQE--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSV 691
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
974-1180 |
2.29e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 974 DKLTKVYKNdKKMalnKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDiRTEMDEIRKNLGMCPQH 1053
Cdd:PRK10771 5 TDITWLYHH-LPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 NVLFDRLTVEEH--LWFYSRLKSMAQEeiRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:PRK10771 80 NNLFSHLTVAQNigLGLNPGLKLNAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1132 AGVDPYARRAIWDLILKYKPGR--TILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2033-2244 |
2.32e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEA-FVNGHSVLKDLLQVQQS- 2110
Cdd:PRK11701 8 SVRGLTKLY-----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 --------LGYCPQF--DALFDELTA----REHL-----QLYTRLRgipwkdeAQVVKWaLEKLEL--TKYADKPAgTYS 2169
Cdd:PRK11701 83 rrrllrteWGFVHQHprDGLRMQVSAggniGERLmavgaRHYGDIR-------ATAGDW-LERVEIdaARIDDLPT-TFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2170 GGNKRKLSTAIALIGYPAFIFLDEPTTGMD--PKARrflwnlILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVN 2242
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR------LLDLLRGlvrelGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
..
gi 568912802 2243 GR 2244
Cdd:PRK11701 228 GR 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
988-1186 |
2.41e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDE--------------IRKNLGMCPQH 1053
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrlLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 NVLFDRLTVEEHLWFYS-RLKSMAQEEIRKETDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:PRK10619 101 FNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1132 AGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
980-1178 |
2.50e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-RKNLGMCPQHNVLFD 1058
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 RlTVEEHLWFYSRLKSMAQEEirketDKMIEDL-------ELSNKRhslVQTLSGGMKRKLSVA--IAFVggSRAIILDE 1129
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQPDP-----AIFLDDLerfalpdTILTKN---IAELSGGEKQRISLIrnLQFM--PKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1130 PTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1178
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
980-1168 |
3.23e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.37 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL-----TGLFppTSGSATIYGHDIRTEMDEIrknLGMCPQHN 1054
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRS---IGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1055 VLFDRLTVEEHLWFYSRL---KSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGM----KRKLSVAIAFVGGSRAII- 1126
Cdd:TIGR00956 846 LHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568912802 1127 LDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHH-----MDEADLL 1168
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQpsailFEEFDRL 973
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
973-1217 |
3.88e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.59 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKkMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1051
Cdd:PRK10790 343 IDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNV-----LFDRLTV-----EEHLWFYSRLKSMAqEEIRKETDKMIEDL-ELSNkrhslvqTLSGGMKRKLSVAIAFVG 1120
Cdd:PRK10790 422 QDPVvladtFLANVTLgrdisEEQVWQALETVQLA-ELARSLPDGLYTPLgEQGN-------NLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1121 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP---LFLKGAYG 1194
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHqqlLAAQGRYW 569
|
250 260
....*....|....*....|...
gi 568912802 1195 DGYRLTLVKQPAEPGTSQEPGLA 1217
Cdd:PRK10790 570 QMYQLQLAGEELAASVREEESLS 592
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2031-2245 |
3.93e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKIgrILAVDrlcLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--------LK 2102
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV--LHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2103 DLL-QVQQSLGYCPQFDALFDELTAREH-LQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAI 2180
Cdd:PRK11264 78 GLIrQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2181 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
988-1180 |
3.97e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.60 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEI----RKNLGMCPQHNVLFDRLTV 1062
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaqlrREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1063 EEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1142
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568912802 1143 WDlILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1180
Cdd:PRK10535 184 MA-ILHQlrDRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2034-2245 |
3.98e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.85 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2034 IENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEafvnghsvlkdLLQVQQSLGy 2113
Cdd:PRK11247 15 LNAVSKRYGERTV-----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-----------LLAGTAPLA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2114 cpqfdalfdelTAREHlqlyTRL-----RGIPWKDEAQVV------KW---ALEKLELTKYADK----PAgTYSGGNKRK 2175
Cdd:PRK11247 78 -----------EARED----TRLmfqdaRLLPWKKVIDNVglglkgQWrdaALQALAAVGLADRanewPA-ALSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2176 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2061-2225 |
4.14e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2061 PGECFGLLGVNGAGKTSTFKMLTGDESTTG--GEAFVNGHSVLKdllQVQQSLGYCPQFDALFDELTAREHLQLYTRLR- 2137
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVFCSLLRl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2138 --GIPWKDEAQVVKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2210
Cdd:PLN03211 170 pkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*
gi 568912802 2211 LDLIKTGRSVVLTSH 2225
Cdd:PLN03211 250 GSLAQKGKTIVTSMH 264
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
999-1161 |
4.18e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 999 QVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDiRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRL---KSM 1075
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1076 AQEEIRKETDKMIEDLELSNKRH-----SLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY-ARRAIWDLILKY 1149
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATaAYRLVLTLGSLA 253
|
170
....*....|..
gi 568912802 1150 KPGRTILLSTHH 1161
Cdd:PLN03211 254 QKGKTIVTSMHQ 265
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2054-2245 |
4.68e-11 |
|
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: 64.82 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2054 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkdllqvqQSLGYCP----------QFDALFDE 2123
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-----------VDVTAAPpadrpvsmlfQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2124 LTAREH--LQLYTRLRGIPwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2201
Cdd:cd03298 85 LTVEQNvgLGLSPGLKLTA--EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 2202 ARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:cd03298 163 LRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
991-1180 |
4.77e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 991 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC------PQHNVLFDR----- 1059
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 ---LTVEEHLWFYSRlksmAQEEIRKETDKMIEDLELSNKRHSlVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1136
Cdd:PRK15439 362 vcaLTHNRRGFWIKP----ARENAVLERYRRALNIKFNHAEQA-ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 1137 YARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK15439 437 SARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2029-2257 |
4.86e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ-V 2107
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGT----KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQF--DALFdELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:PRK13647 78 RSKVGLVFQDpdDQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNR 2257
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2051-2243 |
4.86e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLLQVQQS-LGYCPQFDALFDELTARE 2128
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtFNGPKSSQEAgIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2129 HLQL----YTRLRGIPWK---DEAQVVkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2201
Cdd:PRK10762 99 NIFLgrefVNRFGRIDWKkmyAEADKL---LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568912802 2202 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2243
Cdd:PRK10762 176 ETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
984-1180 |
5.31e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.06 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 984 KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTV 1062
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1063 EEHLwfysRL-KSMAQEEIRKETDKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1133
Cdd:PRK13657 426 EDNI----RVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgergrqLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1134 VDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKL 1180
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNGRV 547
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2029-2245 |
6.04e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.81 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVnGHSVLKD--LLQ 2106
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT---YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEetVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:PRK13635 79 VRRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2245
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEI 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2051-2254 |
6.26e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLLQVQ--QSLGYCPQFDALFDElTARE 2128
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-IADYSEAAlrQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2129 HLQLytrlrGIPWKDEAQVVKwALEKLELTKYADKPAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2198
Cdd:PRK11160 433 NLLL-----AAPNASDEALIE-VLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2199 DPKARRFLWNLILDLIKtGRSVVLTSH---SMEECEALCtrlaIMVNGRLRCLGSIQHL 2254
Cdd:PRK11160 507 DAETERQILELLAEHAQ-NKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQEL 560
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
973-1186 |
6.40e-11 |
|
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: 64.36 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1051
Cdd:cd03369 9 VENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRlTVEEHLWFYSRlksMAQEEIRketdkmiEDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:cd03369 89 QDPTLFSG-TIRSNLDPFDE---YSDEEIY-------GALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 1132 AGVDPYARRAIWDLILKYKPGRTILLSTHHMDE-ADLlgDRIAIISHGKLKCCGSP 1186
Cdd:cd03369 154 ASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVKEYDHP 207
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2029-2251 |
7.41e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.22 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTK---VYKSRKiGRI-------------LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2092
Cdd:PRK13546 2 NVSVNIKNVTKeyrIYRTNK-ERMkdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2093 AFVNGhsvlkDLLQVQQSLGycpqfdaLFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGN 2172
Cdd:PRK13546 81 VDRNG-----EVSVIAISAG-------LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2173 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2251
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1999-2249 |
7.76e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1999 PQRLPVSTKPVEDDVDVASERQRVLRGDAdndMVKIENLTKVYKSR-----KIGR-ILAVDRLCLGVRPGECFGLLGVNG 2072
Cdd:PRK10261 284 PRRFPLISLEHPAKQEPPIEQDTVVDGEP---ILQVRNLVTRFPLRsgllnRVTReVHAVEKVSFDLWPGETLSLVGESG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2073 AGKTSTFKMLTGDESTTGGEAFVNGHSVlkDLLQVQ--QSLGYCPQFdaLFDELTAR------------EHLQLYTRLRG 2138
Cdd:PRK10261 361 SGKSTTGRALLRLVESQGGEIIFNGQRI--DTLSPGklQALRRDIQF--IFQDPYASldprqtvgdsimEPLRVHGLLPG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2139 ipwKDEAQVVKWALEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT- 2216
Cdd:PRK10261 437 ---KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDf 513
|
250 260 270
....*....|....*....|....*....|...
