|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-2367 |
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: 1563.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1 MGFLHQLQLLLWKNVTLKRRSPWVLAFEIFIPLVLFFILLGLRQKKPTISVKEAFYTAAPLTSAGILPVMQSL-C----P 75
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIfCnvnnP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 76 DGQRDEFG-----FLQYANStvtqLLERLHRVVEEGNLFDPVRPSLG---SELEALRQRLEALssgpgtwESHSARPAVS 147
Cdd:TIGR01257 81 CFQSPTPGespgiVSNYNNS----ILARVYRDFQELLMDAPESQHLGqvwAELRTLSQFMDTL-------RTHPERIAGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 148 SFSLDSVARDQRELWRFLMQNLSLPNSTAQALLAARVDPSEVYRllfgPLPDLDGKlgflrkqepwsrlgsnpllqmeel 227
Cdd:TIGR01257 150 GIRIRDILKDEEALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAY----GVPDLELK------------------------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 228 llapalleqlTCAPGSGELGRILTMPEGHQVdlQGYRDAVCS-GQATAraQRFSDlaaELRNQLDTAKIAQQLgfdvPNG 306
Cdd:TIGR01257 202 ----------DIACSEALLERFIIFSQRRGA--QTVRDALCSlSQGTL--QWIED---TLYANVDFFKLFHVL----PTL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 307 SDPQPQAPSPQSLPALLGDLLD-AQKLLQDVDVLSALALLLPqgacagqasapqasslngLANSTGigansgsnttveeg 385
Cdd:TIGR01257 261 LDSRSQGINLRSWGGILSDMSPrIQEFIHRPSVQDLLWVTRP------------------LLQNGG-------------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 386 tqspvspasPDTlqgqcsaFVQLWAGLQPILCGnnrtiEPEAlrrGNMSSLGFTSKEQRN----LGL------------- 448
Cdd:TIGR01257 309 ---------PET-------FTQLMGILSDLLCG-----YPEG---GGSRVFSFNWYEDNNykafLGIdstrkdpiysydk 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 449 --------LVHLMTSNP---------------KILYAPVGSEADRVILKANETFAFVGNVTHYAQVWLNISTEIRSFLEQ 505
Cdd:TIGR01257 365 rttsfcnaLIQSLESNPltkiawraakpllmgKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDK 444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 506 GrlqqhlqWLQQYVADLQLHPEA---MNLSLEELPPALRQDFSLPNGTALLQQLDTIDNAACGWI------------QFM 570
Cdd:TIGR01257 445 S-------TQMTMIRDTLQNPTVkdfINRQLGEEGITAEAVLNFLYNGPREKQADDMTNFDWRDIfnitdrflrlanQYL 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 571 SKVSVDIFKGFPDEESIVNYTLNQAYQDNVtvFASVIFQTRK--DGSLPPHVHYKIRQNSSFTEKTNEIRRAYWRPGPNT 648
Cdd:TIGR01257 518 ECLVLDKFESYDDEVQLTQRALSLLEENRF--WAGVVFPDMYpwTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRA 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 649 GGRFYFLY---GFVWIQDMMERAIINTFVGHDVvEPGNYVQMFPYPCYTRDDFLFVIEHMMPLCMVISWVYSVAMTIQHI 725
Cdd:TIGR01257 596 DPVEDFRYiwgGFAYLQDMVEQGITRSQMQAEP-PVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSI 674
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 726 VAEKEHRLKEVMKTMGLNNAVHWVAWFITGFVQLSISVTALTAILKYGQVLMHSHVLIIWLFLAVYAVATIMFCFLVSVL 805
Cdd:TIGR01257 675 VLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTF 754
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 806 YSKAKLASACGGIIYFLSYVPYMYVAIREevahDKITAFEKCIASLMSTTAFGLGSKYFALYEVAGVGIQWHTFSQSPVE 885
Cdd:TIGR01257 755 FSKASLAAACSGVIYFTLYLPHILCFAWQ----DRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLE 830
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 886 GDDFNLLLAVTMLMVDTVVYGVLTWYIEAVHPGMYGLPRPWYFPLQKSYWLG----SGRTEawewswpwahtprlSVMEE 961
Cdd:TIGR01257 831 GDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGgegcSTREE--------------RALEK 896
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 962 DQACAMESRHFEETRGMEE---EPTHLPLV--VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL 1036
Cdd:TIGR01257 897 TEPLTEEMEDPEHPEGINDsffERELPGLVpgVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSIL 976
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1037 TGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRH 1116
Cdd:TIGR01257 977 TGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRN 1056
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1117 SLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHG 1196
Cdd:TIGR01257 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1197 KLKCCGSPLFLKGAYGDGYRLTLV---KQPAEPGTSQEPGLASSPSG----CP-RLSSCSEPQV--------SQFIRKHV 1260
Cdd:TIGR01257 1137 RLYCSGTPLFLKNCFGTGFYLTLVrkmKNIQSQRGGCEGTCSCTSKGfstrCPaRVDEITPEQVldgdvnelMDLVYHHV 1216
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1261 ASSLLVSDTSTELSYILPSEAVKKGAFERLFQQLEHSLDALHLSSFGLMDTTLEEVFLKVSEEDQSLENSEADVKESRKD 1340
Cdd:TIGR01257 1217 PEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKREN 1296
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1341 VLPgAEGLTAVGGQAGNLARCSELaqsqaslqsassvgSARGEEGTgysdgygdyrplfdnlqDPDNVSLQEAEmealaq 1420
Cdd:TIGR01257 1297 ANL-RHPCSGPTEKAGQTPQASHT--------------CSPGQPAA-----------------HPEGQPPPEPE------ 1338
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1421 vGQGSRKLEGWWLKMRQFHGLLVKRFHCARRNSKALCSQILLPAFFVCVAMTVALSVPEIGDLPPLVLSPSQY-HNYTqp 1499
Cdd:TIGR01257 1339 -DPGVPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYgQQYT-- 1415
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1500 rgnfipyaneerqeyrlRLSPDASPQQLVSTFrlpsgvgATCVLKSPAngslgpmlnlssgesrllaarfFDSMCL-ESF 1578
Cdd:TIGR01257 1416 -----------------FFSMDEPNSEHLEVL-------ADVLLNKPG----------------------FGNRCLkEEW 1449
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1579 TQGLPLSNfvppppspapsdspvspdedsLQAWNMslpPTAGP--------ETWTSAPSLPRlvhepVRCTCSAQGTGF- 1649
Cdd:TIGR01257 1450 LPEYPCGN---------------------STPWKT---PSVSPnithlfqkQKWTAAHPSPS-----CRCSTREKLTMLp 1500
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1650 SCPSSVGGHPPQMRVV-TGDILTDITGHNVSEYLLFT---------SDRFRLH--RYGAITFGNVQKSIPASFGARVP-- 1715
Cdd:TIGR01257 1501 ECPEGAGGLPPPQRTQrSTEILQDLTDRNISDFLVKTypalirsslKSKFWVNeqRYGGISIGGKLPAIPITGEALVGfl 1580
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1716 ------------PMVRKIAVRRVA-----------QVLYNNKGYHSMPTYLNSLNNAILRANLPKSKgNPAAYGITVTNH 1772
Cdd:TIGR01257 1581 sdlgqmmnvsggPVTREASKEMPDflkhletedniKVWFNNKGWHALVSFLNVAHNAILRASLPKDR-DPEEYGITVISQ 1659
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1773 PMNKTSASLS-LDYLLQGTDVVIAIFIIVAMSFVPASFVVFLVAEKSTKAKHLQFVSGCNPVIYWLANYVWDMLNYLVPA 1851
Cdd:TIGR01257 1660 PLNLTKEQLSeITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSA 1739
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1852 TCCVIILFVFDLPAYTSPTNFPAVLSLFLLYGWSITPIMYPASFWFEVPSSAYVFLIVINLFIGITATVATFLLQLFEHD 1931
Cdd:TIGR01257 1740 GLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENN 1819
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1932 KDLKVVNSYLKSCFLIFPNYNLGHGLMEMAYNEYINEYYAKIGQfDKMKSPFEWDIVTRGLVAMTVEGFVGFFLTIMCQY 2011
Cdd:TIGR01257 1820 RTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGE-EHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQH 1898
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2012 NF-----LRQPQRLPVstkpVEDDVDVASERQRVLRGDADNDMVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLL 2086
Cdd:TIGR01257 1899 HFflsrwIAEPAKEPI----FDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP---AVDRLCVGVRPGECFGLL 1971
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2087 GVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVV 2166
Cdd:TIGR01257 1972 GVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVA 2051
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2167 KWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2246
Cdd:TIGR01257 2052 NWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2131
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2247 ECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQ-----NVKDVVRFFNRNFPEAMLKERHHTKVQYQLK 2321
Cdd:TIGR01257 2132 ECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllpDLNPVEQFFQGNFPGSVQRERHYNMLQFQVS 2211
|
2490 2500 2510 2520
....*....|....*....|....*....|....*....|....*.
gi 110225379 2322 SEhiSLAQVFSKMEQVVGVLGIEDYSVSQTTLDNVFVNFAKKQSDN 2367
Cdd:TIGR01257 2212 SS--SLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTET 2255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2050-2273 |
5.66e-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: 5.66e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2129
Cdd:cd03263 1 LQIRNLTKTYKK---GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDlIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2273
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
989-1208 |
4.23e-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: 4.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC 1068
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1149 TAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLK 1208
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2050-2276 |
1.76e-85 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 279.64 E-value: 1.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2129
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRF 2276
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
991-1204 |
7.56e-85 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 278.10 E-value: 7.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1070
Cdd:COG1131 3 VRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1151 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:COG1131 161 GLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2050-2273 |
2.59e-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: 2.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2129
Cdd:cd03265 1 IEVENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2273
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
2057-2360 |
5.09e-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: 5.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2057 KVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFD 2136
Cdd:TIGR01188 1 KVY-----GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2137 ALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2216
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2217 DPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYmITVRTKSSQNVKDVV 2296
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEV 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2297 RFFNRNFPEAMLkERHHTKVQYQLKSEHISLAQvfskmEQVVGVLG--------IEDYSVSQTTLDNVFVNF 2360
Cdd:TIGR01188 235 SMLIAELGETGL-GLLAVTVDSDRIKILVPDGD-----ETVPEIVEaairngirIRSISTERPSLDDVFLKL 300
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
991-1199 |
4.23e-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: 4.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1070
Cdd:COG4555 4 VENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1151 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLK 1199
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
991-1208 |
1.09e-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: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1070
Cdd:cd03265 3 VENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1151 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLK 1208
Cdd:cd03265 161 GLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
991-1198 |
1.15e-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: 1.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1070
Cdd:cd03230 3 VRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLwfysrlksmaqeeirketdkmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110225379 1151 GVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03230 125 GLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
996-1320 |
4.07e-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: 4.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 996 KVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLF 1075
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1155
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1156 ARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGAYGDgyRLTLVKQPAEPGTSQEPGL 1234
Cdd:TIGR01188 159 TRRAIWDYIRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGK--DTLESRPRDIQSLKVEVSM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1235 ASSPSGCPRLSSCSEPQVSQFIRkhvassLLVSDTSTELSYILpSEAVKKGaferlfqqlehsldaLHLSSFGLMDTTLE 1314
Cdd:TIGR01188 237 LIAELGETGLGLLAVTVDSDRIK------ILVPDGDETVPEIV-EAAIRNG---------------IRIRSISTERPSLD 294
|
....*.
gi 110225379 1315 EVFLKV 1320
Cdd:TIGR01188 295 DVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2050-2263 |
6.76e-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: 6.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2129
Cdd:cd03230 1 IEVRNLSKRYGKKT-----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQlytrlrgipwkdeaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2049-2278 |
1.66e-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: 1.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQS 2128
Cdd:COG4555 1 MIEVENLSKKYGKVP-----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2209 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGD 2278
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
991-1202 |
6.12e-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: 6.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLyENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1070
Cdd:cd03264 3 LENLTKRYG--KKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1151 GVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1202
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 ... |
2049-2267 |
2.47e-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: 2.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQS 2128
Cdd:cd03266 1 MITADALTKRFRDVK-KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2209 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2267
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
991-1324 |
7.30e-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: 7.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemDEIRKNLGMCPQ 1070
Cdd:COG4152 4 LKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1151 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGAYGdGYRLTLVKQPAEPGTS 1229
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEADGDAGWLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1230 QEPGLASspsgcprlsscsepqvsqfirkhvassllVSDTSTELSYILPSEAVKkgafERLFQQLehsLDALHLSSFGLM 1309
Cdd:COG4152 238 ALPGVTV-----------------------------VEEDGDGAELKLEDGADA----QELLRAL---LARGPVREFEEV 281
|
330
....*....|....*
gi 110225379 1310 DTTLEEVFLKVSEED 1324
Cdd:COG4152 282 RPSLNEIFIEVVGEK 296
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2049-2366 |
1.44e-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: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllqVQQS 2128
Cdd:COG4152 1 MLELKGLTKRFGDKT-----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKD-EAQVVKWaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2207
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEaKRRADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2208 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGdGYMITVRTK 2287
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEAD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2288 SSQNvkdvvrfFNRNFPEAMLKERHHTKVQYQLKSEHiSLAQVFSkmeQVVGVLGIEDYSVSQTTLDNVFVNFAKKQSD 2366
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 ... |
2050-2264 |
1.17e-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: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQsL 2129
Cdd:cd03268 1 LKTNDLTKTYGKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVvkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2264
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2050-2264 |
1.12e-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: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKigrilAVDRLCLGVRPGeCFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2129
Cdd:cd03264 1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2210 DEPTTGMDPKAR-RFLwNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2264
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 ... |
991-1197 |
1.40e-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: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGMCP 1069
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1149 TAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
991-1204 |
4.73e-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: 4.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYkNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCP 1069
Cdd:COG1122 3 LENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QH--NVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:COG1122 82 QNpdDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1148 PTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2050-2262 |
3.30e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 172.68 E-value: 3.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSL 2129
Cdd:PRK13537 8 IDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2049-2243 |
1.79e-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: 166.50 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQS 2128
Cdd:COG4133 2 MLEAENLSCRRGERLL-----FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAqvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 110225379 2209 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2243
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2050-2267 |
3.54e-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: 3.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllqVQQSL 2129
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2267
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
994-1198 |
8.05e-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: 8.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 994 LTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNV 1073
Cdd:cd03268 6 LTKTYG--KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1074 LFDRLTVEEHLWFYSRLKSMAQEEIrketDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110225379 1154 PYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
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 ... |
991-1198 |
2.12e-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: 2.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKK--MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC 1068
Cdd:cd03266 4 ADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1149 TAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
991-1197 |
8.28e-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: 8.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemDEIRKNLGMCPQ 1070
Cdd:cd03269 3 VENVTKRFG--RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225379 1151 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2049-2262 |
1.26e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 163.46 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIE--NLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQ 2126
Cdd:PRK13536 39 TVAIDlaGVSKSYGDKAV-----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2206
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2207 IFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
988-1204 |
2.21e-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: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 988 VVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRK 1063
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1064 NLGMCPQHNVLFDRLTVEEHLWFYSR-LKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA 1142
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR--VALA-----RA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1143 IIL-------DEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:COG1127 156 LALdpeillyDEPTAGLDPITSAVIDELIreLRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
991-1204 |
2.64e-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: 155.74 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLG 1066
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1067 MCPQHNVLFDRLTVEEHLWFYSRLKS-MAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRAIIL 1145
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKR--VALA-----RALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1146 -------DEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:cd03261 154 dpelllyDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1006-1150 |
1.86e-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: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-RKNLGMCPQHNVLFDRLTVEEHL 1084
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1085 WFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
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 ... |
991-1194 |
4.49e-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: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVY--KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdirTEMDEIRKNLGMC 1068
Cdd:cd03293 3 VRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225379 1149 TAGVDPYARRAIWDLILK--YKPGRTILLSTHHMDEADLLGDRIAIIS 1194
Cdd:cd03293 159 FSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2050-2268 |
1.56e-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: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLL--QVQQ 2127
Cdd:cd03218 1 LRAENLSKRYGKRKV-----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 SLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2207
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2208 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
991-1198 |
3.03e-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: 146.13 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1070
Cdd:cd03259 3 LKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1151 GVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
991-1204 |
8.01e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 148.41 E-value: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1070
Cdd:PRK13537 10 FRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1151 GVDPYARRAIWD-LILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13537 168 GLDPQARHLMWErLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
991-1204 |
1.19e-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: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDE-IRKNLGMC 1068
Cdd:TIGR04406 4 AENLIKSYK--KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlPMHErARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLW-FYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1148 PTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
991-1190 |
3.29e-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: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1070
Cdd:COG4133 5 AENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRkeTDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110225379 1151 GVDPYARRAIWDLILKYKP-GRTILLSTHhmDEADLLGDRI 1190
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 ... |
1005-1204 |
3.70e-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: 143.73 E-value: 3.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1082
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHEIaRLGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 ------------HLWFYSRLKSMAqeEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03219 95 nvmvaaqartgsGLLLARARREER--EARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1151 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:cd03219 173 GLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
991-1204 |
6.43e-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: 6.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEiRKNLGMC- 1068
Cdd:cd03218 3 AENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK-RARLGIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 -PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:cd03218 80 lPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1148 PTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIkiLKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
994-1204 |
6.82e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.51 E-value: 6.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 994 LTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNV 1073
Cdd:PRK13536 47 VSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1074 LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1154 PYARRAIWD----LILKykpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
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 ... |
2051-2274 |
1.04e-37 |
|
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: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQQS 2128
Cdd:cd03219 2 EVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQL-------YTRLRGIPWKDEAQVVKWA---LEKLELTKYADKPAGTYSGGNKRKLSTAI 2198
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVMVaaqartgSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2199 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2274
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2050-2263 |
1.95e-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: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLkDLLQVQQSL 2129
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQReLGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
990-1197 |
1.99e-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: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 990 CVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGMC 1068
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQhnvlfdrltveehlwfysrlksmaqeeirketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1149 TAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:cd00267 108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2050-2268 |
2.13e-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: 141.32 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL-KDLLQVQQS 2128
Cdd:COG1122 1 IELENLSFSYP----GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQF--DALFDElTAREHLQLYTRLRGIPwKDEA-QVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:COG1122 77 VGLVFQNpdDQLFAP-TVEEDVAFGPENLGLP-REEIrERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2206 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
983-1196 |
7.77e-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: 7.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 983 THLPLVVCVDKLTKVY--KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemdE 1060
Cdd:COG1116 2 SAAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1061 IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1140
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1141 RAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1196
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
991-1198 |
8.98e-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: 8.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIR-K 1063
Cdd:cd03255 3 LKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFRrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1064 NLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1143
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 1144 ILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1198
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 ... |
2051-2262 |
1.01e-36 |
|
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: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSL 2129
Cdd:cd03225 1 ELKNLSFSYPDGAR---PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:cd03225 78 GLVFQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2209 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2049-2356 |
1.11e-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: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYK----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAF 2112
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2113 VNGHSVLKD---LL--------QVQQslgycpqfdaLFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADK 2181
Cdd:COG4586 81 VLGYVPFKRrkeFArrigvvfgQRSQ----------LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2182 PAgtysggnkRKLS--------TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALC 2252
Cdd:COG4586 151 PV--------RQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2253 TRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQNVKDVVRFfnrnfpeAMLKERHHTKVQYQLKSEhISLAQVFS 2332
Cdd:COG4586 223 DRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRG-------GEVIEREGNRVRLEVDPR-ESLAEVLA 294
|
330 340
....*....|....*....|....