gi 568912802 2217 GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2249
Cdd:PRK10261 514 GIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2033-2246 |
7.77e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLT---KVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGdeSTTG---GEAFVNGHSV-LKDLL 2105
Cdd:PRK13549 261 EVRNLTawdPVNPHIKR-----VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGrweGEIFIDGKPVkIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 Q-VQQSLGYCPQ---FDALFDELTAREH-----LQLYTRLRGIPWKDEAQVVKWALEKLEL-TKYADKPAGTYSGGNKRK 2175
Cdd:PRK13549 334 QaIAQGIAMVPEdrkRDGIVPVMGVGKNitlaaLDRFTGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQK 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2176 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2246
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2067-2225 |
8.30e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2067 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLqlytrLRGIPWKDEAQ 2146
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC-----LYDIHFSPGAV 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2147 VVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2225
Cdd:PRK13540 107 GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
988-1161 |
1.16e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLW 1067
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1068 FYSRLKSMAQeeirkETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLIL 1147
Cdd:PRK13540 97 YDIHFSPGAV-----GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*
gi 568912802 1148 KY-KPGRTILLSTHH 1161
Cdd:PRK13540 172 EHrAKGGAVLLTSHQ 186
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2032-2244 |
1.26e-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: 63.26 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkdllqvqqSL 2111
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQ--------------FDALFDEltarehlQLYtrlrgipwkdeAQVVK-WALEK-LELTkyadkPAG--------- 2166
Cdd:cd03250 69 AYVSQepwiqngtirenilFGKPFDE-------ERY-----------EKVIKaCALEPdLEIL-----PDGdlteigekg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2167 -TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLW-NLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGR 2244
Cdd:cd03250 126 iNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
987-1179 |
1.27e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIY-------GHDIR-TEmdeiRKNLGMCPQHNVLFD 1058
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfegeelqASNIRdTE----RAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 RLTVEEHLWF---YSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:PRK13549 96 ELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568912802 1136 PYARRAIWDLI--LKYKPGRTILLStHHMDEADLLGDRIAIISHGK 1179
Cdd:PRK13549 176 ESETAVLLDIIrdLKAHGIACIYIS-HKLNEVKAISDTICVIRDGR 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2036-2245 |
1.91e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2036 NLTKVYKSRKIGRILAVDrLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV------LKDLLQVQQ 2109
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHN-VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 sLGYCPQFDALFDELTAREHLQLYTRLRGipwKDEAQVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIGYP 2186
Cdd:PRK11629 89 -LGFIYQFHHLLPDFTALENVAMPLLIGK---KKPAEINSRALEMLAavgLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2187 AFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAiMVNGRL 2245
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2059-2199 |
2.13e-10 |
|
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: 62.67 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTG---GEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLYTR 2135
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2136 LRGipwkdeAQVVKwalekleltkyadkpagTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD 2199
Cdd:cd03233 110 CKG------NEFVR-----------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
992-1180 |
2.49e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 992 SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLGMCPQhnvlfDR--------LT 1061
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPE-----DRkaegiipvHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1062 VEE---------HLWFYSRLKSmAQEeiRKETDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:PRK11288 348 VADninisarrhHLRAGCLINN-RWE--AENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 1132 AGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
988-1189 |
2.57e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRLTVEE-- 1064
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRElv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 ----HLWfYSRLKSMAQEEiRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1140
Cdd:PRK10575 107 aigrYPW-HGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1141 AIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1189
Cdd:PRK10575 185 DVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2059-2273 |
2.63e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLG-Y-CPQFDALFDELTAREHLqlytrL 2136
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYlVPQEPLLFPNLSVKENI-----L 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2137 RGIPWKDEA-QVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK 2215
Cdd:PRK15439 109 FGLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2216 TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIqhlkNRFGDGYMITVRTKSSQN 2273
Cdd:PRK15439 189 QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT----ADLSTDDIIQAITPAARE 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
976-1135 |
3.03e-10 |
|
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: 61.89 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 976 LTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT---SGSATIYGHDIRTEMDEIRKNLGMCPQ 1052
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEEHLWFYSRLKSmaqeeirketdkmiedlelsnkrHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
...
gi 568912802 1133 GVD 1135
Cdd:cd03233 148 GLD 150
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
974-1186 |
3.33e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 974 DKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQ 1052
Cdd:PRK10253 11 EQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 HNVLFDRLTVEE--------HLWFYSRLKSMAQEEIRKETDKM-IEDLELSNkrhslVQTLSGGMKRKLSVAIAFVGGSR 1123
Cdd:PRK10253 89 NATTPGDITVQElvargrypHQPLFTRWRKEDEEAVTKAMQATgITHLADQS-----VDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1124 AIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2031-2245 |
4.82e-10 |
|
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: 62.07 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkDLLQ---- 2106
Cdd:COG4181 8 IIELRGLTKTVGTGA-GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ----DLFAlded 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 ------------VQQSlgycpqFDaLFDELTAREHLQLYTRLRGIPwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKR 2174
Cdd:COG4181 83 ararlrarhvgfVFQS------FQ-LLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2175 KLSTAIALIGYPAFIFLDEPTTGMDPKARRflwnLILDLI-----KTGRSVVLTSHSmEECEALCTRLAIMVNGRL 2245
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGE----QIIDLLfelnrERGTTLVLVTHD-PALAARCDRVLRLRAGRL 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2036-2244 |
5.32e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2036 NLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSV----LKDLLQ--- 2106
Cdd:PRK13549 10 NITK-----TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGEELqasnIRDTERagi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 --VQQSLgycpqfdALFDELTAREHLQL---YTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2181
Cdd:PRK13549 85 aiIHQEL-------ALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2182 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
988-1186 |
5.56e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFpPTSGSATIYGHDIRT----EMDEIRKNLgmCPQHNVLFDRltve 1063
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYL--SQQQTPPFAM---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1064 eHLWFY---SRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI-------ILDEPTAG 1133
Cdd:PRK03695 85 -PVFQYltlHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 1134 VDpYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1186
Cdd:PRK03695 164 LD-VAQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2050-2259 |
5.86e-10 |
|
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: 62.12 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2050 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLLQVQQSLGYCPQFDALFDElTARE 2128
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2129 HLQLYTrlRGIPWKDEAQVVKWA-----LEKLEL---TKYADKPAGtYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2200
Cdd:cd03252 95 NIALAD--PGMSMERVIEAAKLAgahdfISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2201 KARRFLWNLILDlIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2259
Cdd:cd03252 172 ESEHAIMRNMHD-ICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2059-2245 |
6.78e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG-----HSVLKDL-------LQVQQSLGYCPQFDALFDELTA 2126
Cdd:PRK10982 271 LHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnHNANEAInhgfalvTEERRSTGIYAYLDIGFNSLIS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2127 --REHLQLYTRLRGIPWKDEAQvvkWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKAR 2203
Cdd:PRK10982 351 niRNYKNKVGLLDNSRMKSDTQ---WVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAK 427
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568912802 2204 RFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK10982 428 FEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2032-2245 |
9.06e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.41 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG------------------DESTTGGEA 2093
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2094 FVNGHSV-------LKDLLQVQQSLGYCPQFD--ALFDElTAREHLQLYTRLRGIPwKDEAQvvKWALEKLELT----KY 2160
Cdd:PRK13651 83 VLEKLVIqktrfkkIKKIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVS-KEEAK--KRAAKYIELVgldeSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2161 ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIM 2240
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*
gi 568912802 2241 VNGRL 2245
Cdd:PRK13651 239 KDGKI 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2035-2250 |
9.69e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2035 ENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGY 2113
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVE-----IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2114 CPQF-----DALFDELTAR---EHLQLYTRLRgipwKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:PRK10253 86 LAQNattpgDITVQELVARgryPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2029-2231 |
1.26e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.74 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVL-KDL 2104
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKP---ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTaKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2105 LQVQQSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2183
Cdd:PRK13640 80 WDIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568912802 2184 GYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECE 2231
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN 208
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
981-1160 |
1.26e-09 |
|
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: 59.95 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 981 KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL-----TGLfppTSGSATIYGHDIRtemDEIRKNLGMCPQHNV 1055
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLD---KNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1056 LFDRLTVEEHLWFYSRLKSMAQEEirketdkmiedlelsnkrhslvqtlsggmKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:cd03232 90 HSPNLTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*.
gi 568912802 1136 PYARRAIWDLILKY-KPGRTILLSTH 1160
Cdd:cd03232 141 SQAAYNIVRFLKKLaDSGQAILCTIH 166
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2031-2262 |
1.30e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.25 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllqvQQS 2110
Cdd:PRK11248 1 MLQISHLYADYGGKP-----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP----GAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:PRK11248 72 RGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 2191 LDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLgsiQHLKNRFGDGY 2262
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWqETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRF 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2059-2237 |
1.49e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllQVQQSLGYCPQFDALFDELTAREHLQLYTRLRG 2138
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2139 ipwKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGR 2218
Cdd:PRK13543 112 ---RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGG 188
|
170
....*....|....*....
gi 568912802 2219 SVVLTSHSMEECEALCTRL 2237
Cdd:PRK13543 189 AALVTTHGAYAAPPVRTRM 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
985-1181 |
1.68e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 985 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyghdirtemdeIRKNLGMCPQHNVLFDRlTVEE 1064
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLWFYSRLKSmaqEEIRKETD--KMIEDLELSnKRHSLVQ------TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1136
Cdd:PLN03232 698 NILFGSDFES---ERYWRAIDvtALQHDLDLL-PGRDLTEigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568912802 1137 YARRAIWDLILKYK-PGRTILLSTHHMDEADLLgDRIAIISHGKLK 1181
Cdd:PLN03232 774 HVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
988-1160 |
1.83e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatiyghdIRTEmDEIRknLGMCPQhNVLFDR---LTVEE 1064
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRN-GKLR--IGYVPQ-KLYLDTtlpLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1065 HLwfysRLKSMAQEeirketDKMIEDLELSNKRHSL---VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1141
Cdd:PRK09544 89 FL----RLRPGTKK------EDILPALKRVQAGHLIdapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|.
gi 568912802 1142 IWDLI--LKYKPGRTILLSTH 1160
Cdd:PRK09544 159 LYDLIdqLRRELDCAVLMVSH 179
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
985-1180 |
1.97e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 985 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSG-----SATIYGHDIRTEMD--EIRKNLGMCPQHNVLF 1057
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1058 DRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQT----LSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1133
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568912802 1134 VDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
983-1180 |
2.05e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 983 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQHNVLFDRLT 1061
Cdd:PRK10522 334 DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRKLFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1062 VEEhlwfySRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1141
Cdd:PRK10522 414 GPE-----GKPANPALVEKWLERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568912802 1142 IWDLILKY--KPGRTILLSTHHmDEADLLGDRIAIISHGKL 1180
Cdd:PRK10522 488 FYQVLLPLlqEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2031-2245 |
2.12e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT--GD---ESTTGGEAFVNGHSVLK--- 2102
Cdd:PRK14239 5 ILQVSDLSVYYNKKK-----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNIYSprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2103 DLLQVQQSLGYCPQFDALFdELTAREHLQLYTRLRGIpwKDEaQVVKWALEKL--------ELTKYADKPAGTYSGGNKR 2174
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGI--KDK-QVLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2175 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
949-1180 |
2.19e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.55 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 949 MESRHFEETRGMEEEPTHLPLVVCVDKLTkVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGlFPPTSGS 1028
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1029 ATIYGHDIRT-EMDEIRKNL---GMCPQ--HNVLFDRLTV------EEHLWfysrlKSMAQEEIRKETDKMIEDLELSNK 1096
Cdd:PRK11174 406 LKINGIELRElDPESWRKHLswvGQNPQlpHGTLRDNVLLgnpdasDEQLQ-----QALENAWVSEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1097 RHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDeaDLLG-DRIAII 1175
Cdd:PRK11174 481 DQAA--GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQwDQIWVM 556
|
....*
gi 568912802 1176 SHGKL 1180
Cdd:PRK11174 557 QDGQI 561
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2029-2260 |
2.84e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYK--SRKIGRI-------------LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEA 2093
Cdd:PRK13545 2 NYKVKFEHVTKKYKmyNKPFDKLkdlffrskdgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2094 FVNGHSVLkdllqVQQSLGycpqfdaLFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNK 2173
Cdd:PRK13545 82 DIKGSAAL-----IAISSG-------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2174 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2253
Cdd:PRK13545 150 SRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKE 229
|
....*..
gi 568912802 2254 LKNRFGD 2260
Cdd:PRK13545 230 VVDHYDE 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2029-2225 |
3.70e-09 |
|
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: 61.87 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkdllqvq 2108
Cdd:TIGR03719 320 DKVIEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGETV-------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 qSLGYCPQFdalfdeltaREHLQlytrlrgiPWKDEAQVVKWALEKLELTKY---------------AD--KPAGTYSGG 2171
Cdd:TIGR03719 386 -KLAYVDQS---------RDALD--------PNKTVWEEISGGLDIIKLGKReipsrayvgrfnfkgSDqqKKVGQLSGG 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2172 NKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2225
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVISH 498
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2059-2225 |
6.59e-09 |
|
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: 59.30 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTGdesttggeafvnghsvlkdllQVQQSLG-YC--PQFDALFDELTAREhLQLY-T 2134
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAG---------------------KLKPNLGkFDdpPDWDEILDEFRGSE-LQNYfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2135 RLRG--------------IP------------WKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2188
Cdd:cd03236 81 KLLEgdvkvivkpqyvdlIPkavkgkvgellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 568912802 2189 IFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2225
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2032-2245 |
8.22e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.41 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG---HSVLKD--LLQ 2106
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQF--DALFDELTAREhLQLYTRLRGIPWKdeaQVVKWALEKL-ELTKYAD---KPAGTYSGGNKRKLSTAI 2180
Cdd:PRK13646 83 VRKRIGMVFQFpeSQLFEDTVERE-IIFGPKNFKMNLD---EVKNYAHRLLmDLGFSRDvmsQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2181 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
985-1180 |
9.48e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 985 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMC---------P 1051
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRDIQMVfqdsisavnP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVlfdRLTVEEHLWFYSRLKSMAQEEIRKETDKMIE-DLELSNKRHslvQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:PRK10419 105 RKTV---REIIREPLRHLLSLDKAERLARASEMLRAVDlDDSVLDKRP---PQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1131 TAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
969-1173 |
9.83e-09 |
|
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: 60.72 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 969 LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIR-TEMDEIRKNL 1047
Cdd:TIGR03719 321 KVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlAYVDQSRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1048 GmcPQHNVlfdrltveehlWfysrlksmaqEEIRKETDKM-IEDLELSNK------------RHSLVQTLSGGMKRKLSV 1114
Cdd:TIGR03719 398 D--PNKTV-----------W----------EEISGGLDIIkLGKREIPSRayvgrfnfkgsdQQKKVGQLSGGERNRVHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1115 AIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYkPGRTILLStHhmDEADLlgDRIA 1173
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF-AGCAVVIS-H--DRWFL--DRIA 507
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2057-2249 |
1.07e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 60.53 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2057 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKDLLQvqQSLGYCPQFDALFDElTAREHLqly 2133
Cdd:COG4618 353 FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwDREELG--RHIGYLPQDVELFDG-TIAENI--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 TRLRGIpwkDEAQVVKWAlekleltKYAD-------KPAGtY-----------SGGNKRKLSTAIALIGYPAFIFLDEPT 2195
Cdd:COG4618 427 ARFGDA---DPEKVVAAA-------KLAGvhemilrLPDG-YdtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2196 TGMDPKARRFLWNLILDLIKTGRSVVLTSHSMeecEAL--CTRLAIMVNGRLRCLG 2249
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1005-1159 |
1.08e-08 |
|
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: 60.60 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1005 GHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLF-DrlTVEEHLWfYSRLKSmAQEEIRK 1082
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFnD--TIAYNIA-YGRPDA-SEEEVEA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1083 -----ETDKMIEDLElsNKRHSLVQ----TLSGGMKRKlsVAIAfvggsRAI-------ILDEPTAGVDPYARRAIWDLI 1146
Cdd:COG5265 467 aaraaQIHDFIESLP--DGYDTRVGerglKLSGGEKQR--VAIA-----RTLlknppilIFDEATSALDSRTERAIQAAL 537
|
170
....*....|....*...
gi 568912802 1147 LKYKPGRTIL-----LST 1159
Cdd:COG5265 538 REVARGRTTLviahrLST 555
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1008-1181 |
1.13e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1008 GAGKTTTMSILTGLFP-PTSGSATIYGH--DIRTEMDEIRKNLGMCP--------------QHNVLfdrLTVEEHLWFYS 1070
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkrdgivpvmgvGKNIT---LAALDRFTGGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1071 RLKSMAQEE-IRKETDKM---IEDLELSnkrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI 1146
Cdd:PRK13549 375 RIDDAAELKtILESIQRLkvkTASPELA------IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI 448
|
170 180 190
....*....|....*....|....*....|....*.
gi 568912802 1147 LKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1181
Cdd:PRK13549 449 NQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1002-1160 |
1.36e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1002 SFLGHNGAGKTTTMSILTGlfPPTSGsaTIYGhDIRT-----EMDEIRKNLGMCPQHNVLFDRLTVEEHLWF--YSRL-K 1073
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRIsgfpkKQETFARISGYCEQNDIHSPQVTVRESLIYsaFLRLpK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1074 SMAQEEIRKETDKMIEDLELSNKRHSLV-----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA----RRAIWD 1144
Cdd:PLN03140 985 EVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAaaivMRTVRN 1064
|
170
....*....|....*.
gi 568912802 1145 LIlkyKPGRTILLSTH 1160
Cdd:PLN03140 1065 TV---DTGRTVVCTIH 1077
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2030-2227 |
1.40e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2030 DMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGeafvnghsVLKDllQVQQ 2109
Cdd:PRK09544 3 SLVSLENVSVSFGQRRV-----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKR--NGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 SLGYCPQfdALFDELTAREHLQLYTRLRgiPWKDEAQVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2189
Cdd:PRK09544 68 RIGYVPQ--KLYLDTTLPLTVNRFLRLR--PGTKKEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 568912802 2190 FLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSM 2227
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
987-1180 |
2.98e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH-----DIRTEMDEIRknlgMCPQ--HNVLFDR 1059
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIR----MIFQdpSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1060 LTVEEHLWFYSRLKS-MAQEEIRKETDKMIEDLELSNKRHSLV-QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1137
Cdd:PRK15112 104 QRISQILDFPLRLNTdLEPEQREKQIIETLRQVGLLPDHASYYpHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 1138 ARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK15112 184 MRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2051-2248 |
3.98e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKtSTFKM-LTGDESTTGGEAFVNGHSVLKDLLQVQQSLgycpqFDALFDEltareh 2129
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGK-STLAMlLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-----FSAVFTD------ 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2130 LQLYTRL---RGIPwKDEAQVVKWaLEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2201
Cdd:PRK10522 406 FHLFDQLlgpEGKP-ANPALVEKW-LERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568912802 2202 ARRFLWNLILDLIK-TGRSVVLTSHSMEECEaLCTRLAIMVNGRLRCL 2248
Cdd:PRK10522 484 FRREFYQVLLPLLQeMGKTIFAISHDDHYFI-HADRLLEMRNGQLSEL 530
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
986-1160 |
4.56e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 986 MALNKLSLNLYENQV----VSFL--------GHNGAGKTTTMSILTGLFPPTSGSatIYGHDIRTemDEIRKNLGMCPQH 1053
Cdd:PRK13541 2 LSLHQLQFNIEQKNLfdlsITFLpsaityikGANGCGKSSLLRMIAGIMQPSSGN--IYYKNCNI--NNIAKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 NV-LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLeLSNKrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1132
Cdd:PRK13541 78 NLgLKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDL-LDEK----CYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180
....*....|....*....|....*....