gi 110225379 2333 KmeqVVGVLGIEDYSVSQTTLDNV 2356
Cdd:COG4586 295 R---LLARYPVRDLTIEEPPIEEV 315
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1005-1204 |
3.31e-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: 3.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKnLGMCP--QHNVLFDRLTVE 1081
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItGLPPHRIAR-LGIARtfQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1082 EHL-----------WFYS--RLKSMAQEE--IRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:COG0411 98 ENVlvaaharlgrgLLAAllRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1147 EPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2045-2271 |
4.46e-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: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2045 ADNDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ 2124
Cdd:COG1121 2 MMMPAIELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VqqslGYCPQ---FDALFdELTARE----HLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA 2197
Cdd:COG1121 77 I----GYVPQraeVDWDF-PITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2198 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLaIMVNGRLRCLGSIQH 2271
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
992-1204 |
5.48e-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: 5.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 992 DKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMD--EIRKNLGMCP 1069
Cdd:cd03295 4 ENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-EQDpvELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIE--DLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1148 PTAGVDPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1727-1974 |
1.35e-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: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1727 AQVLYNNKGYHSMPTYLNSLNNaILRANLPKSKGNPAAYGITVTNHPMNKTSASLSLDYLLQgtdVVIAIFIIVAMSFVP 1806
Cdd:pfam12698 101 VTVYINSSNLLVSKLILNALQS-LLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAY---YLVGLILMIIILIGA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1807 ASFVVFLVAEKSTKAKHLQFVSGCNPVIYWLANYVWDMLNYLVPATCCVIILFVFDLPaytsPTNFPAVLSLFLLYGWSI 1886
Cdd:pfam12698 177 AIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIP----FGNLGLLLLLFLLYGLAY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1887 TPIMYPASFWFEVPSSAYVFLIVINLFIGItATVATFLLQLFehdkdlkvvNSYLKSCFLIFPNYNLGHGLMEMAYNEYI 1966
Cdd:pfam12698 253 IALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDP---------PSFLQWIFSIIPFFSPIDGLLRLIYGDSL 322
|
....*...
gi 110225379 1967 NEYYAKIG 1974
Cdd:pfam12698 323 WEIAPSLI 330
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
991-1204 |
2.22e-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: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTE--MDE-IRKNLGM 1067
Cdd:COG1137 6 AENLVKSYG--KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THlpMHKrARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1148 PTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMDEAdlLG--DRIAIISHGKLKCCGSP 1204
Cdd:COG1137 163 PFAGVDPIAVADIQKIIrhLKER-GIGVLITDHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1005-1197 |
2.29e-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: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1082
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHERaRAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLwfysRLKSMAQ-EEIRKETDKMIEDL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1159
Cdd:cd03224 95 NL----LLGAYARrRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 110225379 1160 IWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:cd03224 171 IFEAIRELRDeGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
989-1197 |
2.29e-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: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGM 1067
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQHNVLFDRlTVEEHLwfysrlksmaqeeirketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1148 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGK 1197
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2049-2263 |
2.79e-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: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdlLQV--- 2125
Cdd:COG1137 3 TLEAENLVKSYGKRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH--LPMhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 -QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2204
Cdd:COG1137 76 aRLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2205 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
991-1204 |
4.34e-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: 135.56 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMD--EIRKNLGMC 1068
Cdd:COG1120 4 AENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSrrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEE--------HLwfySRLKSMAQEEIRKeTDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1140
Cdd:COG1120 81 PQEPPAPFGLTVRElvalgrypHL---GLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1141 RAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
966-1204 |
8.16e-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: 8.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 966 AMESRHFEETRGMEEEPTHLPLVVcVDKLTKVY---KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP 1042
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPLLE-VRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1043 TSGSATIYGHDIRT----EMDEIRKNLGMCPQH--NVLFDRLTVEEHLWF-YSRLKSMAQEEIRKETDKMIEDLELSNK- 1114
Cdd:COG1123 318 TSGSILFDGKDLTKlsrrSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPPDl 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1115 RHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAI 1192
Cdd:COG1123 398 ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYIADRVAV 477
|
250
....*....|..
gi 110225379 1193 ISHGKLKCCGSP 1204
Cdd:COG1123 478 MYDGRIVEDGPT 489
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
994-1199 |
2.15e-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: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 994 LTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHD-IRTEMdeirKNLGMCPQHN 1072
Cdd:TIGR03740 6 LSKRFG--KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKDL----HKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1073 VLFDRLTVEEHLWFYSRLKSMAQEEIrketDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1152
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225379 1153 DPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1199
Cdd:TIGR03740 156 DPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2051-2262 |
2.73e-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: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSL 2129
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLT-----LKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFdalfdeltarehlqlytrlrgipwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd00267 76 GYVPQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1021-1204 |
3.10e-34 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 144.11 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1021 FLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtEMD----EIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQE 1096
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ----PVDagdiATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1097 EIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTIL 1174
Cdd:NF033858 373 EIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLieLSREDGVTIF 452
|
170 180 190
....*....|....*....|....*....|
gi 110225379 1175 LSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1204
Cdd:NF033858 453 ISTHFMNEA-ERCDRISLMHAGRVLASDTP 481
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
978-1204 |
4.23e-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: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 978 MEEEPthlplVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE 1057
Cdd:COG1121 1 MMMMP-----AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1058 mdeiRKNLGMCPQHnVLFDR---LTVEE--------HLWFYSRLKSmaqeEIRKETDKMIEDLELSNKRHSLVQTLSGGM 1126
Cdd:COG1121 74 ----RRRIGYVPQR-AEVDWdfpITVRDvvlmgrygRRGLFRRPSR----ADREAVDEALERVGLEDLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1127 KRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLkCCGSP 1204
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPP 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
991-1198 |
4.33e-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: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKN 1064
Cdd:cd03257 4 VKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1065 LGMCPQH--NVLFDRLTVEEHLW--FYSRLKSMAQEEIRKETDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIAFVGG 1139
Cdd:cd03257 84 IQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1140 SRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2051-2274 |
1.91e-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: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLG 2130
Cdd:TIGR04406 3 VAENLIKSYKKRKV-----VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2131 --YCPQFDALFDELTAREHLQLYTRLRGIPWKDE-AQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2207
Cdd:TIGR04406 78 igYLPQEASIFRKLTVEENIMAVLEIRKDLDRAErEERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2208 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2274
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
991-1205 |
2.70e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.27 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCP 1069
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSN--KRHSlvQTLSGGMKRKlsVAIAFVGG--SRAII 1144
Cdd:PRK13632 90 QNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDylDKEP--QNLSGGQKQR--VAIASVLAlnPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1145 LDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPL 1205
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 ... |
991-1198 |
3.55e-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: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKN 1064
Cdd:cd03258 4 LKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1065 LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAII 1144
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1145 LDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
986-1198 |
3.60e-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: 3.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 986 PLVVCVDkLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMD 1059
Cdd:COG1136 3 PLLELRN-LTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1060 EIR-KNLGMCPQ-HNvLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFV 1137
Cdd:COG1136 82 RLRrRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1138 GGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1198
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
988-1198 |
4.65e-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: 4.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 988 VVCVDKLTKVYKNDKKmALNKLSLNLYENQVVsFL-GHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIR 1062
Cdd:COG2884 1 MIRFENVSKRYPGGRE-ALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1063 KNLGMCPQ-HNVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGG-MKRklsVAIAfvggs 1140
Cdd:COG2884 79 RRIGVVFQdFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGeQQR---VAIA----- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1141 RAI-------ILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:COG2884 150 RALvnrpellLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
988-1204 |
5.99e-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: 5.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 988 VVCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT---SGSATIYGHDIRTEMDEIR-K 1063
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1064 NLGMCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1142
Cdd:COG1123 84 RIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1143 IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2013-2272 |
9.13e-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: 135.80 E-value: 9.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2013 FLRQPQRL---PVSTKPVEDDVDVASERQRVLRgdadndmvkIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVN 2089
Cdd:COG1123 230 ILAAPQALaavPRLGAARGRAAPAAAAAEPLLE---------VRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGES 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2090 GAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQVQQSLGYCPQ--FDALFDELTAREHLQLYTRLRGIPWKDEA 2163
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAER 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2164 -QVVKWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVL 2240
Cdd:COG1123 381 rERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLF 460
|
250 260 270
....*....|....*....|....*....|..
gi 110225379 2241 TSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2272
Cdd:COG1123 461 ISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
991-1197 |
1.00e-32 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 126.15 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI---RKNLGM 1067
Cdd:cd03229 3 LKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQHNVLFDRLTVEEHLWFysrlksmaqeeirketdkmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1148 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2050-2263 |
2.79e-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: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK------DLL 2123
Cdd:cd03255 1 IELKNLSKTYGGGGE-KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQQsLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:cd03255 80 RRRH-IGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEEcEALCTRLAIMVNGRL 2263
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2051-2263 |
4.23e-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: 4.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSL 2129
Cdd:COG4619 2 ELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDElTAREHLQLYTRLRGIPWkDEAQVVKWaLEKLELTK-YADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKF-DRERALEL-LERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2209 LDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2049-2263 |
5.97e-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: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdlLQVQQ- 2127
Cdd:COG0411 4 LLEVRGLTKRF-----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 -SLG----YcpQFDALFDELTAREHLQL--YTRLRGIPW----------KDEAQVVKWA---LEKLELTKYADKPAGTYS 2187
Cdd:COG0411 77 aRLGiartF--QNPRLFPELTVLENVLVaaHARLGRGLLaallrlprarREEREARERAeelLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2188 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2049-2268 |
9.68e-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: 125.93 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQ 2127
Cdd:COG1120 1 MLEAENLSVGYGGRPV-----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 SLGYCPQFDALFDELTARE--------HLQLYTRLRgipwKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2199
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRElvalgrypHLGLFGRPS----AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2200 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2051-2267 |
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 110225379 2051 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQVQQSLG 2130
Cdd:cd03235 1 EVEDLTVSYGGHPV-----LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2131 YCPQ---FDALFdELTARE--HLQLYTRLRGIPW--KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:cd03235 72 YVPQrrsIDRDF-PISVRDvvLMGLYGHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRlAIMVNGRLRCLG 2267
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2045-2274 |
1.86e-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: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2045 ADNDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----K 2120
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVV-----LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2121 DLLQVQQSLGYCPQFDALFDELTAREHLQL----YTRLrgipwkDEAQVVKWALEKLE---LTKYADKPAGTYSGGNKRK 2193
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFDSLTVFENVAFplreHTDL------SEAEIRELVLEKLElvgLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2194 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2272
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
..
gi 110225379 2273 KN 2274
Cdd:COG1127 230 LA 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
2070-2214 |
2.60e-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: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2070 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKD-LLQVQQSLGYCPQFDALFDELTAREHL 2148
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2149 QLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAG----TYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2214
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
991-1197 |
3.59e-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: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIRKNLG 1066
Cdd:cd03256 3 VENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1067 MCPQHNVLFDRLTVEEH-----LWFYSRLKSMAQEEIRKETDKMIEDLE---LSNKRHSLVQTLSGGMKRKLSVAIAFVG 1138
Cdd:cd03256 82 MIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1139 GSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
991-1198 |
4.75e-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: 4.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVY-------------------KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG 1051
Cdd:cd03267 3 VSNLSKSYrvyskepgligslkslfkrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1052 HDIRTEMDEIRKNLG-MCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKL 1130
Cdd:cd03267 83 LVPWKRRKKFLRRIGvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1131 SVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
998-1202 |
5.38e-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: 5.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTeMD--EIRKNLGMCPQhnvlf 1075
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-LSpkELARKIAYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 drltveehlwfysrlksmaqeeirketdkMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1155
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110225379 1156 ARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1202
Cdd:cd03214 132 HQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
998-1198 |
6.59e-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: 6.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKNLGMCPQHNVLF 1075
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPppEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DRlTVEEHL--WFYSRLKSMAQEEIRKetdkMIEDLELS----NKRhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:COG4619 87 GG-TVRDNLpfPFQLRERKFDRERALE----LLERLGLPpdilDKP---VERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1150 AGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:COG4619 159 SALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
979-1217 |
9.44e-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: 130.27 E-value: 9.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 979 EEEPTHLPLVVCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-E 1057
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1058 MDEIRKNLGMCPQHNVLFDRlTVEEHLwfysRL-KSMAQEEirketdKMIEDLE----------LSNKRHSLV----QTL 1122
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDT-TLRENL----RLaRPDATDE------ELWAALErvglgdwlaaLPDGLDTWLgeggRRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1123 SGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCG 1202
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQG 551
|
250
....*....|....*
gi 110225379 1203 SPLFLKGAYGDGYRL 1217
Cdd:COG4987 552 THEELLAQNGRYRQL 566
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
991-1196 |
1.13e-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: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEmdeiRKNLGMCPQ 1070
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 H-NVLFD-RLTVEE--------HLWFYSRLKsmaqEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1140
Cdd:cd03235 76 RrSIDRDfPISVRDvvlmglygHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1141 RAIILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIA-----IISHG 1196
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLllnrtVVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2050-2274 |
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 110225379 2050 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQV 2125
Cdd:cd03261 1 IELRGLTKSFGGRTV-----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQFDALFDELTAREHLQL----YTRLrgipwkDEAQVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAI 2198
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFplreHTRL------SEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2199 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2274
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2049-2272 |
2.87e-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: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQ 2124
Cdd:cd03258 1 MIELKNVSKVFGDTG-GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPwkdEAQVVKWALEKLELTKYADKpAGTY----SGGNKRKLSTAIAL 2200
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVP---KAEIEERVLELLELVGLEDK-ADAYpaqlSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2201 IGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2272
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
991-1204 |
3.88e-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: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1070
Cdd:cd03300 3 LENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1151 GVDPYARRaiwDLILKYKP-----GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:cd03300 160 ALDLKLRK---DMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2050-2263 |
6.34e-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: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYK----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFV 2113
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2114 NGhsvlkdLLQVQQSLGYCPQFDALFDE-------LTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTY 2186
Cdd:cd03267 81 AG------LVPWKRRKKFLRRIGVVFGQktqlwwdLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2187 SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
991-1204 |
7.54e-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: 7.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKkmaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1070
Cdd:cd03299 3 VENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1151 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:cd03299 159 ALDVRTKEKLREELkkIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
991-1198 |
9.97e-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: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKK-------------------MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG 1051
Cdd:COG4586 4 VENLSKTYRVYEKepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1052 HDIRTEMDEIRKNLGmcpqhnVLF--------DrLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLS 1123
Cdd:COG4586 84 YVPFKRRKEFARRIG------VVFgqrsqlwwD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 1124 GGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
991-1204 |
3.27e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKND---KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKN 1064
Cdd:PRK13637 5 IENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1065 LGMC---PQHNvLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSN---KRHSLVQtLSGGMKRKLSVAIAFVG 1138
Cdd:PRK13637 85 VGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedyKDKSPFE-LSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1139 GSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
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 ... |
2051-2274 |
3.45e-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: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQQS 2128
Cdd:cd03224 2 EVENLNAGY-----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQLYTRLRGIpwkdeaQVVKWALEKL-----ELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRR------AKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2274
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2050-2258 |
3.98e-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: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQVQQSL 2129
Cdd:cd03293 1 LEVRNVSKTYGGGG-GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIM 2258
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2049-2280 |
4.13e-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: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLL- 2123
Cdd:COG1124 1 MLEVRNLSVSYGQGG-RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrrrRKAFRr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQqslgYCPQ--FDALFDELTAREHLQLYTRLRGIPwKDEAQVVKwALEKLELTK-YADKPAGTYSGGNKRKLSTAIAL 2200
Cdd:COG1124 80 RVQ----MVFQdpYASLHPRHTVDRILAEPLRIHGLP-DREERIAE-LLEQVGLPPsFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2201 IGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDG 2279
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
.
gi 110225379 2280 Y 2280
Cdd:COG1124 234 Y 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1005-1204 |
4.73e-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: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIR-KNLGMCPQHNVLFDRLT 1079
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRrKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1080 VEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1159
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110225379 1160 IWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:cd03294 199 MQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2042-2262 |
4.87e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 127.16 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2042 RGDADNDMVKIE--NLTkvyksRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL 2119
Cdd:NF033858 257 RPADDDDEPAIEarGLT-----MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2120 KDLLQVQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2199
Cdd:NF033858 332 AGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2200 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEaLCTRLAIMVNGR 2262
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
992-1217 |
5.71e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.69 E-value: 5.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 992 DKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCP 1069
Cdd:PRK10895 7 KNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKE-TDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 1149 TAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL------KGAY-GDGYRL 1217
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlqdehvKRVYlGEDFRL 241
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2049-2263 |
6.42e-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: 6.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdLLQVQQS 2128
Cdd:cd03257 1 LLEVKNLSVSFPTGG-GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK-LSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 L-----GYCPQ--FDALFDELTAREHLQLYTRLRGIPWKDEAQ--VVKWALEKLELTK-YADKPAGTYSGGNKRKLSTAI 2198
Cdd:cd03257 79 IrrkeiQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARkeAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2199 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
997-1198 |
3.82e-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: 114.59 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 997 VYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP-----PTSGSATIYGHDIRTEMD---EIRKNLGMC 1068
Cdd:cd03260 8 VYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVdvlELRRRVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFdRLTVEEHLWFYSRLKSMAQeeiRKETDKMIEDL--------ELSNKRHSLvqTLSGGMKRKLSVAIAFVGGS 1140
Cdd:cd03260 87 FQKPNPF-PGSIYDNVAYGLRLHGIKL---KEELDERVEEAlrkaalwdEVKDRLHAL--GLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1141 RAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
967-1204 |
4.15e-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: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 967 MESRHFEETRGMEEEPTHLPLVVCVDKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGS 1046
Cdd:COG4988 315 LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1047 ATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDrLTVEEHLWFYSRLKSMAQ-EEIRKET--DKMIEDLElsNKRHSLV--- 1119
Cdd:COG4988 394 ILINGVDLSDlDPASWRRQIAWVPQNPYLFA-GTIRENLRLGRPDASDEElEAALEAAglDEFVAALP--DGLDTPLgeg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1120 -QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1198
Cdd:COG4988 471 gRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRI 549
|
....*.