gi 568912802 1133 GVDPYARRAIWDLI-LKYKPGRTILLSTH 1160
Cdd:PRK13541 153 NLSKENRDLLNNLIvMKANSGGIVLLSSH 181
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
973-1181 |
4.56e-08 |
|
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: 56.79 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPpTSGSATIYGHDIRT-EMDEIRKNLGMCP 1051
Cdd:cd03289 5 VKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRlTVEEHLWFYSRLKSmaqEEIRKETDK-----MIE------DLELSNKRHslvqTLSGGMKRKLSVAIAFVG 1120
Cdd:cd03289 84 QKVFIFSG-TFRKNLDPYGKWSD---EEIWKVAEEvglksVIEqfpgqlDFVLVDGGC----VLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1121 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLK 1181
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2032-2282 |
4.67e-08 |
|
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: 58.28 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKD---LLQVQ 2108
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFT-----IEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEkcgYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 QSLGY-CP-------QFDALFDELTAREHLQLYTRL-----RGIPWKDEAQVVKWALEKLELTKYADKP----------- 2164
Cdd:TIGR03269 76 SKVGEpCPvcggtlePEEVDFWNLSDKLRRRIRKRIaimlqRTFALYGDDTVLDNVLEALEEIGYEGKEavgravdliem 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2165 ----------AGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEAL 2233
Cdd:TIGR03269 156 vqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVIEDL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568912802 2234 CTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQNVKDVVRFFN 2282
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRN 284
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1976-2245 |
4.69e-08 |
|
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: 58.57 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1976 AMTVEGFVGFFLTIMCQYNFLRQ-------PQRLPVSTKPVEDDVDVASER-------QRVlRGDadndmVKIENLTKVY 2041
Cdd:TIGR02203 267 SLTAGDFTAFITAMIALIRPLKSltnvnapMQRGLAAAESLFTLLDSPPEKdtgtraiERA-RGD-----VEFRNVTFRY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2042 KSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ-VQQSLGYCPQFDAL 2120
Cdd:TIGR02203 341 PGRDRP---ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAsLRRQVALVSQDVVL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2121 FDELTAREhlQLYTRLRGIpwkDEAQVVKwALEKLELTKYADK-PAGTY----------SGGNKRKLSTAIALIGYPAFI 2189
Cdd:TIGR02203 418 FNDTIANN--IAYGRTEQA---DRAEIER-ALAAAYAQDFVDKlPLGLDtpigengvllSGGQRQRLAIARALLKDAPIL 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2190 FLDEPTTGMDPKARRfLWNLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRL 2245
Cdd:TIGR02203 492 ILDEATSALDNESER-LVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2029-2256 |
5.91e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DL 2104
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCI-----FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2105 LQVQQSLGYCPQFDALFDELTA--------REHLQLytrlrgiPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRK- 2175
Cdd:PRK11831 80 YTVRKRMSMLFQSGALFTDMNVfdnvayplREHTQL-------PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2176 -LSTAIALigYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2253
Cdd:PRK11831 153 aLARAIAL--EPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
...
gi 568912802 2254 LKN 2256
Cdd:PRK11831 231 LQA 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
973-1181 |
6.73e-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: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFpPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1051
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1052 QHNVLFDRlTVEEHLWFYSRlksMAQEEIRKETDK-----MIE------DLELSNKRHslvqTLSGGMKRKLSVAIAFVG 1120
Cdd:TIGR01271 1299 QKVFIFSG-TFRKNLDPYEQ---WSDEEIWKVAEEvglksVIEqfpdklDFVLVDGGY----VLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1121 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLK 1181
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV-EALLECQQFLVIEGSSVK 1430
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
2055-2226 |
7.80e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2055 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdllqVQQS-LGYCPQFDALFDELTAREHLQLY 2133
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPyCTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 TRLRgipwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2213
Cdd:PRK13541 95 SEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|...
gi 568912802 2214 IKTGRSVVLTSHS 2226
Cdd:PRK13541 170 ANSGGIVLLSSHL 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
991-1188 |
8.18e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 991 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP----TSGS----------ATIYGHDIRTEMDEIRKNLGmcPQHNVl 1056
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRvlldgkpvapCALRGRKIATIMQNPRSAFN--PLHTM- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1057 fdRLTVEEHLWFYSRLKSMAQeeirketdkMIEDLE---LSNKRHSLVQ---TLSGGMKRKLSVAIAFVGGSRAIILDEP 1130
Cdd:PRK10418 99 --HTHARETCLALGKPADDAT---------LTAALEavgLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 1131 TAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS--PLF 1188
Cdd:PRK10418 168 TTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDveTLF 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2032-2242 |
9.26e-08 |
|
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: 55.31 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQS 2110
Cdd:cd03254 3 IEFENVNFSYDEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDElTAREHLQLytrlrGIPWKDEAQVVKWA--------LEKLE--LTKYADKPAGTYSGGNKRKLSTAI 2180
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRL-----GRPNATDEEVIEAAkeagahdfIMKLPngYDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2181 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHsmeecealctRLAIMVN 2242
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAH----------RLSTIKN 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
973-1164 |
9.34e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 973 VDKLTKVYKNDKK----MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAtiyghDIRTEMDEIRKNLG 1048
Cdd:PRK13545 21 FDKLKDLFFRSKDgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1049 mcpqhnvLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:PRK13545 96 -------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 568912802 1129 EPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDE 1164
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEqGKTIFFISHSLSQ 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
987-1237 |
9.66e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDI----RTEMDEIR-KNLGMCPQhnvlfD 1058
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRaEQISMIFQ-----D 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 RLT-------VEEHLWFYSRL-KSMAQEEIRKETDKMIEDLEL--SNKRHSLV-QTLSGGMKRKLSVAIAFVGGSRAIIL 1127
Cdd:PRK09473 106 PMTslnpymrVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMpeARKRMKMYpHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1128 DEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGA--YGDGY---- 1197
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNArdVFYQPShpYSIGLlnav 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1198 -RL-----TLVKQPAEPgtsqePGLASSPSGCPRLSSC--------SEPQVSQF 1237
Cdd:PRK09473 266 pRLdaegeSLLTIPGNP-----PNLLRLPKGCPFQPRCphameicsSAPPLEEF 314
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2015-2254 |
9.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2015 VASERQRVLRGDADNDM----VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-DESTT 2089
Cdd:PRK14271 1 MACERLGGQSGAADVDAaapaMAAVNLTLGFAGKTV-----LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2090 G----GEAFVNGHSVL--KDLLQVQQSLGYC-----PQFDALFDELTA--REH-LQLYTRLRGIPWKDEAQVVKWALEKL 2155
Cdd:PRK14271 76 GyrysGDVLLGGRSIFnyRDVLEFRRRVGMLfqrpnPFPMSIMDNVLAgvRAHkLVPRKEFRGVAQARLTEVGLWDAVKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2156 ELTkyaDKPAgTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTgRSVVLTSHSMEECEALCT 2235
Cdd:PRK14271 156 RLS---DSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISD 230
|
250
....*....|....*....
gi 568912802 2236 RLAIMVNGRLRCLGSIQHL 2254
Cdd:PRK14271 231 RAALFFDGRLVEEGPTEQL 249
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
981-1179 |
1.22e-07 |
|
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: 54.40 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 981 KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtemdeirknLGMCPQ-------- 1052
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQepwiqngt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1053 --HNVLFDRltVEEHLWFYSRLKSMAQEEirketdkmieDLE-LSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAI 1125
Cdd:cd03250 82 irENILFGK--PFDEERYEKVIKACALEP----------DLEiLPDGDLTEIGekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1126 ILDEPTAGVDPYARRAIWD-LILKY-KPGRTILLSTHHMdeaDLLG--DRIAIISHGK 1179
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFEnCILGLlLNNKTRILVTHQL---QLLPhaDQIVVLDNGR 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
997-1194 |
1.41e-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: 55.07 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 997 ENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatiygHDIRTEMDEIRKNLGMCPQHN----VLFDRLTVEEHLWFYSRL 1072
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-----FDDPPDWDEILDEFRGSELQNyftkLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1073 KSMAQ---EEIRKETDK------MIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR---- 1139
Cdd:cd03236 100 PKAVKgkvGELLKKKDErgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaa 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 1140 RAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIaiishgklkCC--GSPlflkGAYG 1194
Cdd:cd03236 180 RLIRELA---EDDNYVLVVEHDLAVLDYLSDYI---------HClyGEP----GAYG 220
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
960-1136 |
1.81e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 960 MEEEPTHLPLVVCVDKLTkvYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT- 1038
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1039 EMDEIRKNLGMCPQhnvLFDRLTVEEHLWFysrLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAF 1118
Cdd:PRK13543 79 DRSRFMAYLGHLPG---LKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLW 152
|
170
....*....|....*...
gi 568912802 1119 VGGSRAIILDEPTAGVDP 1136
Cdd:PRK13543 153 LSPAPLWLLDEPYANLDL 170
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2059-2254 |
1.90e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.03 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTG-DESTTG----GEAFVNGHSVLKDLLQVQQSLGYCPQFDalfdeltarEHlQLY 2133
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGlLQPTSGtvtiGERVITAGKKNKKLKPLRKKVGIVFQFP---------EH-QLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2134 --TRLR---------GIPWKDEAQVVKWALEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2201
Cdd:PRK13634 100 eeTVEKdicfgpmnfGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2202 ARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2254
Cdd:PRK13634 180 GRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2033-2250 |
1.94e-07 |
|
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: 53.68 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2033 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDEST--TGGEAFVNGHSVLkdllqvqqs 2110
Cdd:cd03217 2 EIKDLHVSVGGKEI-----LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDIT--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 lgycpqfdalfdeltareHLQLYTRLR---GIPWKDEAQV--VKWAleklELTKYADKpagTYSGGNKRKLSTAIALIGY 2185
Cdd:cd03217 68 ------------------DLPPEERARlgiFLAFQYPPEIpgVKNA----DFLRYVNE---GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAL-CTRLAIMVNGRLRCLGS 2250
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
932-1180 |
2.96e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 932 WAHTPRLSVMEEDQACAME-----SRHFEETrgmeeepTHLP--LVVCVDKLTKVykndKKMALNKLSLNLYENQVVSFL 1004
Cdd:PRK10982 212 WIATQPLAGLTMDKIIAMMvgrslTQRFPDK-------ENKPgeVILEVRNLTSL----RQPSIRDVSFDLHKGEILGIA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1005 GHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEI----------RKNLGMCPQHNVLFDRL--TVEEHLwfyS 1070
Cdd:PRK10982 281 GLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAInhgfalvteeRRSTGIYAYLDIGFNSLisNIRNYK---N 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1071 RLKSMAQEEIRKETDKMIEDLELSNKRHS-LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY 1149
Cdd:PRK10982 358 KVGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL 437
|
250 260 270
....*....|....*....|....*....|....
gi 568912802 1150 -KPGRTILLSTHHMDEadLLG--DRIAIISHGKL 1180
Cdd:PRK10982 438 aKKDKGIIIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2029-2225 |
3.44e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAfvnghSVLKDLlqvq 2108
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRII-----LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAKGI---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2109 qSLGYCPQFDALFdeLTAREH-LQLYTRLrgIPWKDEAQvvkwalekleLTKY-------ADK---PAGTYSGGNKRKLS 2177
Cdd:PRK10636 376 -KLGYFAQHQLEF--LRADESpLQHLARL--APQELEQK----------LRDYlggfgfqGDKvteETRRFSGGEKARLV 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568912802 2178 TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2225
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVSH 485
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2057-2228 |
3.57e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.82 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2057 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQVQQSLGYCPQFDA-----LFDELT-AREHL 2130
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG----QTINLVRDKDGQLKVADKnqlrlLRTRLTmVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2131 QLYTRLRGIPWKDEAQVVKWALEKLEL----TKYADK------PAGTY----SGGNKRKLSTAIALIGYPAFIFLDEPTT 2196
Cdd:PRK10619 102 NLWSHMTVLENVMEAPIQVLGLSKQEAreraVKYLAKvgiderAQGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190
....*....|....*....|....*....|..
gi 568912802 2197 GMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2228
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2032-2225 |
4.95e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkdllqvqqSL 2111
Cdd:PRK11819 325 IEAENLSKSFGDR-----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT-IKIGETV---------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQF-DALFDELTArehlqlytrlrgipWkdeaQVVKWALEKLELTKY---------------AD--KPAGTYSGGNK 2173
Cdd:PRK11819 390 AYVDQSrDALDPNKTV--------------W----EEISGGLDIIKVGNReipsrayvgrfnfkgGDqqKKVGVLSGGER 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2174 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2225
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PGCAVVISH 500
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
980-1135 |
8.13e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 8.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1058
Cdd:PLN03130 1247 YRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 ---RLTVE---EH----LWfYSRLKSMAQEEIRKETDKMieDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIILD 1128
Cdd:PLN03130 1327 gtvRFNLDpfnEHndadLW-ESLERAHLKDVIRRNSLGL--DAEVSEAG----ENFSVGQRQLLSLARALLRRSKILVLD 1399
|
....*..
gi 568912802 1129 EPTAGVD 1135
Cdd:PLN03130 1400 EATAAVD 1406
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2164-2228 |
8.58e-07 |
|
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: 53.16 E-value: 8.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2164 PAGTYSGGNKRKLSTAIALI---GYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2228
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2029-2245 |
9.41e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2029 NDMVKIENLTkVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTST----FKMLTGDESTTGGEAFVNGHSVLKDL 2104
Cdd:PRK10418 2 PQQIELRNIA-LQAAQPL-----VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2105 LQ------VQQSlgycPQ--FDALfdeLTAREHLQLYTRLRGIPwKDEAQVVKwALEKLELTKyADKPAGTY----SGGN 2172
Cdd:PRK10418 76 LRgrkiatIMQN----PRsaFNPL---HTMHTHARETCLALGKP-ADDATLTA-ALEAVGLEN-AARVLKLYpfemSGGM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2173 KRKLSTAIALIGYPAFIFLDEPTTGMDPKAR-RFLwNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRL 2245
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQaRIL-DLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2011-2236 |
1.11e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2011 DDVDvASERQR-VLRGDADNDM----VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD 2085
Cdd:PRK15064 295 EEVK-PSSRQNpFIRFEQDKKLhrnaLEVENLTKGFDNGPL-----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2086 ESTTGGEafvnghsvlkdllqVQQS----LGYCPQ-----FDalfDELTAREHLQLYTRLrgipwKDEAQVVKWALEKLE 2156
Cdd:PRK15064 369 LEPDSGT--------------VKWSenanIGYYAQdhaydFE---NDLTLFDWMSQWRQE-----GDDEQAVRGTLGRLL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2157 LTK-YADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLwNLILDLIKTgrSVVLTSHSMEECEALCT 2235
Cdd:PRK15064 427 FSQdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL-NMALEKYEG--TLIFVSHDREFVSSLAT 503
|
.
gi 568912802 2236 R 2236
Cdd:PRK15064 504 R 504
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2044-2254 |
1.12e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2044 RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKtstfkmltgdeSTTG----------GEAFVNGHSVlkDLLQVQQSLGY 2113
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGK-----------STTGlallrlinsqGEIWFDGQPL--HNLNRRQLLPV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2114 CPQFDALFDE----LTAR--------EHLQLYTRLRGiPWKDEAQVVKwALEKLEL---TKYadKPAGTYSGGNKRKLST 2178
Cdd:PRK15134 361 RHRIQVVFQDpnssLNPRlnvlqiieEGLRVHQPTLS-AAQREQQVIA-VMEEVGLdpeTRH--RYPAEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2179 AIALIGYPAFIFLDEPTTGMDpkarRFLWNLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2253
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLD----KTVQAQILALLKSlqqkhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
.
gi 568912802 2254 L 2254
Cdd:PRK15134 513 V 513
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2051-2225 |
1.19e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 54.02 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLlqvQQSLGYCPQfDA-LFDElT 2125
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdltLESL---RRQIGVVPQ-DTfLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2126 AREHLQLytrlrGIPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEP 2194
Cdd:COG1132 430 IRENIRY-----GRPDATDEEVEE-AAKAAQAHEFIEAlPDGydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190
....*....|....*....|....*....|.