gi 110225379 1199 KCCGSP 1204
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 ... |
991-1199 |
4.77e-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: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKnDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEmdEIRKNLGMCPQ 1070
Cdd:cd03226 2 IENISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 ---HNVLFDrlTVEEHLWFYSRLKSMAQEEIRKetdkMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:cd03226 79 dvdYQLFTD--SVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1148 PTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1199
Cdd:cd03226 153 PTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2047-2263 |
4.93e-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: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDL 2122
Cdd:COG1136 2 SPLLELRNLTKSYGTGE-GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2123 LQV-QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2201
Cdd:COG1136 81 ARLrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2202 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSmEECEALCTRLAIMVNGRL 2263
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1005-1197 |
5.42e-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: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1082
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHRIaRLGIGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HL--WFYSRLKSMAQEEIRKEtdkmIEDL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1158
Cdd:COG0410 98 NLllGAYARRDRAEVRADLER----VYELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110225379 1159 AIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:COG0410 174 EIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2049-2272 |
7.34e-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: 7.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKDLLQV 2125
Cdd:COG1123 4 LLEVRDLSVRYPG---GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 Q-QSLGYCPQ-FDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:COG1123 81 RgRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2272
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
998-1204 |
1.60e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.80 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDK----KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD--EIRKNLGMCPQH 1071
Cdd:PRK13633 14 YESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 --NVLFDRLtVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSR--AIILDE 1147
Cdd:PRK13633 94 pdNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR--VAIAGILAMRpeCIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1148 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
997-1182 |
3.43e-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: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 997 VYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSG-SATIYGHDI-RTEMDEIRKNLGMCpqHNVL 1074
Cdd:COG1119 11 VRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLV--SPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1075 FDRLTVEEHLW------FYSrlkSM-----AQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1143
Cdd:COG1119 88 QLRFPRDETVLdvvlsgFFD---SIglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110225379 1144 ILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDE 1182
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2049-2262 |
3.98e-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: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLlq 2124
Cdd:COG0410 3 MLEVENLHAGY-----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQFDALFDELTAREHLQLYTRLRgipwKDEAQVvKWALEKL-----ELTKYADKPAGTYSGGNKRKLSTAIA 2199
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSLTVEENLLLGAYAR----RDRAEV-RADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2200 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2050-2268 |
4.03e-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: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQS 2128
Cdd:cd03295 1 IEFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQLYTRLRGipWKdEAQVVKWALEKLEL-----TKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLK--WP-KEKIRERADELLALvgldpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
993-1198 |
6.36e-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: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 993 KLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMC 1068
Cdd:cd03292 5 NVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1149 TAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
989-1198 |
1.00e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 110.04 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMC 1068
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1149 TAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03301 158 LSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
989-1198 |
1.11e-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: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGM 1067
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQHNVLFDRlTVEEHLWFYSRLKSMaqEEIRK-----ETDKMIEdlELSNKRHSLV----QTLSGGMKRKLSVAIAFVG 1138
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGDPDATD--EEIIEaarlaGLHDFIE--ALPMGYDTVVgeggSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1139 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLgDRIAIISHGKL 1198
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2053-2268 |
1.84e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 110.37 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2053 ENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH--SVLKDLLQVQQSLG 2130
Cdd:PRK10895 7 KNLAKAYKGRRV-----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2131 YCPQFDALFDELTAREHLQLYTRLR-GIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2051-2267 |
1.96e-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: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSL 2129
Cdd:cd03214 1 EVENLSVGYGGRTV-----LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQfdalfdeltarehlqlytrlrgipwkdeaqvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03214 76 AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2267
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2050-2276 |
4.14e-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: 108.86 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLkDLLQVQQSL 2129
Cdd:cd03300 1 IELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2210 DEPTTGMDPKARRflwNLILDLI----KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRF 2276
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 ... |
2052-2261 |
5.32e-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: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2052 IENLTkvYKSRKIGRILAVDRLCLgvRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLlqvQQSLG 2130
Cdd:cd03226 2 IENIS--FSYKKGTEILDDLSLDL--YAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKER---RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2131 YCPQ--FDALFDELTAREhlqLYTRLRGIPwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:cd03226 75 YVMQdvDYQLFTDSVREE---LLLGLKELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2209 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2261
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
998-1183 |
6.01e-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: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMCPQH--N 1072
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1073 VLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1152
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 110225379 1153 DPYARRAIWDLILKYKP-GRTILLSTHHMDEA 1183
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAeGMTVVISTHDVDLA 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
999-1202 |
6.34e-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: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 999 KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIRTemDEIRKNLGMCPQHNVLF 1075
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP--DQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DRLTVEEHLWFYSRLKS---MAQEEIRKETDKM-IEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1151
Cdd:cd03234 94 PGLTVRETLTYTAILRLprkSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1152 VDP------------YARRaiwdlilkykpGRTILLSTHHmDEADL--LGDRIAIISHGKLKCCG 1202
Cdd:cd03234 174 LDSftalnlvstlsqLARR-----------NRIVILTIHQ-PRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
989-1205 |
6.82e-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: 6.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMC 1068
Cdd:COG3839 4 LELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRAII---- 1144
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR--VALG-----RALVrepk 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1145 ---LDEPTAGVDP----YARRAIWDLILKYkpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPL 1205
Cdd:COG3839 154 vflLDEPLSNLDAklrvEMRAEIKRLHRRL--GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2062-2296 |
6.91e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 111.75 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2062 RKIGRILAVDRLCLGVRPGECFGLLGVNGAG--KTSTFKMLTGDESTTGGEAFVNGHSVLKDLlqvQQSLG-YCPQFDAL 2138
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRAL---RRTIG*HRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2139 FDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2218
Cdd:NF000106 98 RESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2219 KARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGdGYMITVRTKSSQNVKDVV 2296
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPAHAAELDRMV 254
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2077-2263 |
7.98e-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: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKDllQVQQSLGYCPQFDALFDELTAREHLQLYTR 2153
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2154 LRGIPWKDEAQVVKWAlEKLELTKYADKPAGTY-----SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPkarrFLWNLI 2228
Cdd:cd03234 108 LRLPRKSSDAIRKKRV-EDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110225379 2229 L----DLIKTGRSVVLTSHS-MEECEALCTRLAIMVNGRL 2263
Cdd:cd03234 183 VstlsQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
998-1198 |
1.32e-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: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLF- 1075
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 ----DRLTV------EEHLWFYSRLkSMAQEEIRKETDKMieDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIIL 1145
Cdd:cd03245 92 gtlrDNITLgapladDERILRAAEL-AGVTDFVNKHPNGL--DLQIGERG----RGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1146 DEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLgDRIAIISHGKL 1198
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2047-2269 |
2.66e-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: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYK-----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGG 2109
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2110 EAFVNGH-SVLKDLlqvqqSLGycpqFDAlfdELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSG 2188
Cdd:COG1134 82 RVEVNGRvSALLEL-----GAG----FHP---ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2189 GNKRKLSTAIALIGYPAFIFLDEPTTGMDP----KARRFlwnlILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2264
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLAR----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
....*
gi 110225379 2265 CLGSI 2269
Cdd:COG1134 226 MDGDP 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
986-1198 |
2.79e-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: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 986 PLVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRK 1063
Cdd:COG3845 3 PPALELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1064 NLGMCPQHNVLFDRLTVEEHL---------WFYSRlksmaqEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAI 1134
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIvlgleptkgGRLDR------KAARARIRELSERYGLDVDPDAKVEDLSVGEQQR--VEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1135 --AFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:COG3845 153 lkALYRGARILILDEPTAVLTPQEADELFEILrrLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2049-2263 |
2.91e-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: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQV--- 2125
Cdd:COG3842 5 ALELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNK-RklsTAIA--LIG 2202
Cdd:COG3842 76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VALAraLAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2203 YPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQReLGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2050-2267 |
3.50e-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: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK------DLL 2123
Cdd:cd03301 1 VELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQQSLgycpqfdALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:cd03301 76 MVFQNY-------ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2267
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1002-1198 |
5.67e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 107.22 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1002 KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-----MDEIRKNLGMCPQ--HNVL 1074
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1075 FDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNK--RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1152
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDliSKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110225379 1153 DPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK13641 177 DPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2053-2263 |
1.19e-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: 103.40 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2053 ENLTK-VYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVlkDLLQVQQSL 2129
Cdd:cd03213 7 RNLTVtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL--DKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIpwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03213 85 GYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHS-MEECEALCTRLAIMVNGRL 2263
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
991-1198 |
1.60e-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: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKK--MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE-----IRK 1063
Cdd:COG1135 4 LENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSErelraARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1064 NLGMCPQH-NvLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA 1142
Cdd:COG1135 83 KIGMIFQHfN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR--VGIA-----RA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1143 I-----IL--DEPTAGVDPYARRAIWDLILK--YKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:COG1135 155 LannpkVLlcDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1003-1210 |
1.73e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.87 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1003 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDE-----IRKNLGMC---PQHNvL 1074
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkpLRKKVGIVfqfPEHQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1075 FDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSnkrHSLVQ----TLSGG-MKRklsVAIAFVGG--SRAIILDE 1147
Cdd:PRK13634 99 FEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP---EELLArspfELSGGqMRR---VAIAGVLAmePEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 1148 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGA 1210
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPreIFADPD 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
991-1198 |
1.99e-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: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGM 1067
Cdd:cd03262 3 IKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQHNVLFDRLTVEEHLWFYSR-LKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA---- 1142
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQR--VAIA-----RAlamn 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1143 ---IILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03262 154 pkvMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
988-1204 |
2.74e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 988 VVCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLG 1066
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1067 MCPQH-NVLFDRLTVEEHLWFysrlksmAQEEIRKETDKMIEDLELSNKRHSLVQ-------TLSGGMKRKlsVAIAFVG 1138
Cdd:PRK13635 85 MVFQNpDNQFVGATVQDDVAF-------GLENIGVPREEMVERVDQALRQVGMEDflnrephRLSGGQKQR--VAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1139 GSRA--IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13635 156 ALQPdiIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
993-1198 |
3.81e-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: 102.57 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 993 KLTKVYKNDKKMALNkLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHN 1072
Cdd:cd03298 2 RLDKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1073 VLFDRLTVEEH--LWFYSRLKSMAQEeiRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03298 80 NLFAHLTVEQNvgLGLSPGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1151 GVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03298 158 ALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
997-1204 |
3.94e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 997 VYK-NDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---TEMDEIRKNLGMCPQH- 1071
Cdd:PRK13639 8 KYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 -NVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:PRK13639 88 dDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1151 GVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2049-2246 |
4.67e-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: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKsrkiGRILAVDRLCLGVRPGE-CFgLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLL 2123
Cdd:COG2884 1 MIRFENVSKRYP----GGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQQSLGYCPQfDA-LFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIG 2202
Cdd:COG2884 76 YLRRRIGVVFQ-DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110225379 2203 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2246
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
987-1207 |
4.75e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 4.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 987 LVVCVDKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNL 1065
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1066 GMCPQ--HNVLFDrLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1143
Cdd:PRK13647 82 GLVFQdpDDQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1144 ILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1207
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2047-2262 |
5.00e-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: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDES-TTGGEAFVNGHSVLK-DLLQ 2124
Cdd:COG1119 1 DPLLELRNVTVRRGGKTI-----LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRGGeDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYC-PQFDALFDE-LTARE--------HLQLYtrlRGIPWKDEAQVVKWaLEKLELTKYADKPAGTYSGGNKRKL 2194
Cdd:COG1119 76 LRKRIGLVsPALQLRFPRdETVLDvvlsgffdSIGLY---REPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2195 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTG-RSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
998-1204 |
5.39e-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: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1076
Cdd:COG1132 349 YPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 RlTVEEHLwFYSRLKSmAQEEIRK-----ETDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:COG1132 428 G-TIRENI-RYGRPDA-TDEEVEEaakaaQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1148 PTAGVDPYARRAIWDLILKYKPGRTILLSTH------HMdeadllgDRIAIISHGKLKCCGSP 1204
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA-------DRILVLDDGRIVEQGTH 558
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
991-1204 |
5.85e-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: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1070
Cdd:cd03296 5 VRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSMAQE----EIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1147 EPTAGVDPYARRAI--WDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:cd03296 162 EPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
991-1198 |
5.86e-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: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVY--KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGM 1067
Cdd:COG1124 4 VRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQH--NVLFDRLTVEEHLwfySR-LKSMAQEEIRKETDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1143
Cdd:COG1124 84 VFQDpyASLHPRHTVDRIL---AEpLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 1144 ILDEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2050-2267 |
6.53e-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: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRK-----------------IGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAF 2112
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2113 VNGhsvlkdllQVQQSLGycpqFDALFD-ELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNK 2191
Cdd:cd03220 81 VRG--------RVSSLLG----LGGGFNpELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2192 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2267
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2049-2263 |
8.17e-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: 8.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MV--KIENLTKvYKSRKIGR-ILAVDRLCLG---------VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH 2116
Cdd:COG1129 236 MVgrELEDLFP-KRAAAPGEvVLEVEGLSVGgvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2117 SV-LKDLLQ-VQQSLGYCP---QFDALFDELTARE-----HLQLYTRLRGIPWKDEAQVVKWALEKLEL-TKYADKPAGT 2185
Cdd:COG1129 315 PVrIRSPRDaIRAGIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGN 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2186 YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
993-1202 |
8.38e-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: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 993 KLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhDIRTEMDEirkNLGMCPQhn 1072
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGL---GGGFNPE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1073 vlfdrLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKL--SVAIAFvgGSRAIILDEPTA 1150
Cdd:cd03220 99 -----LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1151 GVDPY----ARRAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1202
Cdd:cd03220 172 VGDAAfqekCQRRLRELL---KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2050-2263 |
9.17e-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: 9.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-----DESTTGGEAFVNGHSVLK---D 2121
Cdd:cd03260 1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldvD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2122 LLQVQQSLGYCPQFDALFDeLTAREHLQLYTRLRGIPWKDE-AQVVKWALEKLELTKY-ADKPAGTY-SGGNKRKLSTAI 2198
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEvKDRLHALGlSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2199 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
989-1198 |
9.27e-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: 9.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLG 1066
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1067 MCPQhnvlfdrltveehlwfysrlksmaqeeirketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1147 EPTAGVDPYARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03216 108 EPTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2049-2262 |
9.84e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 9.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLtkvykSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQ 2126
Cdd:PRK11300 5 LLSVSGL-----MMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDALFDELTARE------HLQLYTR-LRGI---PW--KDEAQVVKWA---LEKLELTKYADKPAGTYSGGNK 2191
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIEnllvaqHQQLKTGlFSGLlktPAfrRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2192 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2050-2262 |
1.91e-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: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQ--- 2126
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDALFDELTAREHLQLytrlrgipwkdeaqvvkwALekleltkyadkpagtySGGNKRKLSTAIALIGYPAF 2206
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIAL------------------GL----------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2207 IFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
997-1198 |
3.22e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.39 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 997 VYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTT---TMSILTGLFP--PTSGSATIYGHDI---RTEMDEIRKNLGMC 1068
Cdd:PRK14239 13 VYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTDTVDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDrLTVEEHLWFYSRLKSMAQEEIrkeTDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1140
Cdd:PRK14239 92 FQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1141 RAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1003-1198 |
4.00e-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: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1003 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCP---QHNVLFDR 1077
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 LTVEEHLwfysrlksmaqeeirketdkmiedlelsnkrhSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1157
Cdd:cd03215 93 LSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110225379 1158 RAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03215 141 AEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
994-1198 |
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 110225379 994 LTKVYKNDKK--MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGM 1067
Cdd:PRK11153 7 ISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQH-NVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRAIIL- 1145
Cdd:PRK11153 87 IFQHfNLLSSR-TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR--VAIARALASNPKVLl 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1146 -DEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK11153 164 cDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1001-1204 |
6.37e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.46 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1001 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMCPQH--NVLF 1075
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1155
Cdd:PRK13636 97 SA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1156 ARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13636 176 GVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1005-1193 |
6.92e-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: 6.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG--HDIRTEMDEIRKNLGMCPQHNVLFDRLTVEE 1082
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLWF---YSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGmKRKLsVAI--AFVGGSRAIILDEPTAGVDPYAR 1157
Cdd:COG1129 99 NIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-QQQL-VEIarALSRDARVLILDEPTASLTEREV 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 110225379 1158 RAIWDLI--LKYKpGRTILLSTHHMDEADLLGDRIAII 1193
Cdd:COG1129 177 ERLFRIIrrLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
993-1198 |
1.02e-22 |
|
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: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 993 KLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGL--FPPTSGSATIYGHDIRteMDEIRKNLGMCPQ 1070
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD--KRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSmaqeeirketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03213 90 DDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1151 GVDPYARRAIWDLILKY-KPGRTILLSTHH-MDEADLLGDRIAIISHGKL 1198
Cdd:cd03213 141 GLDSSSALQVMSLLRRLaDTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2050-2270 |
2.13e-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: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKigrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKDLLQVQQSL 2129
Cdd:cd03299 1 LKVENLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKTGRSVVL-TSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2270
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2067-2263 |
3.33e-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: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2067 ILAVDRLCLG---------VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLLQ-VQQSLGYCP-- 2133
Cdd:cd03215 4 VLEVRGLSVKgavrdvsfeVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDaIRAGIAYVPed 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2134 -QFDALFDELTAREHLQLYTRLrgipwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEP 2212
Cdd:cd03215 84 rKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2213 TTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2049-2263 |
3.46e-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: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVL----KDLL 2123
Cdd:COG1135 1 MIELENLSKTFPTKG-GPVTALDDVSLTIEKGEIFGIIGYSGAGK-STLiRCINLLERPTSGSVLVDGVDLTalseRELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPwKDEAQvvKWALEKLELTKYADKpAGTY----SGGNKRKLSTAIA 2199
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVP-KAEIR--KRVAELLELVGLSDK-ADAYpsqlSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2200 LIGYPAFIFLDEPTTGMDPKARRflwnLILDLIK-----TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTR----SILDLLKdinreLGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
994-1235 |
3.92e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.72 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 994 LTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQH- 1071
Cdd:PRK13652 9 LCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVGLVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 -NVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:PRK13652 88 dDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1151 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGAYGDGYRLTLVKQPAEP 1226
Cdd:PRK13652 167 GLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDLPSLPKLI 246
|
....*....
gi 110225379 1227 GTSQEPGLA 1235
Cdd:PRK13652 247 RSLQAQGIA 255
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
991-1197 |
4.34e-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: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVY---KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKN--- 1064
Cdd:COG1101 4 LKNLSKTFnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKRAkyi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1065 --------LGMCPqhnvlfdRLTVEEHL----------WFYSRLKSMAQEEIRKETDKMieDLELSNKRHSLVQTLSGGM 1126
Cdd:COG1101 83 grvfqdpmMGTAP-------SMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLATL--GLGLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 1127 KRKLSVAIAFVGGSRAIILDEPTAGVDPyaRRAiwDLILKY------KPGRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDP--KTA--ALVLELtekiveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
999-1204 |
5.36e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 999 KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMDEIR-KNLGMCPQHNV 1073
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1074 LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1154 PYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK10070 197 PLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
998-1204 |
6.18e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsaTIYGHDIRTEMD---EIRKNLGMCPQH-NV 1073
Cdd:PRK13648 17 YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAITDDnfeKLRKHIGIVFQNpDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1074 LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:PRK13648 95 QFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1154 PYARRAIWDLILKYKPGR--TILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1204
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 ... |
2047-2263 |
6.26e-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: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ-- 2124
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 ------VQQSLGYCPQFDALFDELTAREHLqlyTRLRGIPWKDEAQVVKwALEKLELTKYADKPA--------GTYSGGN 2190
Cdd:TIGR03269 357 pdgrgrAKRYIGILHQEYDLYPHRTVLDNL---TEAIGLELPDELARMK-AVITLKMVGFDEEKAeeildkypDELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2191 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKArEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1005-1204 |
7.31e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 7.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-----EMDEIRKNLGMCPQ--HNVLFDR 1077
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 lTVEEHLWFYSRLKSMAQEEIRKETDkmiEDLELSNKRHSLVQT----LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAR---EKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1154 PYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13649 178 PKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
998-1204 |
8.39e-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: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1076
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 ---RLTV-------EEHLWfySRLKSMAQEEIRKETDKMIEDLELSNKRHslvqtLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:cd03244 92 gtiRSNLdpfgeysDEELW--QALERVGLKEFVESLPGGLDTVVEEGGEN-----LSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1147 EPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDE-ADLlgDRIAIISHGKLKCCGSP 1204
Cdd:cd03244 165 EATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
988-1204 |
8.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 8.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 988 VVCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSA---TIYGHDIRTE-MDEIRK 1063
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNskiTVDGITLTAKtVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1064 NLGMCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1142
Cdd:PRK13640 85 KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1143 IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP 1204
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 ... |
2050-2268 |
1.05e-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: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQvQQSL 2129
Cdd:cd03296 3 IEVRNVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGI---PWKDE-AQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRserPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2206 FIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2072-2243 |
1.29e-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: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2072 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLY 2151
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 TRLRGipwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA-IALIGYPAFIfLDEPTTGMDPKARRFLWNLILD 2230
Cdd:TIGR01189 98 AAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALArLWLSRRPLWI-LDEPTTALDKAGVALLAGLLRA 172
|
170
....*....|...