gi 568912802 2195 TTGMDPKARRFLWNLILDLIKtGRSVVLTSH 2225
Cdd:COG1132 504 TSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2051-2244 |
1.23e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG----DES-----------TTGGEAFVNGHS-VLKDLLQVQQS---- 2110
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyqkDSGsilfqgkeidfKSSKEALENGISmVHQELNLVLQRsvmd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 ---LGYCPQFDALFDeltareHLQLYTRLRGIpwkdeaqvvkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2187
Cdd:PRK10982 93 nmwLGRYPTKGMFVD------QDKMYRDTKAI------------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2188 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2244
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
988-1179 |
1.37e-06 |
|
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: 51.45 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 988 LNKLSLN----LYENQVVSFL-------GHNGAGKTTTMS----ILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMC 1050
Cdd:cd03240 1 IDKLSIRnirsFHERSEIEFFspltlivGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIRegEVRAQVKLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 PQHNVLFDR-LTVEEHLWFYSrlksmaQEEIRKETDKMIEdlelsnkrhslvqTLSGGMKRKLSV----AIAFVGGSRA- 1124
Cdd:cd03240 81 NGKKYTITRsLAILENVIFCH------QGESNWPLLDMRG-------------RCSGGEKVLASLiirlALAETFGSNCg 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 1125 -IILDEPTAGVDPYARR-AIWDLI--LKYKPGRTILLSTHHMDEADLLGD--RIAIISHGK 1179
Cdd:cd03240 142 iLALDEPTTNLDEENIEeSLAEIIeeRKSQKNFQLIVITHDEELVDAADHiyRVEKDGRQK 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
2043-2250 |
1.64e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2043 SRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTG--------GEAFVNGHSVLK-DLLQVQQSLGY 2113
Cdd:PRK13547 10 ARRHRAIL--RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAiDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2114 CPQ-----FDALFDELT-------AREHLQLYTRLRGIPWKdeaqvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2181
Cdd:PRK13547 88 LPQaaqpaFAFSAREIVllgryphARRAGALTHRDGEIAWQ--------ALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2182 L---------IGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECEALCTRLAIMVNGRLRCLGS 2250
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
987-1135 |
1.93e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMDEIRKNLGMCPQHNV--LFDRL 1060
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1061 TV----EEHLWFYSrlKSMAQEEIRKETDKMIEDLEL-SNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:PRK15079 116 TIgeiiAEPLRTYH--PKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2032-2263 |
2.62e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKDLLQVQQSL 2111
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLD-----IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRFGDGYM 2263
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFVAGFI 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2052-2229 |
2.64e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.87 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2052 VDRLCLGVRPGEcFGLL-GVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREH 2129
Cdd:PRK10247 23 LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2130 LQLYTRLRGIpwKDEAQVVKWALEKLELTKYA-DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2208
Cdd:PRK10247 101 LIFPWQIRNQ--QPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170 180
....*....|....*....|..
gi 568912802 2209 LILDLIK-TGRSVVLTSHSMEE 2229
Cdd:PRK10247 179 IIHRYVReQNIAVLWVTHDKDE 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2059-2199 |
3.50e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTsTF-KMLTGDESTTGGEafvnghsVLKDLlqvqqSLGYCPQFDALFDELTAREHL-QLYTRL 2136
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKT-TFaKLLAGVLKPDEGE-------VDPEL-----KISYKPQYIKPDYDGTVEDLLrSITDDL 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 2137 RGIPWKDEaqvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALiGYPAFIF-LDEPTTGMD 2199
Cdd:PRK13409 429 GSSYYKSE------IIKPLQLERLLDKNVKDLSGGELQRVAIAACL-SRDADLYlLDEPSAHLD 485
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2057-2225 |
4.10e-06 |
|
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: 50.31 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2057 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkDLLQVQQ-----SLGYCPQFDALFDElTAREHLQ 2131
Cdd:cd03253 22 FTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ----DIREVTLdslrrAIGVVPQDTVLFND-TIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2132 lYTRLRGipwkDEAQVVKWA--------LEKLElTKYADKPA--GTY-SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2200
Cdd:cd03253 97 -YGRPDA----TDEEVIEAAkaaqihdkIMRFP-DGYDTIVGerGLKlSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180
....*....|....*....|....*
gi 568912802 2201 KARRFLWNLILDLIKtGRSVVLTSH 2225
Cdd:cd03253 171 HTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2032-2199 |
4.13e-06 |
|
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: 52.09 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKigriLAVDRlclG-VRPGECFGLLGVNGAGKTsTF-KMLTGDESTTGGEafvnghsvlkdlLQVQQ 2109
Cdd:COG1245 342 VEYPDLTKSYGGFS----LEVEG---GeIREGEVLGIVGPNGIGKT-TFaKILAGVLKPDEGE------------VDEDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 SLGYCPQFDALFDELTAREHL--QLYTRLRGIPWKDEaqvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALiGYPA 2187
Cdd:COG1245 402 KISYKPQYISPDYDGTVEEFLrsANTDDFGSSYYKTE------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACL-SRDA 474
|
170
....*....|...
gi 568912802 2188 FIF-LDEPTTGMD 2199
Cdd:COG1245 475 DLYlLDEPSAHLD 487
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2059-2203 |
4.21e-06 |
|
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: 50.48 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2059 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkdllqvqqslGYCPQFDALFDELTAREHLQLYTRLRG 2138
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 2139 IP--WKDEaqvvkwALEKLELTKYADKPAGTYSGGNKRKlsTAIAL-IGYPAFIFL-DEPTTGMDPKAR 2203
Cdd:cd03237 91 THpyFKTE------IAKPLQIEQILDREVPELSGGELQR--VAIAAcLSKDADIYLlDEPSAYLDVEQR 151
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2031-2203 |
6.71e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.00 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV------LKDL 2104
Cdd:PRK11650 3 GLKLQAVRKSYD----GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepaDRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2105 LQVQQSlgYcpqfdALFDELTAREHLQLYTRLRGIPwKDE-AQVVKWALEKLELTKYAD-KPAgTYSGGNKRKLSTAIAL 2182
Cdd:PRK11650 79 AMVFQN--Y-----ALYPHMSVRENMAYGLKIRGMP-KAEiEERVAEAARILELEPLLDrKPR-ELSGGQRQRVAMGRAI 149
|
170 180
....*....|....*....|..
gi 568912802 2183 IGYPA-FIFlDEPTTGMDPKAR 2203
Cdd:PRK11650 150 VREPAvFLF-DEPLSNLDAKLR 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
971-1266 |
7.22e-06 |
|
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: 51.87 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 971 VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMc 1050
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSL- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1051 pQHNVLFDRLTVEEHlwFYSRLKSMAqeeirketdkMIEDLEL--SNKRHSLVQ---TLSGGMKRKLSVAIAFVGGSRAI 1125
Cdd:TIGR00957 716 -RENILFGKALNEKY--YQQVLEACA----------LLPDLEIlpSGDRTEIGEkgvNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1126 ILDEPTAGVDPYARRAIWDLILKYK---PGRTILLSTHHMDEADLLgDRIAIISHGKLKCCGS-PLFLK--GAYGDGYRl 1199
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSyQELLQrdGAFAEFLR- 860
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912802 1200 tlVKQPAEPGTSQEPGLASSPSGCPRLSSCSEPQVS-------QFIRKHVASSLLVSDTSTELSyilPSEAVKK 1266
Cdd:TIGR00957 861 --TYAPDEQQGHLEDSWTALVSGEGKEAKLIENGMLvtdvvgkQLQRQLSASSSDSGDQSRHHG---SSAELQK 929
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2032-2200 |
1.06e-05 |
|
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: 49.03 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTST----FKMLtgdeSTTGGEAFVNGHSVLK-DLLQ 2106
Cdd:cd03244 3 IEFKNVSLRYRP---NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKiGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQQSLGYCPQFDALFDElTAREHLQLYTRlrgipwKDEAQVVKwALEKLELTKYADKPAGT-----------YSGGNKRK 2175
Cdd:cd03244 76 LRSRISIIPQDPVLFSG-TIRSNLDPFGE------YSDEELWQ-ALERVGLKEFVESLPGGldtvveeggenLSVGQRQL 147
|
170 180
....*....|....*....|....*
gi 568912802 2176 LSTAIALIGYPAFIFLDEPTTGMDP 2200
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDP 172
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1097-1160 |
1.19e-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: 47.74 E-value: 1.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1097 RHSLVQTLSGGMKRKLSVAIAFVGGSRA----IILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTH 1160
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILALASLKprplYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITH 139
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2060-2225 |
1.64e-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: 50.17 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2060 RPGECFGLLGVNGAGKTSTFKMLTGD------------------ESTTGGEAfvngHSVLKDLLQVQQSLGYCPQF-DAL 2120
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswdevlKRFRGTEL----QDYFKKLANGEIKVAHKPQYvDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2121 FDEL--TAREHLQLYtrlrgipwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2198
Cdd:COG1245 173 PKVFkgTVRELLEKV---------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*..
gi 568912802 2199 DPKARRFLWNLILDLIKTGRSVVLTSH 2225
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2031-2213 |
1.78e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.02 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSR----KIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLL 2105
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2106 QVQQSLGYCPQfdalfDELTAREHLQLYTRLRGIPWKDEAQVVKWALEK---LELTKYADKP--AGTY----SGGNKRKL 2176
Cdd:PRK15112 84 YRSQRIRMIFQ-----DPSTSLNPRQRISQILDFPLRLNTDLEPEQREKqiiETLRQVGLLPdhASYYphmlAPGQKQRL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 568912802 2177 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2213
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2057-2225 |
1.81e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2057 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ-----------------VQQSLGYCPQFDA 2119
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvydfvaegIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2120 LFDELT---AREHLQLYTRLRGI-----PWKDEAQVvKWALEKLELTkyADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:PRK11147 104 ISHLVEtdpSEKNLNELAKLQEQldhhnLWQLENRI-NEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLL 180
|
170 180 190
....*....|....*....|....*....|....