gi 110225379 2231 LIKTGRSVVLTSH 2243
Cdd:TIGR01189 173 HLARGGIVLLTTH 185
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2050-2263 |
1.30e-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: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSR-------------------KIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2110
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2111 AFVNGHSVL----KDLLQVQ-QSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGT 2185
Cdd:cd03294 81 VLIDGQDIAamsrKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2186 YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1002-1215 |
1.62e-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: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1002 KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE---IRKNLGMCPQHNVLFDRL 1078
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTakiMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1079 TVEEHL----WFYSRlkSMAQEEIRKetdkmIEDL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1152
Cdd:PRK11614 96 TVEENLamggFFAER--DQFQERIKW-----VYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1153 DPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK--LKCCGSPLFLKGAYGDGY 1215
Cdd:PRK11614 169 APIIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDALLANEAVRSAY 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1004-1204 |
1.71e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.21 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1004 MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCP--QHNVLFDRLTVE 1081
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1082 EHL-----------WFYSRLKSMAQEeiRKETDKM---------IEDLELSNKRHSlvqTLSGGMKRKLSVAIAFVGGSR 1141
Cdd:PRK11300 99 ENLlvaqhqqlktgLFSGLLKTPAFR--RAESEALdraatwlerVGLLEHANRQAG---NLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1142 AIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2046-2263 |
2.86e-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: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2046 DNDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSV-LKDLL 2123
Cdd:COG1129 1 AEPLLEMRGISKSF-----GGVKALDGVSLELRPGEVHALLGENGAGK-STLmKILSGVYQPDSGEILLDGEPVrFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 Q--------VQQSLgycpqfdALFDELTAREHL---QLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKR 2192
Cdd:COG1129 75 DaqaagiaiIHQEL-------NLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2193 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1005-1203 |
2.91e-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: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIR-KNLGMC-----PqhNVlFDRL 1078
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDEHEiARLGIGrkfqkP--TV-FEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1079 TVEEHL---------WFysrlKSMAQEEIRKETDKMIEDLE---LSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:COG4674 101 TVFENLelalkgdrgVF----ASLFARLTAEERDRIEEVLEtigLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 1147 EPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS 1203
Cdd:COG4674 177 EPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1000-1211 |
3.39e-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: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1000 NDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1078
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1079 TVEEHLwFYSRLkSMAQEEIRKETDK-MIED--LELSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1151
Cdd:cd03253 90 TIGYNI-RYGRP-DATDEEVIEAAKAaQIHDkiMRFPDGYDTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1152 VDPYARRAIWDLILKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPLFL---KGAY 1211
Cdd:cd03253 168 LDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELlakGGLY 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1005-1179 |
3.57e-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: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEH 1083
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1084 LwfysRL--KSMAQEEIRKETDKM-----IEDLE--LSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1154
Cdd:TIGR02868 429 L----RLarPDATDEELWAALERVgladwLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*
gi 110225379 1155 YARRAIWDLILKYKPGRTILLSTHH 1179
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITHH 529
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2049-2312 |
3.70e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.98 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkDLLQV--- 2125
Cdd:PRK11607 19 LLEIRNLTKSFDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV----DLSHVppy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2206 FIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS----IQHLKNRFGDGY 2280
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEF 249
|
250 260 270
....*....|....*....|....*....|..
gi 110225379 2281 MITVrtkssqnvkdvvrffnrNFPEAMLKERH 2312
Cdd:PRK11607 250 IGSV-----------------NVFEGVLKERQ 264
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2050-2263 |
3.92e-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: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkdllqvqqsl 2129
Cdd:cd03216 1 LELRGITKRF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 gycpQFDALFDeltAREHlqlytrlrGIpwkdeaQVVkwalekleltkyadkpagtY--SGGNKRKLSTAIALIGYPAFI 2207
Cdd:cd03216 65 ----SFASPRD---ARRA--------GI------AMV-------------------YqlSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2208 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1001-1204 |
3.98e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.82 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1001 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQH-NVLFDR 1077
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNpETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 LTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1157
Cdd:PRK13644 93 RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225379 1158 RAIWDLILK-YKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13644 173 IAVLERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEP 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
991-1209 |
5.25e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDK-KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKNLGM 1067
Cdd:PRK13650 7 VKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENvwDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRA--II 1144
Cdd:PRK13650 86 VFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR--VAIAGAVAMRPkiII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1145 LDEPTAGVDPYARRaiwDLI-----LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP--LFLKG 1209
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 ... |
1000-1209 |
6.70e-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: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1000 NDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1078
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1079 TVEEHLwFYSRLKSMAQEEIR--KET--DKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03254 92 TIMENI-RLGRPNATDEEVIEaaKEAgaHDFIMKLP--NGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1151 GVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP--LFLKG 1209
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNA----DKILVLDDGKIIEEGTHdeLLAKK 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2051-2262 |
7.94e-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: 93.79 E-value: 7.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQVQ 2126
Cdd:cd03256 2 EVENLSKTYPNGKK----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDALFDELTAREHLqLYTRLRGIPW---------KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA 2197
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENV-LSGRLGRRSTwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2198 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2077-2243 |
8.62e-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: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTGDEST---TGGEAFVNGHSVLKDLlqvQQSLGYCPQFDALFDELTAREHLQLYTR 2153
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2154 LR---GIPWKDEAQVVKWALEKLELTKYADKPAGTYSGG----NKRKLSTAIALIGYPA-FIFLDEPTTGMDPKARRFLW 2225
Cdd:TIGR00956 863 LRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*...
gi 110225379 2226 NLILDLIKTGRSVVLTSH 2243
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIH 960
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1005-1219 |
1.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-----EMDEIRKNLGMCPQ--HNVLFDR 1077
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 lTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSnkRHSLVQT---LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1154
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1155 YARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGAYGDGYRLTL 1219
Cdd:PRK13646 179 QSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPkeLFKDKKKLADWHIGL 247
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
998-1199 |
1.27e-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: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDr 1077
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 ltveehlwfysrlksmaqeeirketdkmiedlelSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1157
Cdd:cd03247 89 ----------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110225379 1158 RAIWDLILKYKPGRTILLSTHHmdeadLLG----DRIAIISHGKLK 1199
Cdd:cd03247 135 RQLLSLIFEVLKDKTLIWITHH-----LTGiehmDKILFLENGKII 175
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2050-2269 |
1.53e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.34 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---DLLQVQ 2126
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFD--ALFDElTAREHLQLYTRLRGIPWKDEAQVVKWALE--KLELTKYADKPAGTYSGGNKRKLSTAIALIG 2202
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2203 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2269
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
998-1203 |
1.73e-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: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1076
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 RlTVEEHLWFYSRLKSMAQ-EEIRKETDKMIEDLELSNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1151
Cdd:cd03252 90 R-SIRDNIALADPGMSMERvIEAAKLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1152 VDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLKCCGS 1203
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2049-2243 |
2.45e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.40 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTkvykSRKIGRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQS 2128
Cdd:PRK13538 1 MLEARNLA----CERDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQLYTRLRGIPwkDEAQVVKwALEKLELTKYADKPAGTYSGGNKRKLSTA-IALIGYPAFI 2207
Cdd:PRK13538 76 LLYLGHQPGIKTELTALENLRFYQRLHGPG--DDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALArLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 110225379 2208 fLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2243
Cdd:PRK13538 153 -LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1001-1204 |
3.29e-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: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1001 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdiRT----EMdeirkNLGMCPQhnvlfd 1076
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVsallEL-----GAGFHPE------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 rLTVEEHLWFYSRLKSMAQEEIRKETDKmIEDL-ELSNKRHSLVQTLSGGMKRKLSVAIAFvggsrAI-----ILDEPTA 1150
Cdd:COG1134 103 -LTGRENIYLNGRLLGLSRKEIDEKFDE-IVEFaELGDFIDQPVKTYSSGMRARLAFAVAT-----AVdpdilLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1151 GVDPY----ARRAIWDLILKykpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:COG1134 176 VGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
2079-2264 |
3.46e-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: 91.20 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2079 PGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG----HSVLKDLLQVQQ-SLGYCPQFDALFDELTAREHLqLYTR 2153
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQrKIGLVFQQYALFPHLNVRENL-AFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2154 LRGIPWKDEAQVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK 2233
Cdd:cd03297 101 KRKRNREDRISVDE-LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|..
gi 110225379 2234 T-GRSVVLTSHSMEECEALCTRLAIMVNGRLR 2264
Cdd:cd03297 180 NlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2049-2274 |
3.47e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQ 2126
Cdd:PRK09700 5 YISMAGIGK-----SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDALFDELTAREHL---QLYTR-LRGIP---WKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2199
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigRHLTKkVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2200 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2274
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2077-2243 |
3.64e-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: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVLKDLlqvQQSLGYCPQFDALFDELTAREHLQLYTRL 2154
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2155 RGIpwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT 2234
Cdd:cd03232 107 RGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
....*....
gi 110225379 2235 GRSVVLTSH 2243
Cdd:cd03232 158 GQAILCTIH 166
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2047-2264 |
3.65e-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: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkdllqvq 2126
Cdd:COG0488 313 KKVLELEGLSKSYGDKTL-----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETV-------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 qSLGYCPQ-FDALFDELTAREHLQlytrlRGIPWKDEAQVVKWaLEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYP 2204
Cdd:COG0488 379 -KIGYFDQhQEELDPDKTVLDELR-----DGAPGGTEQEVRGY-LGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2205 AFIFLDEPTTGMDPKARrflwNLILDLIKT--GrSVVLTSHSMEECEALCTRLAIMVNGRLR 2264
Cdd:COG0488 452 NVLLLDEPTNHLDIETL----EALEEALDDfpG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2069-2263 |
4.25e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.83 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKDLLQVQQSLGYCPQF--DALF---- 2139
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKTVGIVFQNpdDQLFaptv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2140 DELTAREHLQLytrlrGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2219
Cdd:PRK13639 97 EEDVAFGPLNL-----GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110225379 2220 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1005-1183 |
4.33e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtemdeirKNLGMCPQHNVLFDRL--TVEE 1082
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 ----HLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1158
Cdd:NF040873 77 lvamGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180
....*....|....*....|....*.
gi 110225379 1159 AIWDLILKY-KPGRTILLSTHHMDEA 1183
Cdd:NF040873 157 RIIALLAEEhARGATVVVVTHDLELV 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
991-1194 |
4.90e-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: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVY--KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEiRknlGMC 1068
Cdd:COG4525 6 VRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-R---GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225379 1149 TAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIIS 1194
Cdd:COG4525 162 FGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
978-1204 |
5.92e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.63 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 978 MEEEPTHLPLVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTE 1057
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1058 MDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIR---KETDKMIEDLELSNKRhslVQTLSGGMKRKLSVAI 1134
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITprvMEALRMVQLEEFAQRK---PHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1135 AFVGGSRAIILDEPTAGVDpYARRAIWDLILKY---KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD-YKLRKQMQNELKAlqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2049-2263 |
6.85e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.71 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQ 2124
Cdd:PRK11153 1 MIELKNISKVFPQGG-RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPwkdEAQVVKWALEKLELTKYADKpAGTY----SGGNKRKLSTAIAL 2200
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTP---KAEIKARVTELLELVGLSDK-ADRYpaqlSGGQKQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2201 IGYPAFIFLDEPTTGMDPKARRflwnLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTR----SILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
994-1204 |
8.10e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 8.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 994 LTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNV 1073
Cdd:PRK11607 25 LTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1074 LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1154 PYARR----AIWDLILKYkpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK11607 182 KKLRDrmqlEVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
998-1179 |
9.73e-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: 9.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDR 1077
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 LTVEEHLWFYSRLKSMAQEEIrketDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1157
Cdd:TIGR01189 88 LSALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|...
gi 110225379 1158 RAIWDLILKY-KPGRTILLSTHH 1179
Cdd:TIGR01189 164 ALLAGLLRAHlARGGIVLLTTHQ 186
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1006-1204 |
1.03e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVL-FDrLTVEE- 1082
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAVLPQHSSLsFP-FTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 -HLWFYSRLKSMAQEEIrkETDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFV--------GGSRAIILDEPTAGVD 1153
Cdd:PRK13548 97 vAMGRAPHGLSRAEDDA--LVAAALAQVDLAHLAGRDYPQLSGGEQQR--VQLARVlaqlwepdGPPRWLLLDEPTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1154 PY--------ARRaiwdliLKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13548 173 LAhqhhvlrlARQ------LAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1010-1198 |
1.24e-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: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1010 SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLGMCP---QHNVLFDRLTVEE-- 1082
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYVPedrKGEGLVLDLSIREni 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 ---HLWFYSRLKSMAQEEIRKETDKMIEDLEL-SNKRHSLVQTLSGGMKRKlsVAIA--FVGGSRAIILDEPTAGVDPYA 1156
Cdd:COG1129 352 tlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPTRGIDVGA 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 1157 RRAIWDLILKY-KPGRTILLSTHHMDEadLLG--DRIAIISHGKL 1198
Cdd:COG1129 430 KAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
988-1204 |
1.34e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 96.35 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 988 VVCVDKLTKVYKndKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNL 1065
Cdd:NF033858 1 VARLEGVSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1066 GMCPQ---HNvLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1142
Cdd:NF033858 79 AYMPQglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1143 IILDEPTAGVDPYARRAIWDLI---LKYKPGRTILLSTHHMDEADLLgDRIAIISHGKLKCCGSP 1204
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIdriRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
998-1197 |
1.38e-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: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1076
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 RlTVEEHLwFYSRLKSmAQEEIRK-----ETDKMIEDLElsNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:cd03251 90 D-TVAENI-AYGRPGA-TREEVEEaaraaNAHEFIMELP--EGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1148 PTAGVDPYARRAIWDLILKYKPGRTIL-----LSThhMDEAdllgDRIAIISHGK 1197
Cdd:cd03251 165 ATSALDTESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1006-1196 |
1.56e-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: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrtemDEIRKNLGMCPQHNVLFDRLTVEEH-- 1083
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRMVVFQNYSLLPWLTVRENia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1084 LWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1163
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 110225379 1164 ILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1196
Cdd:TIGR01184 157 LMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2069-2277 |
1.87e-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: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLL--QVQQSLGYCPQFDALFDElTARE 2146
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD-LRDLDedDLRRRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2147 HLQLytrlrGIPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTG 2215
Cdd:COG4987 428 NLRL-----ARPDATDEELWA-ALERVGLGDWLAAlPDGldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2216 MDPKARRFLWNLILDLIKtGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2277
Cdd:COG4987 502 LDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2078-2282 |
1.97e-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: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2078 RPGECFGLLGVNGAGKTS-----TFKMLTGdeSTTGGEAFVNGHSVlkDLLQVQQSLGYCPQFDALFDELTAREHLQLYT 2152
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2153 RLR---GIPWKDEAQVVKWALEKLELTKYADKPAGT------YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2223
Cdd:TIGR00955 125 HLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2224 LWNLILDLIKTGRSVVLTSH--SMEECEaLCTRLAIMVNGRLRCLGSIQHLKNRFGD-GYMI 2282
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDlGHPC 265
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1005-1204 |
2.02e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSA-----TIYGHDIRTEMDEIRKNLGMCPQ--HNVLFDR 1077
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 lTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNK--RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1155
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1156 ARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK13643 179 ARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
991-1204 |
3.08e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.07 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1070
Cdd:PRK10851 5 IANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWF----YSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:PRK10851 82 HYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1147 EPTAGVDPYARRAI--WDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK10851 162 EPFGALDAQVRKELrrWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1006-1227 |
3.13e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMC---PQHNVLFDrlT 1079
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYT--D 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1080 VEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1159
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1160 IWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGAYGDGYRLT---LVKQPAEPG 1227
Cdd:PRK13638 175 MIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPgeVFACTEAMEQAGLTqpwLVKLHTQLG 248
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
985-1204 |
4.29e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 985 LPLVVCVDKLTKVYkndkkmaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIrtEMDEI 1061
Cdd:TIGR00955 27 LRGCFCRERPRKHL-------LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1062 RKNLGMCPQHNVLFDRLTVEEHLWFYSRLK---SMAQEEIRKETDKMIEDLELSNKRHSLVQT------LSGGMKRKLSV 1132
Cdd:TIGR00955 98 RAISAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1133 AIAFVGGSRAIILDEPTAGVDPYAR----RAIWDLILKykpGRTILLSTHHmDEADL--LGDRIAIISHGKLKCCGSP 1204
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAysvvQVLKGLAQK---GKTIICTIHQ-PSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2050-2263 |
5.03e-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: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKD--LLQV 2125
Cdd:cd03292 1 IEFINVTKTYP----NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdLRGraIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2206 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
991-1192 |
7.33e-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: 7.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIRT----EMDEI 1061
Cdd:COG0444 4 VRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1062 R-KNLGMCPQhnvlfD-------RLTVEEHLW-FYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQ---TLSGGMKRK 1129
Cdd:COG0444 84 RgREIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1130 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAI 1192
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2067-2263 |
7.90e-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: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2067 ILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAR 2145
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2146 EHLQLytrlrGIPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2214
Cdd:cd03245 96 DNITL-----GAPLADDERILR-AAELAGVTDFVNKhPNGldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2215 GMDPKA-RRFLWNliLDLIKTGRSVVLTSH--SMEEceaLCTRLAIMVNGRL 2263
Cdd:cd03245 170 AMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGRI 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2052-2243 |
8.66e-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: 8.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2052 IENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkdllqvqQSLGY 2131
Cdd:COG0488 1 LENLSKSFGGRPL-----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2132 CPQFDALFDELTAREHL--------QLYTRLRGIP-------------------------WKDEAQVVKwALEKLELTK- 2177
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVldgdaelrALEAELEELEaklaepdedlerlaelqeefealggWEAEARAEE-ILSGLGFPEe 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2178 YADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLildLIKTGRSVVLTSH 2243
Cdd:COG0488 145 DLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LKNYPGTVLVVSH 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2049-2258 |
9.02e-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: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdllqvqqs 2128
Cdd:COG4525 3 MLTVRHVSVRYPGGG-QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 lgycP--------QFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIAL 2200
Cdd:COG4525 74 ----PgadrgvvfQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2201 IGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIM 2258
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2018-2277 |
1.42e-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: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2018 QRL-PVSTKPVEDDVDVASERQRVLRGDadndmVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTST 2096
Cdd:COG2274 446 ERLdDILDLPPEREEGRSKLSLPRLKGD-----IELENVSFRYPGDSP---PVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2097 FKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREHLQLytrlrGIPWKDEAQVVkWALEKLEL 2175
Cdd:COG2274 518 LKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITL-----GDPDATDEEII-EAARLAGL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2176 TKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHS 2244
Cdd:COG2274 591 HDFIEAlPMGydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHR 669
|
250 260 270
....*....|....*....|....*....|...
gi 110225379 2245 MeECEALCTRLAIMVNGRLRCLGSIQHLKNRFG 2277
Cdd:COG2274 670 L-STIRLADRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1005-1205 |
1.47e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT------EMDEIRKNLGMC---PQHNVLF 1075
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikEVKRLRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DrlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSN---KRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1152
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyvKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1153 DPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPL 1205
Cdd:PRK13645 182 DPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1005-1202 |
1.54e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.77 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCPQHNVLFDRLTVEE 1082
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLwFYSRL---KSMA-----QEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1154
Cdd:PRK09700 100 NL-YIGRHltkKVCGvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1155 YARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1202
Cdd:PRK09700 179 KEVDYLFLIMnqLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2049-2263 |
2.03e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.07 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL---KDLLQV 2125
Cdd:PRK09493 1 MIEFKNVSKHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQFDALFDELTAREHLQL-YTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2204
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2205 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
997-1198 |
2.30e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 997 VYKNDKKMALNKL---SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQH- 1071
Cdd:PRK13642 11 VFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 NVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1151
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110225379 1152 VDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKL 1198
Cdd:PRK13642 171 LDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
978-1204 |
2.34e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.75 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 978 MEEEPTHLPLVVCVDKLTKVY---KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI----Y 1050
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYCVFdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1051 GHDIRTEMD-------------EIRKNLGMC---PQHNVLFDrlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSN- 1113
Cdd:PRK13631 91 GDKKNNHELitnpyskkiknfkELRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDs 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1114 --KRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRI 1190
Cdd:PRK13631 169 ylERSPF--GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEVADEV 246
|
250
....*....|....
gi 110225379 1191 AIISHGKLKCCGSP 1204
Cdd:PRK13631 247 IVMDKGKILKTGTP 260
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
2069-2247 |
4.52e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.59 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvlkdllqvqqSLGYCPQFDALFDEL--TARE 2146
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2147 --------HLQLYTRLRgipwKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2218
Cdd:NF040873 77 lvamgrwaRRGLWRRLT----RDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*....
gi 110225379 2219 KARRFLWNLILDLIKTGRSVVLTSHSMEE 2247
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2067-2263 |
4.63e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2067 ILAVDRLC--------LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQQSLGYCP--- 2133
Cdd:PRK15439 268 VLTVEDLTgegfrnisLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2134 QFDALFDELTAREHLQLYTRLRGIPWKDEAQvvkwalEKLELTKY----------ADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:PRK15439 348 QSSGLYLDAPLAWNVCALTHNRRGFWIKPAR------ENAVLERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1001-1179 |
4.99e-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: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1001 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTV 1080
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1081 EEHLWFYSRLKSMAQEEirketdKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1160
Cdd:cd03231 91 LENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 110225379 1161 WDLILKY-KPGRTILLSTHH 1179
Cdd:cd03231 165 AEAMAGHcARGGMVVLTTHQ 184
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
997-1203 |
5.31e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 997 VYKNDKKMaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP------PTSGSATIYGHDI-RTEMDEIRKNLGMCP 1069
Cdd:PRK14246 18 LYINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRLTVEEHLWFysRLKSMAQEEiRKETDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSR 1141
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAY--PLKSHGIKE-KREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1142 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS 1203
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2050-2263 |
5.42e-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: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL---KDLLQVQ 2126
Cdd:cd03262 1 IEIKNLHKSFGDFHV-----LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDALFDELTAREHLQL-YTRLRGIPwKDEAQvvKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIG 2202
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMS-KAEAE--ERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2203 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1005-1198 |
5.66e-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: 5.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDE-----IRKNLGMCPQHNVLFDR 1077
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairlLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 LTVEEHLWFYS-RLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1156
Cdd:COG4161 97 LTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110225379 1157 RRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:COG4161 177 TAQVVEIIRELSqTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1006-1211 |
6.01e-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: 6.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHL 1084
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1085 WF--YSRLKSMAQEEIRK-ETDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1157
Cdd:cd03249 98 RYgkPDATDEEVEEAAKKaNIHDFIMSLP--DGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1158 RAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP---LFLKGAY 1211
Cdd:cd03249 176 KLVQEALDRAMKGRTTIVIAHRLStirNA----DLIAVLQNGQVVEQGTHdelMAQKGVY 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2046-2263 |
1.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2046 DNDMVKIENLTKVYKSRKIG-RILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG--HSVLKDL 2122
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEStEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2123 LQVQQSLGYCPQ------FDALFDELTA--REHLqlytrlrGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKL 2194
Cdd:PRK13633 81 WDIRNKAGMVFQnpdnqiVATIVEEDVAfgPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2195 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECeALCTRLAIMVNGRL 2263
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
992-1199 |
1.18e-17 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 85.25 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 992 DKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdirtEMDEIRKNLGMCPQh 1071
Cdd:PRK13546 26 DALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 nvlfdrLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP-TA 1150
Cdd:PRK13546 100 ------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1151 GVDPYARRAIwDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLK 1199
Cdd:PRK13546 174 GDQTFAQKCL-DKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2070-2267 |
1.68e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2070 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLLQVQQSLGYCPQFDALFDELTAREHL 2148
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2149 QL-----YTRLRGIPWKDEAqVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD-PKARR 2222
Cdd:PRK09536 99 EMgrtphRSRFDTWTETDRA-AVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 2223 FLwNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2267
Cdd:PRK09536 178 TL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
991-1198 |
1.69e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKM-----ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-------- 1057
Cdd:PRK13651 5 VKNIVKIF--NKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1058 -----------------MDEIRKNLGMCPQ--HNVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIE--DLELSNKRH 1116
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIElvGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1117 SLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISH 1195
Cdd:PRK13651 162 SPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
...
gi 110225379 1196 GKL 1198
Cdd:PRK13651 241 GKI 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
992-1198 |
2.36e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.39 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 992 DKLTKVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGM 1067
Cdd:PRK10908 5 EHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQ-HNVLFDRlTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:PRK10908 84 IFQdHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1147 EPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1017-1198 |
2.84e-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: 82.73 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1017 QVVSFLGHNGAGKTTTMSILTGLFPPTSGsaTIYGHDirTEMDEIRKNLGMCP---------QHNVLFDRLTVEEHLWFy 1087
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGG--TIVLNG--TVLFDSRKKINLPPqqrkiglvfQQYALFPHLNVRENLAF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1088 sRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY 1167
Cdd:cd03297 99 -GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|...
gi 110225379 1168 KP--GRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:cd03297 178 KKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
988-1196 |
3.21e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.91 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 988 VVCVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP--PTSGS-ATIYGHDIRTE---MDEI 1061
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQREgrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1062 RKN---LGMCPQHNVLFDRLTVEEHLW--------FYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKL 1130
Cdd:PRK09984 82 RKSranTGYIFQQFNLVNRLSVLENVLigalgstpFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1131 SVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHG 1196
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1009-1178 |
3.26e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1009 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGmcpQHNVLFDRLTVEEHLWFY 1087
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG---HRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1088 SRLKSMAQEEIrketDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY 1167
Cdd:PRK13539 98 AAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|..
gi 110225379 1168 -KPGRTILLSTH 1178
Cdd:PRK13539 174 lAQGGIVIAATH 185
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2050-2262 |
4.01e-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: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQS 2128
Cdd:cd03228 1 IEFKNVSFSYPGRPK---PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDElTAREHLqlytrlrgipwkdeaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2209 LDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMEECEaLCTRLAIMVNGR 2262
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1003-1196 |
4.34e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.60 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1003 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEirknLGMCPQHNVLFDRLTVEE 1082
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWD 1162
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 110225379 1163 LILK--YKPGRTILLSTHHMDEADLLGDRIAIISHG 1196
Cdd:PRK11248 170 LLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
991-1198 |
6.28e-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: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1069
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDrltveehlwfysrlKSMAqEEIrketdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:cd03246 83 QDDELFS--------------GSIA-ENI-----------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1150 AGVDPYARRAIWDLI--LKyKPGRTILLSTHHMdEADLLGDRIAIISHGKL 1198
Cdd:cd03246 125 SHLDVEGERALNQAIaaLK-AAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2049-2268 |
6.46e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLL--QVQ 2126
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKP-ISMLSsrQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDALFDELTARE--------HLQLYTRLRGipwKDEaQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAI 2198
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRElvaygrspWLSLWGRLSA---EDN-ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2199 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
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 ... |
991-1198 |
6.97e-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: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE------ 1060
Cdd:TIGR02323 6 VSGLSKSYGGGK--GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAElelyQLSEaerrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1061 IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQE---EIRKETDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIAF 1136
Cdd:TIGR02323 84 MRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1137 VGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
980-1199 |
1.13e-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: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 980 EEPTHLP-LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIRtem 1058
Cdd:COG0488 306 PPPERLGkKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1059 deirknLGMCPQHNVLFD-RLTVEEHLWfysRLKSMAQE-EIRketdKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIA 1135
Cdd:COG0488 380 ------IGYFDQHQEELDpDKTVLDELR---DGAPGGTEqEVR----GYLGRFLFSGDDaFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1136 FVGGSRAIILDEPTAGVDPYARRAIWDLILKYkPGrTILLSTHHMDEADLLGDRIAIISHGKLK 1199
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2047-2272 |
1.23e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQvQ 2126
Cdd:PRK11432 4 KNFVVLKNITKRF-----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2206
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2207 IFLDEPTTGMDPKARRFLWNLILDLIKtgrSVVLTS----HSMEECEALCTRLAIMVNGRLRCLGSIQHL 2272
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQ---QFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
970-1198 |
1.30e-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: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 970 RHFEETRGMEEepthlplvvcVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI 1049
Cdd:TIGR02203 322 RAIERARGDVE----------FRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1050 YGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHLwFYSRLKSMAQEEIRkETDKMIEDLELSNKRHSLVQT------- 1121
Cdd:TIGR02203 392 DGHDLADyTLASLRRQVALVSQDVVLFND-TIANNI-AYGRTEQADRAEIE-RALAAAYAQDFVDKLPLGLDTpigengv 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1122 -LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1198
Cdd:TIGR02203 469 lLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1005-1204 |
1.46e-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: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIR--------KNLGMCPQHNVLFD 1076
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGpdgrgrakRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 RLTVEEHLWFYSRLKSMAQEEIRKE--TDKMI--EDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1152
Cdd:TIGR03269 379 HRTVLDNLTEAIGLELPDELARMKAviTLKMVgfDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1153 DPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:TIGR03269 459 DPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2049-2262 |
1.51e-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: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIG--RILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQV- 2125
Cdd:COG4778 4 LLEVENLSKTFTLHLQGgkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQAs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 --------QQSLGYCPQF-------DALfdELTArEHLqlytRLRGIPwKDEAQV-VKWALEKLEL-TKYADKPAGTYSG 2188
Cdd:COG4778 84 preilalrRRTIGYVSQFlrviprvSAL--DVVA-EPL----LERGVD-REEARArARELLARLNLpERLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2189 GNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
2049-2268 |
1.78e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTG----GEAFVNGHSVLKDLL 2123
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGkvtvGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQQSLGYCPQF--DALFDElTAREHLQLYTRLRGIPwKDEAQvvKWALEKLELT----KYADKPAGTYSGGNKRKLSTA 2197
Cdd:PRK13643 81 PVRKKVGVVFQFpeSQLFEE-TVLKDVAFGPQNFGIP-KEKAE--KIAAEKLEMVgladEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2198 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1005-1198 |
2.39e-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: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEH 1083
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1084 LWFYSRLKSMAQE--------EIRKETDKMIEDLELSNKRHSlvQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1155
Cdd:TIGR01193 568 LLLGAKENVSQDEiwaaceiaEIKDDIENMPLGYQTELSEEG--SSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110225379 1156 ARRAIWDLILKYKPgRTILLSTHHMDEADLLgDRIAIISHGKL 1198
Cdd:TIGR01193 646 TEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
986-1184 |
2.60e-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: 84.65 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 986 PLVVCVDKLTKVYkNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKN 1064
Cdd:TIGR02857 319 ASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1065 LGMCPQHNVLFDRlTVEEHLWFYSRLKS---MAQEEIRKETDKMIEDLELSnkRHSLV----QTLSGGMKRKLSVAIAFV 1137
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIRLARPDASdaeIREALERAGLDEFVAALPQG--LDTPIgeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1138 GGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTH---HMDEAD 1184
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1082-1212 |
3.11e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.86 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1082 EHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1161
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1162 DLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGAYG 1212
Cdd:NF000106 185 DEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1004-1198 |
3.54e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1004 MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLF-----PPTSGSATIYGHDIRTE-MD--EIRKNLGMCPQHNVLF 1075
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPdVDpiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DRLTVEEHLWFYSRLKSMAQEeiRKETDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKS--KKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1148 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2049-2263 |
3.59e-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: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVL----KD 2121
Cdd:COG0444 1 LLEVRNLKVYFPTRR-GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLklseKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2122 LLQV-QQSLGYCPQ--FDAL---------FDElTAREHlqlytrlRGIPWKDEAQVVKWALEKLELT---KYADKPAGTY 2186
Cdd:COG0444 80 LRKIrGREIQMIFQdpMTSLnpvmtvgdqIAE-PLRIH-------GGLSKAEARERAIELLERVGLPdpeRRLDRYPHEL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2187 SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
991-1204 |
4.76e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.44 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGMCP 1069
Cdd:PRK11231 5 TENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRLTVEE--------HLWFYSRLKSMAQEEIRKETDKMiEDLELSNKRhslVQTLSGGMKRKLSVAIAFVGGSR 1141
Cdd:PRK11231 83 QHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQT-RINHLADRR---LTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1142 AIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2072-2243 |
5.02e-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: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2072 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLY 2151
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 TRLRGipwkDEAqvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2231
Cdd:cd03231 98 HADHS----DEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|..
gi 110225379 2232 IKTGRSVVLTSH 2243
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2049-2280 |
5.20e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrILAVDrlcLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSV------L 2119
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA--LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVqregrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2120 KDLLQVQQSLGYCPQFDALFDELTAREHLqLYTRLRGIP-WK--------DEAQVVKWALEKLELTKYADKPAGTYSGGN 2190
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPfWRtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2191 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2269
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
250
....*....|..
gi 110225379 2270 QHLKN-RFGDGY 2280
Cdd:PRK09984 238 QQFDNeRFDHLY 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2053-2297 |
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 110225379 2053 ENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLLQVQ-Q 2127
Cdd:PRK10070 27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVRrK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 SLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2207
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2208 FLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMIT--- 2283
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTffr 266
|
250
....*....|....*
gi 110225379 2284 -VRTKSSQNVKDVVR 2297
Cdd:PRK10070 267 gVDISQVFSAKDIAR 281
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2050-2277 |
6.51e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.41 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--KDLLQVQQ 2127
Cdd:NF033858 2 ARLEGVSHRY-----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdaRHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 SLGYCPQF--DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:NF033858 77 RIAYMPQGlgKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2206 FIFLDEPTTGMDPKARRFLWNLIlDLIKTGR---SVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2277
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELI-DRIRAERpgmSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2046-2263 |
6.94e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.42 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2046 DNDMVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVLKD-LL 2123
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEN---NALKNVSFEINEGEYVAILGHNGSGK-STIsKILTGLLKPQSGEIKIDGITISKEnLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQQSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIG 2202
Cdd:PRK13632 80 EIRKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2203 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2263
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKL 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1006-1204 |
1.00e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.98 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---TEMDEIRKNLGMCPQHNVLFDRLTVEE 1082
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVFQQFYLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLWFYS-RLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR---- 1157
Cdd:PRK09493 97 NVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRhevl 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110225379 1158 RAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK09493 177 KVMQDLA---EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2049-2263 |
1.04e-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: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDLLQ 2124
Cdd:COG3845 5 ALELRGITKRF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 -----VQQslgycpQFdALFDELTAREHLQLY---TRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLST 2196
Cdd:COG3845 80 lgigmVHQ------HF-MLVPNLTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2197 AIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2084-2275 |
1.08e-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: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2084 GLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhSVLKD------LLQVQQSLGYCPQFDALFDELTAREHLQL-YTRLRG 2156
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-RTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYgMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2157 ipwkdEAQVVKWA--LEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARR----FLWNLILD 2230
Cdd:TIGR02142 106 -----SERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYeilpYLERLHAE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 2231 LiktGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNR 2275
Cdd:TIGR02142 181 F---GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2069-2282 |
1.09e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKDLLQVQQSLGYCPQ------FDALF 2139
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQdpdnqlFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2140 DELTAREHLQLytrlrGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2219
Cdd:PRK13636 101 YQDVSFGAVNL-----KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2220 ARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLknrFGDGYMI 2282
Cdd:PRK13636 176 GVSEIMKLLVEMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV---FAEKEML 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1005-1204 |
2.32e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDE-----IRKNLGMCPQHNVLFDR 1077
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkaireLRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 LTVEEHLWFYS-RLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1156
Cdd:PRK11124 97 LTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1157 RRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIA------IISHGKLKCCGSP 1204
Cdd:PRK11124 177 TAQIVSIIRELaETGITQVIVTHEVEVARKTASRVVymenghIVEQGDASCFTQP 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2048-2311 |
2.38e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2048 DMVKIENLTKVYKSRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKD-LLQVQ 2126
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKYTL--NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2206 FIFLDEPTTGMDPKARrflwnliLDLIKTGRS--------VVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFG 2277
Cdd:PRK13650 161 IIILDEATSMLDPEGR-------LELIKTIKGirddyqmtVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
250 260 270
....*....|....*....|....*....|....