gi 568912802 2192 DEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2225
Cdd:PRK11147 181 DEPTNHLDIETIEWLEGFLKTF---QGSIIFISH 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2051-2199 |
1.96e-05 |
|
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: 50.12 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2051 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREH 2129
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 2130 LQLYTRlRGIPWKDEAQVVKWA-----LEKLEL---TKYADKpAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD 2199
Cdd:TIGR01193 568 LLLGAK-ENVSQDEIWAACEIAeikddIENMPLgyqTELSEE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1963-2256 |
2.06e-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: 50.29 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1963 SPFEWDIVTrglvAMTVEGFVgffLTIMCQYNFLRQPQRLPV---STKPVEDDVDVASERQRVLRGDADNDMVKIENLTK 2039
Cdd:TIGR01271 1153 STLQWAVNS----SIDVDGLM---RSVSRVFKFIDLPQEEPRpsgGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTA 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2040 VYKSRkiGRILAVDrLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTgGEAFVNGHSVLKDLLQV-QQSLGYCPQFD 2118
Cdd:TIGR01271 1226 KYTEA--GRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTwRKAFGVIPQKV 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2119 ALFDElTAREHLQLYTRlrgipWKDEaQVVKWALE---KLELTKYADK-----PAGTY--SGGNKRKLSTAIALIGYPAF 2188
Cdd:TIGR01271 1302 FIFSG-TFRKNLDPYEQ-----WSDE-EIWKVAEEvglKSVIEQFPDKldfvlVDGGYvlSNGHKQLMCLARSILSKAKI 1374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912802 2189 IFLDEPTTGMDPkarrFLWNLILDLIKTGRS---VVLTSHSME---ECEALctrlaIMVNG-RLRCLGSIQHLKN 2256
Cdd:TIGR01271 1375 LLLDEPSAHLDP----VTLQIIRKTLKQSFSnctVILSEHRVEallECQQF-----LVIEGsSVKQYDSIQKLLN 1440
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2032-2225 |
2.56e-05 |
|
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: 47.92 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKDL-LQ-VQQ 2109
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPIL--KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLnLRwLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2110 SLGYCPQFDALFDeLTAREHLQLytrlrGIPWKDEAQVVKwALEKLELTKYADKPAGTY-----------SGGNKRKLST 2178
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENIRY-----GKPDATDEEVEE-AAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568912802 2179 AIALIGYPAFIFLDEPTTGMDPKARRflwnLI---LDLIKTGRSVVLTSH 2225
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEK----LVqeaLDRAMKGRTTIVIAH 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2032-2225 |
2.63e-05 |
|
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: 48.00 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLlqv 2107
Cdd:cd03251 1 VEFKNVTFRYPGDGP---PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdytLASL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2108 QQSLGYCPQFDALFDElTAREHLqLYtrlrGIPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNKRKL 2176
Cdd:cd03251 75 RRQIGLVSQDVFLFND-TVAENI-AY----GRPGATREEVEE-AARAANAHEFIMElPEGydtvigergvKLSGGQRQRI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568912802 2177 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSH 2225
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2032-2228 |
3.41e-05 |
|
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: 46.38 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTkvYKSRKiGRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAfvnGHSVLKDLLQVQQsL 2111
Cdd:cd03223 1 IELENLS--LATPD-GRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGEDLLFLPQ-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2112 GYCPQfdalfdeLTAREHLqLYtrlrgiPWKDEaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFL 2191
Cdd:cd03223 73 PYLPL-------GTLREQL-IY------PWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568912802 2192 DEPTTGMDPKARRFLWNLILD----LIKTGRSVVLTS-HSME 2228
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKElgitVISVGHRPSLWKfHDRV 157
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
970-1185 |
3.65e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 970 VVCVDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---------- 1037
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1038 ----TEMDEIR-KNLGMCPQH-----NVLFdrlTVEEHLWFYSRL-KSMAQEEIRKETDKMIEDLELSNKRHSLVQ---T 1103
Cdd:PRK10261 92 eqsaAQMRHVRgADMAMIFQEpmtslNPVF---TVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1104 LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1181
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....
gi 568912802 1182 CCGS 1185
Cdd:PRK10261 249 ETGS 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
987-1180 |
3.71e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 987 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIRKNLGMCPQ--HNVLFDRL 1060
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1061 TVEEHLWFYSRLKSMAQ-EEIRKETDKMIEDLELSnKRHSL--VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1137
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLL-PEHAWryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568912802 1138 ARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKL 1180
Cdd:PRK10261 498 IRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2047-2254 |
3.92e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.86 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2047 GRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDELT 2125
Cdd:PRK10575 23 GRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2126 AREhlqlytrLRGI---PW--------KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEP 2194
Cdd:PRK10575 102 VRE-------LVAIgryPWhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912802 2195 TTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2254
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1994-2273 |
4.85e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1994 NFLRQPQRLPVSTKPVE---DDVDVASE------RQRVLRGDADNDMVKIENLTKVYKSrkiGRILAVDRLCLGVRPGEC 2064
Cdd:PLN03232 1188 GVLRQASKAENSLNSVErvgNYIDLPSEataiieNNRPVSGWPSRGSIKFEDVHLRYRP---GLPPVLHGLSFFVSPSEK 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2065 FGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREHLQlytrlrgiPWKD 2143
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSG-TVRFNID--------PFSE 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2144 EAQVVKW-ALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2211
Cdd:PLN03232 1336 HNDADLWeALERAHIKDVIDRnPFGldaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR 1415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2212 DLIKTGrSVVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQN 2273
Cdd:PLN03232 1416 EEFKSC-TMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2032-2229 |
4.89e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.34 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT------GDESTTGGEAFVNGH----SVL 2101
Cdd:PRK14258 8 IKVNNLSFYYDTQKI-----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNiyerRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2102 KDLLQVQQSLGYcPQFDaLFdELTAREHLQLYTRLRGipWKDEAQ---VVKWALEKLEL----TKYADKPAGTYSGGNKR 2174
Cdd:PRK14258 83 LNRLRRQVSMVH-PKPN-LF-PMSVYDNVAYGVKIVG--WRPKLEiddIVESALKDADLwdeiKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2175 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEE 2229
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
989-1224 |
5.02e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 989 NKLSLNLYENQVVSFLGHNGAGKT-TTMSILTGL-FPP---TSGSATIYGHDI----RTEMDEIRKN-LGMCPQH----- 1053
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLlhasEQTLRGVRGNkIAMIFQEpmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 NVLFdrlTVEEHLW-FYSRLKSMAQEEIRKEtdkMIEDLELSNKRHS------LVQTLSGGMKRKLSVAIAFVGGSRAII 1126
Cdd:PRK15134 106 NPLH---TLEKQLYeVLSLHRGMRREAARGE---ILNCLDRVGIRQAakrltdYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1127 LDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKlkccgsplflkgAYGDGYRLTLVKQ 1204
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR------------CVEQNRAATLFSA 247
|
250 260
....*....|....*....|
gi 568912802 1205 PAEPGTSQEpgLASSPSGCP 1224
Cdd:PRK15134 248 PTHPYTQKL--LNSEPSGDP 265
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
982-1180 |
6.11e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 982 NDKKMaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTG--LFPPTSGSATIYGHDIRTEMDEIRKNLG--MCPQH---- 1053
Cdd:CHL00131 18 NENEI-LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGifLAFQYpiei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1054 ----NVLFDRLTveehlwFYSRLKSMAQEEIRKetdkmIEDLELSNKRHSLV------------QTLSGGMKRK---LSV 1114
Cdd:CHL00131 97 pgvsNADFLRLA------YNSKRKFQGLPELDP-----LEFLEIINEKLKLVgmdpsflsrnvnEGFSGGEKKRneiLQM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912802 1115 AIAfvgGSRAIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEAD-LLGDRIAIISHGKL 1180
Cdd:CHL00131 166 ALL---DSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDyIKPDYVHVMQNGKI 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2162-2245 |
7.47e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2162 DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMV 2241
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
....
gi 568912802 2242 NGRL 2245
Cdd:NF040905 479 EGRI 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1004-1135 |
1.17e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1004 LGHNGAGKTTTMSILTGL---FPPTSGSATIY-GHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMA--- 1076
Cdd:TIGR00956 93 LGRPGSGCSTLLKTIASNtdgFHIGVEGVITYdGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQnrp 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912802 1077 -----QEEIRKETDKMIEDLELSNKRHS-----LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:TIGR00956 173 dgvsrEEYAKHIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
983-1135 |
1.24e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 983 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPpTSGSATIYGHDI----RTEMDEIRKNLGMCPQ--HNVL 1056
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1057 FDRLTV----EEHLWFYSRLKSMAQEEIRkeTDKMIEDLELS-NKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1131
Cdd:PRK15134 376 NPRLNVlqiiEEGLRVHQPTLSAAQREQQ--VIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
....