gi 110225379 2278 DGYMITVRTKSSQNVKDVVRFFNRNFPEAMLKER 2311
Cdd:PRK13650 233 DLLQLGLDIPFTTSLVQSLRQNGYDLPEGYLTEK 266
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
996-1215 |
4.19e-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: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 996 KVYKNDKKMaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGlFP---PTSGSATIYGHDIrTEM--DEI-RKNLGMCP 1069
Cdd:cd03217 7 HVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLppEERaRLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRLTVEEHLwfysrlksmaqeeirketdkmiedlelsnkrHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:cd03217 84 QYPPEIPGVKNADFL-------------------------------RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1150 AGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLL-GDRIAIISHGKLKCCGSPLFLKGAYGDGY 1215
Cdd:cd03217 133 SGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
2075-2269 |
4.33e-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: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2075 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---DLLQVQQSLgycpqfdALFDELTAREHLQLY 2151
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNY-------SLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 TR--LRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2229
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110225379 2230 DLIKTGR-SVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2269
Cdd:TIGR01184 159 QIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2070-2263 |
4.49e-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: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2070 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREHL 2148
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2149 qlytrlrgipwkdeaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2228
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*
gi 110225379 2229 LDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRL 2263
Cdd:cd03246 140 AALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
978-1198 |
4.61e-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: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 978 MEEEPTHLPLVVCVDKLTkVYKNDKKmALNKLSLNLYENQVVSFLGHNGAGKTT---TMSILTGLFPP--TSGSATIYGH 1052
Cdd:COG1117 1 MTAPASTLEPKIEVRNLN-VYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1053 DIRT-EMD--EIRKNLGMCPQH----------NVLFD-RLtveeHlwfysRLKSmaqeeiRKETDKMIEDL--------E 1110
Cdd:COG1117 79 DIYDpDVDvvELRRRVGMVFQKpnpfpksiydNVAYGlRL----H-----GIKS------KSELDEIVEESlrkaalwdE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1111 LSNKRHSLVQTLSGGMKRKLSVAiafvggsRAI------IL-DEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEA 1183
Cdd:COG1117 144 VKDRLKKSALGLSGGQQQRLCIA-------RALavepevLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQA 216
|
250
....*....|....*
gi 110225379 1184 DLLGDRIAIISHGKL 1198
Cdd:COG1117 217 ARVSDYTAFFYLGEL 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1002-1204 |
4.90e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.99 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1002 KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNVLFDRLTVE 1081
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1082 EHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1161
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 1162 DLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK11432 177 EKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1006-1198 |
4.91e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMD----------EIRKN----LGMCP 1069
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDglangivyisEDRKRdglvLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVlfdRLTVEEHLwfysrlkSMAQEEIRKETDKM-IED-LELSN-KRHSLVQT---LSGGMKRKLSVAIAFVGGSRAI 1143
Cdd:PRK10762 348 KENM---SLTALRYF-------SRAGGSLKHADEQQaVSDfIRLFNiKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1144 ILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEadLLG--DRIAIISHGKL 1198
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
998-1211 |
6.41e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE--IRKNLGMCPQHNVLF 1075
Cdd:PRK11160 348 YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DRlTVEEHLwfysrlkSMAQEEIRKEtdKMIEDLE---LSNkrhsLVQT--------------LSGGMKRKLSVAIAFVG 1138
Cdd:PRK11160 427 SA-TLRDNL-------LLAAPNASDE--ALIEVLQqvgLEK----LLEDdkglnawlgeggrqLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1139 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTH------HMdeadllgDRIAIISHGKLKCCGS---PLFLKG 1209
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltgleQF-------DRICVMDNGQIIEQGThqeLLAQQG 565
|
..
gi 110225379 1210 AY 1211
Cdd:PRK11160 566 RY 567
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2078-2243 |
6.61e-15 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 81.43 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2078 RPGECFGLLGVNGAGKTSTFKMLTGDEstTGGeaFVNGHSVLKDLLQVQQSL----GYCPQFDALFDELTAREHL--QLY 2151
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESLiySAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 TRLRGIPWKDEAQV-VKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLW 2225
Cdd:PLN03140 980 LRLPKEVSKEEKMMfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
170
....*....|....*...
gi 110225379 2226 NLILDLIKTGRSVVLTSH 2243
Cdd:PLN03140 1060 RTVRNTVDTGRTVVCTIH 1077
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2050-2276 |
7.18e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.84 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL------KDLL 2123
Cdd:PRK09452 15 VELRGISKSFDGKEV-----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvpaenRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQQSlgYcpqfdALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:PRK09452 90 TVFQS--Y-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRF 2276
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
991-1198 |
7.22e-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: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTkVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKnLGMC 1068
Cdd:COG3845 260 VENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSprERRR-LGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 -----PQHNVLFDRLTVEEHLWF-------YSRLKSMAQEEIRKETDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIA 1135
Cdd:COG3845 337 yipedRLGRGLVPDMSVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDVRTPGpDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1136 FVGGSRAIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2059-2271 |
8.10e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2059 YKSRKIGRI-LAVDRL---------CLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KDllQ 2124
Cdd:PRK11288 248 YRPRPLGEVrLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirspRD--A 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQ---FDALFDELTAREHLQLYTRLRGIPW------KDEAQVVKWALEKLEL-TKYADKPAGTYSGGNKRK- 2193
Cdd:PRK11288 326 IRAGIMLCPEdrkAEGIIPVHSVADNINISARRHHLRAgclinnRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKa 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2194 -----LSTAIALIgypafiFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRclGS 2268
Cdd:PRK11288 406 ilgrwLSEDMKVI------LLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GE 477
|
...
gi 110225379 2269 IQH 2271
Cdd:PRK11288 478 LAR 480
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2044-2272 |
8.67e-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: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2044 DADNDMVKIENLTKVYKSRKigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DL 2122
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGR----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2123 LQVQQSLGYCPQFDALFdELTAREHLQLYTrlrgiPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNK 2191
Cdd:COG4988 407 ASWRRQIAWVPQNPYLF-AGTIRENLRLGR-----PDASDEELEA-ALEAAGLDEFVAAlPDGldtplgeggrGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2192 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQH 2271
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEE 557
|
.
gi 110225379 2272 L 2272
Cdd:COG4988 558 L 558
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2049-2270 |
8.67e-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: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLLQVQQS 2128
Cdd:COG4559 1 MLEAENLSVRLGGRTL-----LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP-LAAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 --LGYCPQFDAL-FDeLTAREHLqlytRLRGIPW----KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2201
Cdd:COG4559 75 rrRAVLPQHSSLaFP-FTVEEVV----ALGRAPHgssaAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2202 -------GYPAFIFLDEPTTGMDPK--------ARRFLwnlildliKTGRSVV-------LTSHsmeeceaLCTRLAIMV 2259
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAhqhavlrlARQLA--------RRGGGVVavlhdlnLAAQ-------YADRILLLH 214
|
250
....*....|.
gi 110225379 2260 NGRLRCLGSIQ 2270
Cdd:COG4559 215 QGRLVAQGTPE 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1008-1204 |
1.17e-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: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1008 KLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-----RKNLGMCPQHNVLFDRLTVEE 1082
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLwFYSRLKSMAqEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD--------P 1154
Cdd:TIGR02142 95 NL-RYGMKRARP-SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdprkyeilP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1155 YARRaiwdliLKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:TIGR02142 173 YLER------LHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1006-1198 |
1.30e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.10 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLF-----PPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVLFDRLT 1079
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1080 VEEHLWFYSRLKSMA------QEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:PRK14247 99 IFENVALGLKLNRLVkskkelQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 1154 PYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2027-2263 |
1.44e-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: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2027 VEDDVDVASERQRVLRGDAdndMVKIENLTkVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDEST 2106
Cdd:COG3845 238 VGREVLLRVEKAPAEPGEV---VLEVENLS-VRDDRGV---PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2107 TGGEAFVNGHSVL-KDLLQVQQS-LGYCP---QFDALFDELTAREHLQLyTRLRGIP-----WKDEAQVVKWALEKLElt 2176
Cdd:COG3845 311 ASGSIRLDGEDITgLSPRERRRLgVAYIPedrLGRGLVPDMSVAENLIL-GRYRRPPfsrggFLDRKAIRAFAEELIE-- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2177 KY------ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEA 2250
Cdd:COG3845 388 EFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILA 467
|
250
....*....|...
gi 110225379 2251 LCTRLAIMVNGRL 2263
Cdd:COG3845 468 LSDRIAVMYEGRI 480
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2049-2270 |
1.55e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.96 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDL--LQVQ 2126
Cdd:PRK13548 2 MLEARNLSV-----RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWspAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQFDAL-FDeLTAREhlqlYTRLRGIPW----KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2201
Cdd:PRK13548 76 RRRAVLPQHSSLsFP-FTVEE----VVAMGRAPHglsrAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2202 ------GYPAFIFLDEPTTGMDPK--------ARRFLWnlildliKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2267
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAhqhhvlrlARQLAH-------ERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
...
gi 110225379 2268 SIQ 2270
Cdd:PRK13548 224 TPA 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
982-1198 |
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 110225379 982 PTHLPLVVCVDKLTKVYKN-DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMD 1059
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1060 EIRKNLGMCPQHNVLFDRlTVEEHLWFysRLKSMAQEEIRKETDK-----MIEDLEL-----SNKRHSLvqtLSGGMKRK 1129
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAY--GLQSCSFECVKEAAQKahahsFISELASgydteVGEKGSQ---LSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1130 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1198
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2068-2263 |
1.78e-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: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2068 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDElTAREH 2147
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2148 LqlytrlrGIPwkdeaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNL 2227
Cdd:cd03247 95 L-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 110225379 2228 ILDLIKtGRSVVLTSHSMEECEALcTRLAIMVNGRL 2263
Cdd:cd03247 141 IFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2067-2263 |
1.82e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2067 ILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLLQ-----VQQSLGYCPqfda 2137
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAagvaiIYQELHLVP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2138 lfdELTAREHL---QLYTRLrGipWKDEAQVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDE 2211
Cdd:PRK11288 93 ---EMTVAENLylgQLPHKG-G--IVNRRLLNYEAREQLEhlgVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2212 PTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2075-2264 |
2.05e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2075 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLLQVQ------QSLGYCPQFDALFDELTAREHL 2148
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2149 QLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2228
Cdd:PRK10584 110 ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 110225379 2229 LDLIKT-GRSVVLTSHSmEECEALCTRLAIMVNGRLR 2264
Cdd:PRK10584 190 FSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2073-2244 |
2.29e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2073 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkDLLQVQQSLGYCPQFDALFDELTAREHLQLYT 2152
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2153 RLRGipwKDEAQVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY-PAFIfLDEPTTGMDPKARRFLWNLILDL 2231
Cdd:PRK13539 99 AFLG---GEELDIAA-ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNrPIWI-LDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|...
gi 110225379 2232 IKTGRSVVLTSHS 2244
Cdd:PRK13539 174 LAQGGIVIAATHI 186
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2075-2263 |
2.35e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2075 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG-----HSVLKDLLQVQQSLGYCPQF--DALFDElTAREH 2147
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitsTSKNKDIKQIRKKVGLVFQFpeSQLFEE-TVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2148 LQLYTRLRGIPwKDEAQvvKWALEKLELTKYA----DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2223
Cdd:PRK13649 107 VAFGPQNFGVS-QEEAE--ALAREKLALVGISeslfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110225379 2224 LWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2062-2262 |
2.65e-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: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2062 RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVL---------KDLLQVQQSLg 2130
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKasnirdterAGIVIIHQEL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2131 ycpqfdALFDELTAREHLQLYTR--LRGIPWKDEAQVVKWA--LEKLELTKYAD-KPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:TIGR02633 88 ------TLVPELSVAENIFLGNEitLPGGRMAYNAMYLRAKnlLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2206 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2049-2250 |
3.25e-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: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDES---TTGGEAFVNGHSVlkDLLQV 2125
Cdd:COG4136 1 MLSLENLTITLGGRPL-----LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRL--TALPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQ-SLGYCPQFDALFDELTAREHLQLYTRlRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2204
Cdd:COG4136 74 EQrRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 2205 AFIFLDEPTTGMDP----KARRFLWNLILDLiktGRSVVLTSHSMEECEA 2250
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 ... |
2050-2243 |
3.48e-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: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILAvdrlcLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEafVNGHSVLKdllqvqqsL 2129
Cdd:cd03221 1 IELENLSKTYGGKLLLKDIS-----LTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--VTWGSTVK--------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFdalfdeltarehlqlytrlrgipwkdeaqvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03221 66 GYFEQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....
gi 110225379 2210 DEPTTGMDPKARRFLWNLildLIKTGRSVVLTSH 2243
Cdd:cd03221 95 DEPTNHLDLESIEALEEA---LKEYPGTVILVSH 125
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
989-1197 |
3.55e-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: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsatiyghdirtemdeirknlgmc 1068
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG----------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 pqhnvlfdrlTVEEHlwfysrlksmaqeeirketdkmiedlelSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:cd03221 56 ----------IVTWG----------------------------STVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1149 TAGVDPYARRAIWDLILKYKpgRTILLSTHhmDEA--DLLGDRIAIISHGK 1197
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2049-2263 |
3.72e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.84 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKS----RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---- 2120
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2121 -------DLLQV-QQSLG-YCPQFDAlfdELTAREHLQLYTRLrgipwkDEAQVVKWALEKLEL----TKYADKPAGTYS 2187
Cdd:TIGR02769 82 qrrafrrDVQLVfQDSPSaVNPRMTV---RQIIGEPLRHLTSL------DESEQKARIAELLDMvglrSEDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2188 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDpkarRFLWNLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
.
gi 110225379 2263 L 2263
Cdd:TIGR02769 229 I 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1005-1197 |
5.04e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE--MDEIRKNLGMCPQHNVLFDRLTVEE 1082
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLW----FYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1158
Cdd:PRK10762 99 NIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110225379 1159 AIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:PRK10762 179 SLFRVIRELKSqGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1009-1204 |
5.06e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.80 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1009 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMCPQHNVLFDRLTVEEHL 1084
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1085 WFYSRLKSMAQEEIRKETDKM-IEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1163
Cdd:PRK11831 106 AYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110225379 1164 I--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK11831 186 IseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1009-1179 |
5.16e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1009 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYS 1088
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1089 RLKSMAQEeirketDKMIEDLE---LSNKRHSLVQTLSGGMKRKlsVAIA--FVGGSRAIILDEP-----TAGVDPYARR 1158
Cdd:PRK13538 100 RLHGPGDD------EALWEALAqvgLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPftaidKQGVARLEAL 171
|
170 180
....*....|....*....|.
gi 110225379 1159 aiwdLILKYKPGRTILLSTHH 1179
Cdd:PRK13538 172 ----LAQHAEQGGMVILTTHQ 188
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
991-1217 |
8.27e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.98 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1069
Cdd:PRK11176 344 FRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRlTVEEHLwFYSRLKSMAQEEIRKETdKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSR 1141
Cdd:PRK11176 424 QNVHLFND-TIANNI-AYARTEQYSREQIEEAA-RMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1142 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP---LFLKGAYGDGYRL 1217
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGTHaelLAQNGVYAQLHKM 578
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2044-2264 |
9.28e-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: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2044 DADNDMVKIENLTKVY-KSRKIGRilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTGGEAFVNGHSV-LK 2120
Cdd:TIGR02633 252 EIGDVILEARNLTCWDvINPHRKR---VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2121 DLLQ-VQQSLGYCPQ---FDALFDELTAREH-----LQLYTRLRGIPWKDEAQVVKWALEKLEL-TKYADKPAGTYSGGN 2190
Cdd:TIGR02633 329 NPAQaIRAGIAMVPEdrkRHGIVPILGVGKNitlsvLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2191 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2264
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2080-2261 |
9.47e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2080 GECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLlqvQQSL-GYCPQ-------FDALFDELTAREHLQLY 2151
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAYVPQseevdwsFPVLVEDVVMMGRYGHM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 TRLRgIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2231
Cdd:PRK15056 110 GWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL 188
|
170 180 190
....*....|....*....|....*....|
gi 110225379 2232 IKTGRSVVLTSHSMEECEALCTrLAIMVNG 2261
Cdd:PRK15056 189 RDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1017-1178 |
1.07e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1017 QVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE-----IR-KNLGMCPQHNVLFDRLTVEEHLWFYSRL 1090
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-HQMDEearakLRaKHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1091 KSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYK 1168
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNRE 195
|
170
....*....|
gi 110225379 1169 PGRTILLSTH 1178
Cdd:PRK10584 196 HGTTLILVTH 205
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
705-911 |
1.12e-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: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 705 MMPLCMVISWVYSVAMTIQHIVAEKEHRLKEVMKTMGLNNAVHWVAWFITGFVqLSISVTALTAILKYGQVLMHSHVLII 784
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFL-VGLLQLLIILLLLFGIGIPFGNLGLL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 785 WLFLAVYAVATIMFCFLVSVLYSKAKLASACGGIIYFLSYVPYMYVAIREEVAHdkitaFEKCIASLMSTTAFGLGSKYF 864
Cdd:pfam12698 242 LLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPS-----FLQWIFSIIPFFSPIDGLLRL 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110225379 865 ALYEVAgvgiqwhtfsqspvegddFNLLLAVTMLMVDTVVYGVLTWY 911
Cdd:pfam12698 317 IYGDSL------------------WEIAPSLIILLLFAVVLLLLALL 345
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2065-2263 |
1.31e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2065 GRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-----DESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDAL 2138
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2139 FDELTAREHLQLYTRL-RGIPWKDEAQV-VKWALEKLEL----TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEP 2212
Cdd:PRK14247 94 IPNLSIFENVALGLKLnRLVKSKKELQErVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2213 TTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1004-1191 |
1.79e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1004 MALNKLSLNLYENQVVSFLGHNGAGKTTTMSI---LTGLFPP--TSGSATIYGHDIR-TEMD--EIRKNLGMCPQHNVLF 1075
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYaPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DRlTVEEHLWFYSRLKSMaqeeiRKETDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1147
Cdd:PRK14243 104 PK-SIYDNIAYGARINGY-----KGDMDELVERSlrqaalwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110225379 1148 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIA 1191
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2082-2263 |
2.44e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.18 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2082 CFGLLGVNGAGKTS---TFKMLT--GDESTTGGEAFVNGHSVLK---DLLQVQQSLGYCPQFDALFDELTAREHLQLYTR 2153
Cdd:PRK14267 32 VFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2154 LRGI--PWKDEAQVVKWALEKLEL-----TKYADKPaGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2226
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 110225379 2227 LILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK14267 191 LLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2047-2263 |
2.69e-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: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQVQ 2126
Cdd:PRK11614 3 KVMLSFDKVSAHY-----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDITDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 ------QSLGYCPQFDALFDELTAREHLQLytrlrGIPWKDEAQV---VKWALEKL-ELTKYADKPAGTYSGGNKRKLST 2196
Cdd:PRK11614 74 takimrEAVAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFqerIKWVYELFpRLHERRIQRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2197 AIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
989-1180 |
3.17e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYKNDKkMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMdeiRKNL-GM 1067
Cdd:PRK15056 7 IVVNDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1068 CPQ-HNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIED-----LELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSR 1141
Cdd:PRK15056 83 VPQsEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTaalarVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110225379 1142 AIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHM 1180
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNL 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2085-2272 |
3.45e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2085 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQF--DALFDElTAREHLQLYTRLRGIPWKD 2161
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRKFVGLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2162 EAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVL 2240
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIF 193
|
170 180 190
....*....|....*....|....*....|..
gi 110225379 2241 TSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2272
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
991-1198 |
5.03e-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: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVY-------KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMD 1059
Cdd:TIGR02769 5 VRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1060 EIRKNLGMCPQ--HNVLFDRLTVE----EHLWFYSRLKSMAQEEirkETDKMIEDLEL-SNKRHSLVQTLSGGMKRKLSV 1132
Cdd:TIGR02769 85 AFRRDVQLVFQdsPSAVNPRMTVRqiigEPLRHLTSLDESEQKA---RIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1133 AIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2046-2263 |
5.10e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.58 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2046 DNDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFK----MLTGDESTTGGEAFVNGHSV--- 2118
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGDKKnnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2119 ----------LKDLLQVQQSLGYCPQFD--ALFDElTAREHLQLYTRLRGIPWKDEAQVVKWALEKLEL-TKYADKPAGT 2185
Cdd:PRK13631 98 elitnpyskkIKNFKELRRRVSMVFQFPeyQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2186 YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1005-1198 |
5.62e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCPQHNVLFDRLTVEE 1082
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLW---FYSRL----KSMAQEEIRKETDKMIEDLELSNKrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDpy 1155
Cdd:PRK11288 99 NLYlgqLPHKGgivnRRLLNYEAREQLEHLGVDIDPDTP----LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110225379 1156 AR------RAIWDLilkYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK11288 173 AReieqlfRVIREL---RAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
994-1207 |
5.64e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 994 LTKVYKNDKKMALNK-LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatIYGHDIRteMDEI---RKNLGMCP 1069
Cdd:PRK11000 6 LRNVTKAYGDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD--LFIGEKR--MNDVppaERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1150 AGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1207
Cdd:PRK11000 162 SNLDAALRVQMRIEIsrLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2080-2274 |
6.36e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2080 GECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKDLLQVQQSLGYCPQFDALFDELTAREHL-QLY 2151
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNLiEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 TRLRGIpwkDEAQVVKWA---LEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2228
Cdd:PRK11124 108 CRVLGL---SKDQALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110225379 2229 LDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2274
Cdd:PRK11124 185 RELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2069-2244 |
6.97e-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: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREH 2147
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2148 LQLytrlrGIPWKDEAQVVkWALEKLELTKY-ADKPAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2216
Cdd:TIGR02868 429 LRL-----ARPDATDEELW-AALERVGLADWlRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*...