gi 568912802 1132 AGVD 1135
Cdd:PRK15134 454 SSLD 457
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
2067-2251 |
1.43e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.41 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2067 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsVLKD------LLQVQQSLGYCPQfDA-LFDELTAREHLQlYtrlrGI 2139
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDaekgicLPPEKRRIGYVFQ-DArLFPHYKVRGNLR-Y----GM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2140 PWKDEAQ---VVKW-ALEKLeLTKYadkPAgTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD-PKARR---FLWNLIL 2211
Cdd:PRK11144 102 AKSMVAQfdkIVALlGIEPL-LDRY---PG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKREllpYLERLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568912802 2212 DlIKTgrSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2251
Cdd:PRK11144 177 E-INI--PILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2031-2225 |
1.69e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.03 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2031 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLLQ 2106
Cdd:PRK10535 4 LLELKDIRRSYPSGE-EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2107 VQ-QSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2185
Cdd:PRK10535 83 LRrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2225
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2041-2229 |
1.73e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2041 YKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESttggEAFVNgHSVL--------KDLLQVQQSLG 2112
Cdd:PRK10938 270 YNDRPI-----LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP----QGYSN-DLTLfgrrrgsgETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2113 YcpqfdalfdeLTAREHL--QLYTRLR-----------GI----PWKDEAQVVKWaLEKLELTKY-ADKPAGTYSGGNKR 2174
Cdd:PRK10938 340 Y----------VSSSLHLdyRVSTSVRnvilsgffdsiGIyqavSDRQQKLAQQW-LDILGIDKRtADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568912802 2175 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVL-TSHSMEE 2229
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAED 464
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2186-2290 |
2.15e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.15 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2186 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEecealctrLAIMVNgrlrcLGSIQHLKNRFGDGYMIT 2265
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH--------LLSEVP-----LENIRRLRRDSGGTTSTK 254
|
90 100
....*....|....*....|....*
gi 568912802 2266 VRTKSSQNVKDVVRFFNRNFPEAML 2290
Cdd:COG3593 255 LIDLDDEDLRKLLRYLGVTRSELLF 279
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
963-1142 |
2.23e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 963 EPTHLP-LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIRtemd 1041
Cdd:PRK10636 304 APESLPnPLLKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1042 eirknLGMCPQHNVLFDRLTvEEHLWFYSRLKSmaqeeirKETDKMIEDLE-----LSNKRHSLVQTLSGGMKRKLSVAI 1116
Cdd:PRK10636 377 -----LGYFAQHQLEFLRAD-ESPLQHLARLAP-------QELEQKLRDYLggfgfQGDKVTEETRRFSGGEKARLVLAL 443
|
170 180
....*....|....*....|....*.
gi 568912802 1117 AFVGGSRAIILDEPTAGVDPYARRAI 1142
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1001-1228 |
2.36e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1001 VSFLGHNGAGKTTTMSILTGLFPPTSGSATIyghdirtemdeIRKNLGMCPQHNVLFDRlTVEEHLWFYSRLKSMAQEEI 1080
Cdd:PLN03130 646 VAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TVRDNILFGSPFDPERYERA 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1081 RKETdKMIEDLELSnKRHSLVQ------TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYK-PGR 1153
Cdd:PLN03130 714 IDVT-ALQHDLDLL-PGGDLTEigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElRGK 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1154 TILLST---HHMDEAdllgDRIAIISHGKLK--------CCGSPLFLKGAYGDGYRLTLVKQPAE---PGTSQEPGLASS 1219
Cdd:PLN03130 792 TRVLVTnqlHFLSQV----DRIILVHEGMIKeegtyeelSNNGPLFQKLMENAGKMEEYVEENGEeedDQTSSKPVANGN 867
|
....*....
gi 568912802 1220 PSGCPRLSS 1228
Cdd:PLN03130 868 ANNLKKDSS 876
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
991-1160 |
2.67e-04 |
|
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: 46.33 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 991 LSLNLYENQVVsFL-GHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRknlgmcpQH-------NVLFDRLT 1061
Cdd:COG4615 351 IDLTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYR-------QLfsavfsdFHLFDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1062 VEEhlwfysrlksmaQEEIRKETDKMIEDLELSNK------RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1135
Cdd:COG4615 423 GLD------------GEADPARARELLERLELDHKvsvedgRFSTTD-LSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180 190
....*....|....*....|....*....|
gi 568912802 1136 PYARRAIWDLILkykP-----GRTILLSTH 1160
Cdd:COG4615 490 PEFRRVFYTELL---PelkarGKTVIAISH 516
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2162-2226 |
3.51e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 3.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912802 2162 DKPAGTYSGGNKR--KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHS 2226
Cdd:cd03238 82 GQKLSTLSGGELQrvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2052-2256 |
3.81e-04 |
|
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: 44.85 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2052 VDRLCLGVRPGECFGLLGVNGAGKTSTF----KMLtgdesTTGGEAFVNGHSVLKDLLQV-QQSLGYCPQFDALFDElTA 2126
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLsaflRLL-----NTEGDIQIDGVSWNSVPLQKwRKAFGVIPQKVFIFSG-TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2127 REHLQLYTRlrgipWKDEaQVVKWALE---KLELTKYADK-----PAGTY--SGGNKRKLSTAIALIGYPAFIFLDEPTT 2196
Cdd:cd03289 94 RKNLDPYGK-----WSDE-EIWKVAEEvglKSVIEQFPGQldfvlVDGGCvlSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2197 GMDPKARRFLwNLILDLIKTGRSVVLTSHSMeecEAL--CTRLAIMVNGRLRCLGSIQHLKN 2256
Cdd:cd03289 168 HLDPITYQVI-RKTLKQAFADCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLLN 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2055-2225 |
4.65e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2055 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGdeSTTG-GEAFVNGHSvLKDLLQVQQSL--GY-CPQFDALFdELTAREHL 2130
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG--LLPGsGSIQFAGQP-LEAWSAAELARhrAYlSQQQTPPF-AMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2131 QLYtrlrgIPWKDEAQVVKWALEKL-ELTKYADK---PAGTYSGGN-KRKLSTAIALIGYPA------FIFLDEPTTGMD 2199
Cdd:PRK03695 91 TLH-----QPDKTRTEAVASALNEVaEALGLDDKlgrSVNQLSGGEwQRVRLAAVVLQVWPDinpagqLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*.
gi 568912802 2200 PKARRFLWNLILDLIKTGRSVVLTSH 2225
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
2169-2225 |
5.78e-04 |
|
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: 42.73 E-value: 5.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912802 2169 SGGNKRKLSTAIAL-----IGYPaFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2225
Cdd:cd03227 79 SGGEKELSALALILalaslKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2027-2212 |
5.83e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2027 ADNDMVKIENLTkVYKSRkiGRILaVDRLCLGVRPGEcfGLL--GVNGAGKTSTFKMLTG-DESTTGgeafvnghsvlkd 2103
Cdd:COG4178 358 SEDGALALEDLT-LRTPD--GRPL-LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGlWPYGSG------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2104 llqvqqSLGYCPQFDALFdeLTAREHLQLYTrLRGI--------PWKDEAqvVKWALEKLELTKYADKP------AGTYS 2169
Cdd:COG4178 419 ------RIARPAGARVLF--LPQRPYLPLGT-LREAllypataeAFSDAE--LREALEAVGLGHLAERLdeeadwDQVLS 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568912802 2170 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2212
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
969-1031 |
9.45e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 9.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912802 969 LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI 1031
Cdd:PRK11819 323 KVIEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2032-2199 |
2.15e-03 |
|
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: 42.01 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2032 VKIENLTKVYKSrKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQS 2110
Cdd:cd03369 7 IEVENLSVRYAP-DLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2111 LGYCPQFDALFDElTAREHLQLYTRLrgipwkDEAQVvkwaLEKLELTKYADkpagTYSGGNKRKLSTAIALIGYPAFIF 2190
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDPFDEY------SDEEI----YGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLV 148
|
....*....
gi 568912802 2191 LDEPTTGMD 2199
Cdd:cd03369 149 LDEATASID 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
980-1203 |
2.44e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.20 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 980 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVLFD 1058
Cdd:cd03288 29 YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSIILQDPILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1059 rltveehlwfySRLKSMAQEEIRKETDKMIEDLELSNKRhSLVQTLSGGM--------------KRKL-SVAIAFVGGSR 1123
Cdd:cd03288 109 -----------GSIRFNLDPECKCTDDRLWEALEIAQLK-NMVKSLPGGLdavvteggenfsvgQRQLfCLARAFVRKSS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1124 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPLFLKgAYGDGYRLTLVK 1203
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENLL-AQEDGVFASLVR 254
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
969-1131 |
3.16e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 969 LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatiyghdIR-TEmdeiRKNL 1047
Cdd:PRK15064 318 NALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKwSE----NANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1048 GMCPQ-HNVLFDR-LTVEEhlWfysrlksMAQEEIRKETDKMI-----------EDLelsNKRhslVQTLSGGMKRKLSV 1114
Cdd:PRK15064 385 GYYAQdHAYDFENdLTLFD--W-------MSQWRQEGDDEQAVrgtlgrllfsqDDI---KKS---VKVLSGGEKGRMLF 449
|
170
....*....|....*..
gi 568912802 1115 AIAFVGGSRAIILDEPT 1131
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPT 466
|
|
| MelB |
COG2211 |
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]; |
687-812 |
4.69e-03 |
|
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
Pssm-ID: 441813 [Multi-domain] Cd Length: 447 Bit Score: 41.81 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 687 MMPLCMVISWVYSVAMTIQHIVAEKEH-RLKEVMKTMgLNNAVHWVAWFITGFVQLSISVTAlTAILKYGQVLMHSHVLI 765
Cdd:COG2211 188 IFAVLGLLAFLLTFFGTKERPVPEEEKvSLKESLKAL-LKNRPFLLLLLAYLLFFLALALVA-ALLLYYFKYVLGLSAAL 265
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568912802 766 IWLFLAVYAVATIMFCFLVSVL---YSKAKLASAcGGIIYFLSYVPYMYV 812
Cdd:COG2211 266 VGLLLALYFLAALLGAPLWPRLakrFGKKKAFII-GLLLAALGLLLLFFL 314
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2175-2257 |
7.10e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.04 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 2175 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2253
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 568912802 2254 LKNR 2257
Cdd:COG4170 246 ILKS 249
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1098-1179 |
8.92e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912802 1098 HSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAII 1175
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
....
gi 568912802 1176 SHGK 1179
Cdd:PRK15093 233 YCGQ 236
|
|
| |