gi 110225379 2217 DPKARRFLWNLILDlIKTGRSVVLTSHS 2244
Cdd:TIGR02868 503 DAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2049-2263 |
9.44e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 9.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYksrkIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLLQ 2124
Cdd:PRK10908 1 MIRFEHVSKAY----LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2204
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2205 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2049-2262 |
9.54e-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: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--------K 2120
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2121 DLLQVQQ--SLGYCPqfdalfdELTAREHLQL-YTR--LRGIPW---KDEAQVVKWALEKLE--LTKYADKPAGTYSGGN 2190
Cdd:COG1101 81 YIGRVFQdpMMGTAP-------SMTIEENLALaYRRgkRRGLRRgltKKRRELFRELLATLGlgLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2191 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRsvvLTS----HSMEECEALCTRLAIMVNGR 2262
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEGR 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1001-1191 |
1.01e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1001 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTS-----GSATIYGHDI---RTEMDEIRKNLGMC-PQH 1071
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLNRLRRQVSMVhPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 NvLFDrLTVEEHLWFYSRLKSMAQE-EIRKETDKMIEDLEL----SNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:PRK14258 98 N-LFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110225379 1147 EPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIA 1191
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
997-1198 |
1.27e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 997 VYKNDKKMALNkLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQH--- 1071
Cdd:PRK09700 271 VTSRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrd 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 NVLFDRLTVEEHLWFYSRLKS---------MAQEEIRKETDKMIEDLELsnKRHSLVQT---LSGGMKRKLSVAIAFVGG 1139
Cdd:PRK09700 350 NGFFPNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELLAL--KCHSVNQNiteLSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1140 SRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
2073-2246 |
1.28e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2073 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKDLLQVQQSLGYC---PQFDALFDELTARE 2146
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2147 HLQLytRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2226
Cdd:PRK13638 100 AFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180
....*....|....*....|
gi 110225379 2227 LILDLIKTGRSVVLTSHSME 2246
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDID 197
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2050-2271 |
1.46e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL-----KDLLQ 2124
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQF--DALFDElTAREHLQLYTRLRGIPwKDEA--QVVKWaLEKLEL-TKYADKPAGTYSGGNKRKLSTAIA 2199
Cdd:PRK13641 83 LRKKVSLVFQFpeAQLFEN-TVLKDVEFGPKNFGFS-EDEAkeKALKW-LKKVGLsEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2200 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLrclgsIQH 2271
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL-----IKH 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
1009-1204 |
1.60e-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: 69.32 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1009 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP----TSGSATIYGHDIrTEMDEIRKNLGMCPQH-----NVLFdrlT 1079
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL-LPLSIRGRHIATIMQNprtafNPLF---T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1080 VEEHLwfysRLKSMAQEEIRKE-TDKMIEDLELSNKRHS--LVQT----LSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1152
Cdd:TIGR02770 81 MGNHA----IETLRSLGKLSKQaRALILEALEAVGLPDPeeVLKKypfqLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1153 DPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:TIGR02770 157 DVVNQARVLKLLreLRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
980-1198 |
1.71e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 980 EEPTHL----PLVVcvDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsATIYGhdiR 1055
Cdd:PRK11247 2 MNTARLnqgtPLLL--NAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---T 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1056 TEMDEIRKNLGMCPQHNVLFDRLTVEEHL-------WfysrlksmaqeeiRKETDKMIEDLELSNKRHSLVQTLSGGMKR 1128
Cdd:PRK11247 74 APLAEAREDTRLMFQDARLLPWKKVIDNVglglkgqW-------------RDAALQALAAVGLADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1129 KLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2079-2263 |
1.87e-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: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2079 PGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKDLLQVQQSLGYCPQFDALFDELTAREHL-QL 2150
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVFQQYNLWPHLTVMENLiEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2151 YTRLRGIPwKDEAQV-VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2229
Cdd:COG4161 107 PCKVLGLS-KEQAREkAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIR 185
|
170 180 190
....*....|....*....|....*....|....
gi 110225379 2230 DLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:COG4161 186 ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1006-1204 |
1.92e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGMCPQHNVL---FD-RLTV 1080
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDTSLsfeFDvRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1081 E----EHLwfySRLKSMAQEEiRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDpyA 1156
Cdd:PRK09536 99 EmgrtPHR---SRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1157 RRAIWDLILKYK---PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK09536 173 NHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1000-1199 |
2.04e-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: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1000 NDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT-SGSATIYGH--DIRTEMDEIRKNLGMCPQ------ 1070
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrhg 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 --------HNVlfdRLTVEEHLWFYSRLKSMAQEEIrkeTDKMIEDLELSNKRHSL-VQTLSGGMKRKLSVAIAFVGGSR 1141
Cdd:TIGR02633 350 ivpilgvgKNI---TLSVLKSFCFKMRIDAAAELQI---IGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1142 AIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1199
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
991-1198 |
2.15e-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: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE---------MDEI 1061
Cdd:PRK11264 6 VKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1062 RKNLGMCPQHNVLFDRLTVEEHLWFYSRL-KSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1140
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1141 RAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2049-2268 |
2.28e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.02 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKDLLQVQ 2126
Cdd:PRK13644 1 MIRLENVSYSYPDGTP----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:PRK13644 77 KLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2206 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGS 2268
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2070-2263 |
2.45e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2070 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllQVQQSLGYCPQF-------DALFDEL 2142
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR--SPQDGLANGIVYisedrkrDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2143 TAREHLQLyTRLR-------GIPWKDEAQVVKWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2214
Cdd:PRK10762 346 SVKENMSL-TALRyfsraggSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110225379 2215 GMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1005-1197 |
2.56e-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: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIY--GHDIRTE--MDEIRKNLGMCPQHNVLFDRLTV 1080
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLKASniRDTERAGIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1081 EEHLWFYSRL----KSMAQEEIRKETDKMIEDLELSNKRHSL-VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1155
Cdd:TIGR02633 96 AENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110225379 1156 ARRAIWDLI--LKYKPGRTILLStHHMDEADLLGDRIAIISHGK 1197
Cdd:TIGR02633 176 ETEILLDIIrdLKAHGVACVYIS-HKLNEVKAVCDTICVIRDGQ 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
986-1187 |
3.10e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 986 PLVVCvDKLTKVYKNDKKMA--LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMD 1059
Cdd:PRK11629 4 ILLQC-DNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1060 EIRKN-LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVG 1138
Cdd:PRK11629 83 ELRNQkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1139 GSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLG 1187
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2068-2260 |
4.01e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.01 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2068 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLLQ---------VQQSLGYCPQ 2134
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLRKhigivfqnpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2135 FDALFDeltAREHLqlytrlrgIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2214
Cdd:PRK13648 103 YDVAFG---LENHA--------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110225379 2215 GMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVN 2260
Cdd:PRK13648 172 MLDPDARQNLLDLVRKV-KSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
991-1199 |
4.87e-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: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATiyghdirtemdeIRKNL--GMC 1068
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS------------IPKGLriGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDRLTVEEHLW--FYSRLKSMAQ-EEIRKETDKMIEDL----ELSNK--------------------------R 1115
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgDAELRALEAElEELEAKLAEPDEDLerlaELQEEfealggweaearaeeilsglgfpeedL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1116 HSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRaiW--DLILKYkPGrTILLSTH--H-MDEadlLGDRI 1190
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNY-PG-TVLVVSHdrYfLDR---VATRI 219
|
....*....
gi 110225379 1191 AIISHGKLK 1199
Cdd:COG0488 220 LELDRGKLT 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2037-2263 |
5.42e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2037 RQRVLRGDADNDMVKIENLTkvykSRKIGRilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH 2116
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT----SRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2117 --SVLKDLLQVQQSLGYCPQF---DALFDELTAREHLQLYTRLRGIPWK---------DEAQVVKWALEKLELTKYA-DK 2181
Cdd:PRK09700 326 diSPRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKDGGYKgamglfhevDEQRTAENQRELLALKCHSvNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2182 PAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2261
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
..
gi 110225379 2262 RL 2263
Cdd:PRK09700 486 RL 487
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1005-1196 |
8.53e-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: 67.07 E-value: 8.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSaTIYGHDIRT---------EMDEIRKN-LGMCPQH-NV 1073
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS-ILVRHDGGWvdlaqasprEILALRRRtIGYVSQFlRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1074 LfDRLT----VEEHLwfysRLKSMAQEEIRKETDKMIEDLELSNKRHSLV-QTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:COG4778 105 I-PRVSaldvVAEPL----LERGVDREEARARARELLARLNLPERLWDLPpATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110225379 1149 TAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHG 1196
Cdd:COG4778 180 TASLDAANRAVVVELIEEAKArGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2047-2310 |
9.68e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.20 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLtkVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL-KDLLQV 2125
Cdd:PRK13642 2 NKILEVENL--VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2204
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2205 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMIT 2283
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSEDMVEIG 238
|
250 260
....*....|....*....|....*..
gi 110225379 2284 VRTKSSQNVKDVVRFFNRNFPEAMLKE 2310
Cdd:PRK13642 239 LDVPFSSNLMKDLRKNGFDLPEKYLSE 265
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2083-2282 |
1.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.38 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2083 FGLLGVNGAGKTSTFKMLT------GDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDELTAREHLQLYTRLR 2155
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2156 GIPWKDE-AQVVKWALEKLELTKYA----DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2230
Cdd:PRK14246 119 GIKEKREiKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2231 LiKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRFGDGYMI 2282
Cdd:PRK14246 199 L-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2050-2270 |
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 110225379 2050 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdLLQVQQSL 2129
Cdd:PRK10851 3 IEIANIKKSF-----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-LHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLytRLRGIPWKDEA------QVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAF--GLTVLPRRERPnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2204 PAFIFLDEPTTGMDPKA----RRFLWNLILDLIKTGrsvVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2270
Cdd:PRK10851 155 PQILLLDEPFGALDAQVrkelRRWLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
974-1202 |
1.37e-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: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 974 ETRGMEEEPTHLP-----LVVcvDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAT 1048
Cdd:COG4618 313 AAVPAEPERMPLPrpkgrLSV--ENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1049 IYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHLwfySRLKSMAQEEI-----RKETDKMIedLELSNKRHSLV--- 1119
Cdd:COG4618 391 LDGADLSQwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDADPEKVvaaakLAGVHEMI--LRLPDGYDTRIgeg 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1120 -QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMdeaDLLG--DRIAIIS 1194
Cdd:COG4618 465 gARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIraLKAR-GATVVVITHRP---SLLAavDKLLVLR 540
|
....*...
gi 110225379 1195 HGKLKCCG 1202
Cdd:COG4618 541 DGRVQAFG 548
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1005-1197 |
1.46e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQHNVLFDRLTVEE 1082
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLWF--YSrLKSM--AQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1158
Cdd:PRK10982 93 NMWLgrYP-TKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110225379 1159 AIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:PRK10982 172 HLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2043-2246 |
1.64e-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: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2043 GDADNDMVKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDL 2122
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYP----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2123 LQ--VQQSLGYCPQFDALFdELTAREHLQLYTrlrgiPWKDEAQVVKwALEKLELTKY-ADKPAGTY----------SGG 2189
Cdd:TIGR02857 390 DAdsWRDQIAWVPQHPFLF-AGTIAENIRLAR-----PDASDAEIRE-ALERAGLDEFvAALPQGLDtpigeggaglSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2190 NKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSME 2246
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2052-2268 |
1.82e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2052 IENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV------LKDLLQV 2125
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQFD--ALFDELTARE------HLQlytrlrgipwKDEAQVVKWALEKLELTK----YADKPAGTYSGGNKRK 2193
Cdd:PRK13645 89 RKEIGLVFQFPeyQLFQETIEKDiafgpvNLG----------ENKQEAYKKVPELLKLVQlpedYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2194 LSTA--IALIGYPafIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:PRK13645 159 VALAgiIAMDGNT--LVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
978-1198 |
2.23e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 978 MEEEPTHLPLVVCVDKLTKVYKNdkKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE 1057
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1058 MDEIRKNLG--MCPQHNVLFDRLTVEEHLWF--------YSRLKSMAQE-EIRKETDKMIEDLELSNKRhsLVQTLSGGM 1126
Cdd:PRK15439 79 TPAKAHQLGiyLVPQEPLLFPNLSVKENILFglpkrqasMQKMKQLLAAlGCQLDLDSSAGSLEVADRQ--IVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 1127 KRklsvaiafvggSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK15439 157 RD-----------SRILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1006-1198 |
2.33e-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: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMDE--IRKNLGMCPQHNVLFDRlTVEEH 1083
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHhyLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1084 LWFysRLKSMAQEEIRKETDKMIED---LELSNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1156
Cdd:TIGR00958 575 IAY--GLTDTPDEEIMAAAKAANAHdfiMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110225379 1157 RRAIWDliLKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1198
Cdd:TIGR00958 653 EQLLQE--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSV 691
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
992-1198 |
2.35e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 992 DKLTKVYKNdKKMalnKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDiRTEMDEIRKNLGMCPQH 1071
Cdd:PRK10771 5 TDITWLYHH-LPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 NVLFDRLTVEEH--LWFYSRLKSMAQEeiRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:PRK10771 80 NNLFSHLTVAQNigLGLNPGLKLNAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1150 AGVDPYARRAIWDLILKYKPGR--TILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
986-1197 |
2.42e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 986 PLVVcVDKLTKVYKNDKkmALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE- 1060
Cdd:PRK11701 5 PLLS-VRGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLrdlyALSEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1061 -----IRKNLGMCPQHNVLFDRLTVE------EHLwfysrlksMAQ-----EEIRKETDKMIEDLELSNKR-HSLVQTLS 1123
Cdd:PRK11701 82 errrlLRTEWGFVHQHPRDGLRMQVSaggnigERL--------MAVgarhyGDIRATAGDWLERVEIDAARiDDLPTTFS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1124 GGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1197
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
998-1196 |
2.52e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-RKNLGMCPQHNVLFD 1076
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 RlTVEEHLWFYSRLKSMAQEEirketDKMIEDL-------ELSNKRhslVQTLSGGMKRKLSVA--IAFVggSRAIILDE 1147
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQPDP-----AIFLDDLerfalpdTILTKN---IAELSGGEKQRISLIrnLQFM--PKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1148 PTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1196
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2051-2262 |
2.58e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEA-FVNGHSVLKDLLQVQQS- 2128
Cdd:PRK11701 8 SVRGLTKLY-----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 --------LGYCPQF--DALFDELTA----REHL-----QLYTRLRgipwkdeAQVVKWaLEKLEL--TKYADKPAgTYS 2187
Cdd:PRK11701 83 rrrllrteWGFVHQHprDGLRMQVSAggniGERLmavgaRHYGDIR-------ATAGDW-LERVEIdaARIDDLPT-TFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2188 GGNKRKLSTAIALIGYPAFIFLDEPTTGMD--PKARrflwnlILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVN 2260
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR------LLDLLRGlvrelGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
..
gi 110225379 2261 GR 2262
Cdd:PRK11701 228 GR 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1006-1204 |
2.60e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDE--------------IRKNLGMCPQH 1071
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrlLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 NVLFDRLTVEEHLWFYS-RLKSMAQEEIRKETDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:PRK10619 101 FNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1150 AGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
998-1186 |
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 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL-----TGLFppTSGSATIYGHDIRTEMDEIrknLGMCPQHN 1072
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRS---IGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1073 VLFDRLTVEEHLWFYSRL---KSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGM----KRKLSVAIAFVGGSRAII- 1144
Cdd:TIGR00956 846 LHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225379 1145 LDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHH-----MDEADLL 1186
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQpsailFEEFDRL 973
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1006-1198 |
4.00e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.60 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEI----RKNLGMCPQHNVLFDRLTV 1080
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaqlrREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1081 EEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1160
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110225379 1161 WDlILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1198
Cdd:PRK10535 184 MA-ILHQlrDRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2052-2263 |
4.01e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.85 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2052 IENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEafvnghsvlkdLLQVQQSLGy 2131
Cdd:PRK11247 15 LNAVSKRYGERTV-----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-----------LLAGTAPLA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2132 cpqfdalfdelTAREHlqlyTRL-----RGIPWKDEAQVV------KW---ALEKLELTKYADK----PAgTYSGGNKRK 2193
Cdd:PRK11247 78 -----------EARED----TRLmfqdaRLLPWKKVIDNVglglkgQWrdaALQALAAVGLADRanewPA-ALSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2194 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2049-2263 |
4.03e-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: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKIgrILAVDrlcLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--------LK 2120
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV--LHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2121 DLL-QVQQSLGYCPQFDALFDELTAREH-LQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAI 2198
Cdd:PRK11264 78 GLIrQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2199 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
991-1235 |
4.08e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKkMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1069
Cdd:PRK10790 343 IDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNV-----LFDRLTV-----EEHLWFYSRLKSMAqEEIRKETDKMIEDL-ELSNkrhslvqTLSGGMKRKLSVAIAFVG 1138
Cdd:PRK10790 422 QDPVvladtFLANVTLgrdisEEQVWQALETVQLA-ELARSLPDGLYTPLgEQGN-------NLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1139 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP---LFLKGAYG 1212
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHqqlLAAQGRYW 569
|
250 260
....*....|....*....|...
gi 110225379 1213 DGYRLTLVKQPAEPGTSQEPGLA 1235
Cdd:PRK10790 570 QMYQLQLAGEELAASVREEESLS 592
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1017-1179 |
4.43e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1017 QVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDiRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRL---KSM 1093
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1094 AQEEIRKETDKMIEDLELSNKRH-----SLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY-ARRAIWDLILKY 1167
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATaAYRLVLTLGSLA 253
|
170
....*....|..
gi 110225379 1168 KPGRTILLSTHH 1179
Cdd:PLN03211 254 QKGKTIVTSMHQ 265
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2079-2243 |
4.43e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2079 PGECFGLLGVNGAGKTSTFKMLTGDESTTG--GEAFVNGHSVLKdllQVQQSLGYCPQFDALFDELTAREHLQLYTRLR- 2155
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVFCSLLRl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2156 --GIPWKDEAQVVKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2228
Cdd:PLN03211 170 pkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*
gi 110225379 2229 LDLIKTGRSVVLTSH 2243
Cdd:PLN03211 250 GSLAQKGKTIVTSMH 264
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2047-2275 |
4.85e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ-V 2125
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGT----KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQF--DALFdELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:PRK13647 78 RSKVGLVFQDpdDQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNR 2275
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2069-2261 |
4.90e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLLQVQQS-LGYCPQFDALFDELTARE 2146
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtFNGPKSSQEAgIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2147 HLQL----YTRLRGIPWK---DEAQVVkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2219
Cdd:PRK10762 99 NIFLgrefVNRFGRIDWKkmyAEADKL---LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110225379 2220 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2261
Cdd:PRK10762 176 ETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1009-1198 |
5.06e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1009 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC------PQHNVLFDR----- 1077
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 ---LTVEEHLWFYSRlksmAQEEIRKETDKMIEDLELSNKRHSlVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1154
Cdd:PRK15439 362 vcaLTHNRRGFWIKP----ARENAVLERYRRALNIKFNHAEQA-ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 1155 YARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK15439 437 SARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1002-1198 |
5.26e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.06 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1002 KKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTV 1080
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1081 EEHLwfysRL-KSMAQEEIRKETDKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1151
Cdd:PRK13657 426 EDNI----RVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgergrqLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1152 VDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKL 1198
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNGRV 547
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2072-2263 |
5.59e-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: 64.44 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2072 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkdllqvqQSLGYCP----------QFDALFDE 2141
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-----------VDVTAAPpadrpvsmlfQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2142 LTAREH--LQLYTRLRGIPwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2219
Cdd:cd03298 85 LTVEQNvgLGLSPGLKLTA--EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 2220 ARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:cd03298 163 LRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2047-2263 |
6.09e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.81 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVnGHSVLKD--LLQ 2124
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT---YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEetVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:PRK13635 79 VRRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2263
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEI 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
991-1204 |
6.46e-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: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1069
Cdd:cd03369 9 VENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRlTVEEHLWFYSRlksMAQEEIRketdkmiEDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:cd03369 89 QDPTLFSG-TIRSNLDPFDE---YSDEEIY-------GALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 1150 AGVDPYARRAIWDLILKYKPGRTILLSTHHMDE-ADLlgDRIAIISHGKLKCCGSP 1204
Cdd:cd03369 154 ASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVKEYDHP 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2069-2272 |
7.12e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKDLLQVQ--QSLGYCPQFDALFDElTARE 2146
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-IADYSEAAlrQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2147 HLQLytrlrGIPWKDEAQVVKwALEKLELTKYADKPAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2216
Cdd:PRK11160 433 NLLL-----AAPNASDEALIE-VLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2217 DPKARRFLWNLILDLIKtGRSVVLTSH---SMEECEALCtrlaIMVNGRLRCLGSIQHL 2272
Cdd:PRK11160 507 DAETERQILELLAEHAQ-NKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQEL 560
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2047-2269 |
7.47e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.22 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTK---VYKSRKiGRI-------------LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2110
Cdd:PRK13546 2 NVSVNIKNVTKeyrIYRTNK-ERMkdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2111 AFVNGhsvlkDLLQVQQSLGycpqfdaLFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGN 2190
Cdd:PRK13546 81 VDRNG-----EVSVIAISAG-------LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2191 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2269
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2051-2264 |
7.84e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLT---KVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGdeSTTG---GEAFVNGHSV-LKDLL 2123
Cdd:PRK13549 261 EVRNLTawdPVNPHIKR-----VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGrweGEIFIDGKPVkIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 Q-VQQSLGYCPQ---FDALFDELTAREH-----LQLYTRLRGIPWKDEAQVVKWALEKLEL-TKYADKPAGTYSGGNKRK 2193
Cdd:PRK13549 334 QaIAQGIAMVPEdrkRDGIVPVMGVGKNitlaaLDRFTGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQK 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2194 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2264
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2085-2243 |
8.36e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2085 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLqlytrLRGIPWKDEAQ 2164
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC-----LYDIHFSPGAV 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2165 VVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2243
Cdd:PRK13540 107 GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2017-2267 |
8.38e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2017 PQRLPVSTKPVEDDVDVASERQRVLRGDAdndMVKIENLTKVYKSR-----KIGR-ILAVDRLCLGVRPGECFGLLGVNG 2090
Cdd:PRK10261 284 PRRFPLISLEHPAKQEPPIEQDTVVDGEP---ILQVRNLVTRFPLRsgllnRVTReVHAVEKVSFDLWPGETLSLVGESG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2091 AGKTSTFKMLTGDESTTGGEAFVNGHSVlkDLLQVQ--QSLGYCPQFdaLFDELTAR------------EHLQLYTRLRG 2156
Cdd:PRK10261 361 SGKSTTGRALLRLVESQGGEIIFNGQRI--DTLSPGklQALRRDIQF--IFQDPYASldprqtvgdsimEPLRVHGLLPG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2157 ipwKDEAQVVKWALEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT- 2234
Cdd:PRK10261 437 ---KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDf 513
|
250 260 270
....*....|....*....|....*....|...
gi 110225379 2235 GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2267
Cdd:PRK10261 514 GIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1006-1179 |
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 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLW 1085
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1086 FYSRLKSMAQeeirkETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLIL 1165
Cdd:PRK13540 97 YDIHFSPGAV-----GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*
gi 110225379 1166 KY-KPGRTILLSTHH 1179
Cdd:PRK13540 172 EHrAKGGAVLLTSHQ 186
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2050-2262 |
1.27e-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: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkdllqvqqSL 2129
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQ--------------FDALFDEltarehlQLYtrlrgipwkdeAQVVK-WALEK-LELTkyadkPAG--------- 2184
Cdd:cd03250 69 AYVSQepwiqngtirenilFGKPFDE-------ERY-----------EKVIKaCALEPdLEIL-----PDGdlteigekg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2185 -TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLW-NLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGR 2262
Cdd:cd03250 126 iNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1005-1197 |
1.28e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIY-------GHDIR-TEmdeiRKNLGMCPQHNVLFD 1076
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfegeelqASNIRdTE----RAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 RLTVEEHLWF---YSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:PRK13549 96 ELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110225379 1154 PYARRAIWDLI--LKYKPGRTILLStHHMDEADLLGDRIAIISHGK 1197
Cdd:PRK13549 176 ESETAVLLDIIrdLKAHGIACIYIS-HKLNEVKAISDTICVIRDGR 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2077-2217 |
2.15e-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: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTG---GEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLYTR 2153
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2154 LRGipwkdeAQVVKwalekleltkyadkpagTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD 2217
Cdd:cd03233 110 CKG------NEFVR-----------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2054-2263 |
2.19e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2054 NLTKVYKSRKIGRILAVDrLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV------LKDLLQVQQ 2127
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHN-VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 sLGYCPQFDALFDELTAREHLQLYTRLRGipwKDEAQVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIGYP 2204
Cdd:PRK11629 89 -LGFIYQFHHLLPDFTALENVAMPLLIGK---KKPAEINSRALEMLAavgLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2205 AFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAiMVNGRL 2263
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1010-1198 |
2.51e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1010 SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLGMCPQhnvlfDR--------LT 1079
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPE-----DRkaegiipvHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1080 VEE---------HLWFYSRLKSmAQEeiRKETDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:PRK11288 348 VADninisarrhHLRAGCLINN-RWE--AENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 1150 AGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1006-1207 |
2.61e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRLTVEE-- 1082
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRElv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 ----HLWfYSRLKSMAQEEiRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1158
Cdd:PRK10575 107 aigrYPW-HGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1159 AIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1207
Cdd:PRK10575 185 DVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2077-2291 |
2.82e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLG-Y-CPQFDALFDELTAREHLqlytrL 2154
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYlVPQEPLLFPNLSVKENI-----L 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2155 RGIPWKDEA-QVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK 2233
Cdd:PRK15439 109 FGLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2234 TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIqhlkNRFGDGYMITVRTKSSQN 2291
Cdd:PRK15439 189 QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT----ADLSTDDIIQAITPAARE 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
994-1153 |
3.05e-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: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 994 LTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT---SGSATIYGHDIRTEMDEIRKNLGMCPQ 1070
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEEHLWFYSRLKSmaqeeirketdkmiedlelsnkrHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
...
gi 110225379 1151 GVD 1153
Cdd:cd03233 148 GLD 150
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
992-1204 |
3.35e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 992 DKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQ 1070
Cdd:PRK10253 11 EQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 HNVLFDRLTVEE--------HLWFYSRLKSMAQEEIRKETDKM-IEDLELSNkrhslVQTLSGGMKRKLSVAIAFVGGSR 1141
Cdd:PRK10253 89 NATTPGDITVQElvargrypHQPLFTRWRKEDEEAVTKAMQATgITHLADQS-----VDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1142 AIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2049-2263 |
4.95e-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: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkDLLQ---- 2124
Cdd:COG4181 8 IIELRGLTKTVGTGA-GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ----DLFAlded 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 ------------VQQSlgycpqFDaLFDELTAREHLQLYTRLRGIPwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKR 2192
Cdd:COG4181 83 ararlrarhvgfVFQS------FQ-LLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2193 KLSTAIALIGYPAFIFLDEPTTGMDPKARRflwnLILDLI-----KTGRSVVLTSHSmEECEALCTRLAIMVNGRL 2263
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGE----QIIDLLfelnrERGTTLVLVTHD-PALAARCDRVLRLRAGRL 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2054-2262 |
5.37e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2054 NLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSV----LKDLLQ--- 2124
Cdd:PRK13549 10 NITK-----TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGEELqasnIRDTERagi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 --VQQSLgycpqfdALFDELTAREHLQL---YTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2199
Cdd:PRK13549 85 aiIHQEL-------ALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2200 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1006-1204 |
5.87e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFpPTSGSATIYGHDIRT----EMDEIRKNLgmCPQHNVLFDRltve 1081
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYL--SQQQTPPFAM---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1082 eHLWFY---SRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI-------ILDEPTAG 1151
Cdd:PRK03695 85 -PVFQYltlHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 1152 VDpYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1204
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 ... |
2068-2277 |
5.90e-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: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2068 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLLQVQQSLGYCPQFDALFDElTARE 2146
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2147 HLQLYTrlRGIPWKDEAQVVKWA-----LEKLEL---TKYADKPAGtYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2218
Cdd:cd03252 95 NIALAD--PGMSMERVIEAAKLAgahdfISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2219 KARRFLWNLILDlIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2277
Cdd:cd03252 172 ESEHAIMRNMHD-ICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2077-2263 |
6.95e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG-----HSVLKDL-------LQVQQSLGYCPQFDALFDELTA 2144
Cdd:PRK10982 271 LHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnHNANEAInhgfalvTEERRSTGIYAYLDIGFNSLIS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2145 --REHLQLYTRLRGIPWKDEAQvvkWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKAR 2221
Cdd:PRK10982 351 niRNYKNKVGLLDNSRMKSDTQ---WVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAK 427
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110225379 2222 RFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK10982 428 FEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2050-2263 |
9.13e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.41 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG------------------DESTTGGEA 2111
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2112 FVNGHSV-------LKDLLQVQQSLGYCPQFD--ALFDElTAREHLQLYTRLRGIPwKDEAQvvKWALEKLELT----KY 2178
Cdd:PRK13651 83 VLEKLVIqktrfkkIKKIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVS-KEEAK--KRAAKYIELVgldeSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2179 ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIM 2258
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*
gi 110225379 2259 VNGRL 2263
Cdd:PRK13651 239 KDGKI 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2053-2268 |
9.77e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2053 ENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGY 2131
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVE-----IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2132 CPQF-----DALFDELTAR---EHLQLYTRLRgipwKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:PRK10253 86 LAQNattpgDITVQELVARgryPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2047-2249 |
1.27e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.74 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVL-KDL 2122
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKP---ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTaKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2123 LQVQQSLGYCPQF-DALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2201
Cdd:PRK13640 80 WDIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110225379 2202 GYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECE 2249
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN 208
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
999-1178 |
1.35e-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: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 999 KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL-----TGLfppTSGSATIYGHDIRtemDEIRKNLGMCPQHNV 1073
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLD---KNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1074 LFDRLTVEEHLWFYSRLKSMAQEEirketdkmiedlelsnkrhslvqtlsggmKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:cd03232 90 HSPNLTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*.
gi 110225379 1154 PYARRAIWDLILKY-KPGRTILLSTH 1178
Cdd:cd03232 141 SQAAYNIVRFLKKLaDSGQAILCTIH 166
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2049-2280 |
1.48e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.25 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllqvQQS 2128
Cdd:PRK11248 1 MLQISHLYADYGGKP-----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP----GAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:PRK11248 72 RGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 2209 LDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLgsiQHLKNRFGDGY 2280
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWqETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRF 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2077-2255 |
1.58e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDllQVQQSLGYCPQFDALFDELTAREHLQLYTRLRG 2156
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2157 ipwKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGR 2236
Cdd:PRK13543 112 ---RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGG 188
|
170
....*....|....*....
gi 110225379 2237 SVVLTSHSMEECEALCTRL 2255
Cdd:PRK13543 189 AALVTTHGAYAAPPVRTRM 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1003-1199 |
1.70e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1003 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyghdirtemdeIRKNLGMCPQHNVLFDRlTVEE 1082
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLWFYSRLKSmaqEEIRKETD--KMIEDLELSnKRHSLVQ------TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1154
Cdd:PLN03232 698 NILFGSDFES---ERYWRAIDvtALQHDLDLL-PGRDLTEigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110225379 1155 YARRAIWDLILKYK-PGRTILLSTHHMDEADLLgDRIAIISHGKLK 1199
Cdd:PLN03232 774 HVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1003-1198 |
1.99e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1003 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSG-----SATIYGHDIRTEMD--EIRKNLGMCPQHNVLF 1075
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1076 DRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQT----LSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1151
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110225379 1152 VDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1006-1178 |
2.10e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatiyghdIRTEmDEIRknLGMCPQhNVLFDR---LTVEE 1082
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRN-GKLR--IGYVPQ-KLYLDTtlpLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1083 HLwfysRLKSMAQEeirketDKMIEDLELSNKRHSL---VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1159
Cdd:PRK09544 89 FL----RLRPGTKK------EDILPALKRVQAGHLIdapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|.
gi 110225379 1160 IWDLI--LKYKPGRTILLSTH 1178
Cdd:PRK09544 159 LYDLIdqLRRELDCAVLMVSH 179
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2049-2263 |
2.14e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT--GD---ESTTGGEAFVNGHSVLK--- 2120
Cdd:PRK14239 5 ILQVSDLSVYYNKKK-----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNIYSprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2121 DLLQVQQSLGYCPQFDALFdELTAREHLQLYTRLRGIpwKDEaQVVKWALEKL--------ELTKYADKPAGTYSGGNKR 2192
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGI--KDK-QVLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2193 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1001-1198 |
2.20e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1001 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQHNVLFDRLT 1079
Cdd:PRK10522 334 DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRKLFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1080 VEEhlwfySRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1159
Cdd:PRK10522 414 GPE-----GKPANPALVEKWLERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110225379 1160 IWDLILKY--KPGRTILLSTHHmDEADLLGDRIAIISHGKL 1198
Cdd:PRK10522 488 FYQVLLPLlqEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
967-1198 |
2.28e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.55 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 967 MESRHFEETRGMEEEPTHLPLVVCVDKLTkVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGlFPPTSGS 1046
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1047 ATIYGHDIRT-EMDEIRKNL---GMCPQ--HNVLFDRLTV------EEHLWfysrlKSMAQEEIRKETDKMIEDLELSNK 1114
Cdd:PRK11174 406 LKINGIELRElDPESWRKHLswvGQNPQlpHGTLRDNVLLgnpdasDEQLQ-----QALENAWVSEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1115 RHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDeaDLLG-DRIAII 1193
Cdd:PRK11174 481 DQAA--GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQwDQIWVM 556
|
....*
gi 110225379 1194 SHGKL 1198
Cdd:PRK11174 557 QDGQI 561
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2047-2278 |
2.86e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYK--SRKIGRI-------------LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEA 2111
Cdd:PRK13545 2 NYKVKFEHVTKKYKmyNKPFDKLkdlffrskdgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2112 FVNGHSVLkdllqVQQSLGycpqfdaLFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNK 2191
Cdd:PRK13545 82 DIKGSAAL-----IAISSG-------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2192 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2271
Cdd:PRK13545 150 SRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKE 229
|
....*..
gi 110225379 2272 LKNRFGD 2278
Cdd:PRK13545 230 VVDHYDE 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2047-2243 |
3.73e-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: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkdllqvq 2126
Cdd:TIGR03719 320 DKVIEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGETV-------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 qSLGYCPQFdalfdeltaREHLQlytrlrgiPWKDEAQVVKWALEKLELTKY---------------AD--KPAGTYSGG 2189
Cdd:TIGR03719 386 -KLAYVDQS---------RDALD--------PNKTVWEEISGGLDIIKLGKReipsrayvgrfnfkgSDqqKKVGQLSGG 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2190 NKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2243
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) ... |
2077-2243 |
6.65e-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: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTGdesttggeafvnghsvlkdllQVQQSLG-YC--PQFDALFDELTAREhLQLY-T 2152
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAG---------------------KLKPNLGkFDdpPDWDEILDEFRGSE-LQNYfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2153 RLRG--------------IP------------WKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2206
Cdd:cd03236 81 KLLEgdvkvivkpqyvdlIPkavkgkvgellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 110225379 2207 IFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2243
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2050-2263 |
8.29e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.41 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG---HSVLKD--LLQ 2124
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQF--DALFDELTAREhLQLYTRLRGIPWKdeaQVVKWALEKL-ELTKYAD---KPAGTYSGGNKRKLSTAI 2198
Cdd:PRK13646 83 VRKRIGMVFQFpeSQLFEDTVERE-IIFGPKNFKMNLD---EVKNYAHRLLmDLGFSRDvmsQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2199 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
987-1191 |
9.91e-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: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 987 LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIR-TEMDEIRKNL 1065
Cdd:TIGR03719 321 KVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlAYVDQSRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1066 GmcPQHNVlfdrltveehlWfysrlksmaqEEIRKETDKM-IEDLELSNK------------RHSLVQTLSGGMKRKLSV 1132
Cdd:TIGR03719 398 D--PNKTV-----------W----------EEISGGLDIIkLGKREIPSRayvgrfnfkgsdQQKKVGQLSGGERNRVHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1133 AIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYkPGRTILLStHhmDEADLlgDRIA 1191
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF-AGCAVVIS-H--DRWFL--DRIA 507
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1003-1198 |
1.05e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1003 KMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMC---------P 1069
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRDIQMVfqdsisavnP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVlfdRLTVEEHLWFYSRLKSMAQEEIRKETDKMIE-DLELSNKRHslvQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:PRK10419 105 RKTV---REIIREPLRHLLSLDKAERLARASEMLRAVDlDDSVLDKRP---PQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1149 TAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2075-2267 |
1.08e-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: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2075 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKDLLQvqQSLGYCPQFDALFDElTAREHLqly 2151
Cdd:COG4618 353 FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwDREELG--RHIGYLPQDVELFDG-TIAENI--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 TRLRGIpwkDEAQVVKWAlekleltKYAD-------KPAGtY-----------SGGNKRKLSTAIALIGYPAFIFLDEPT 2213
Cdd:COG4618 427 ARFGDA---DPEKVVAAA-------KLAGvhemilrLPDG-YdtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2214 TGMDPKARRFLWNLILDLIKTGRSVVLTSHSMeecEAL--CTRLAIMVNGRLRCLG 2267
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1023-1177 |
1.11e-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: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1023 GHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLF-DrlTVEEHLWfYSRLKSmAQEEIRK 1100
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFnD--TIAYNIA-YGRPDA-SEEEVEA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1101 -----ETDKMIEDLElsNKRHSLVQ----TLSGGMKRKlsVAIAfvggsRAI-------ILDEPTAGVDPYARRAIWDLI 1164
Cdd:COG5265 467 aaraaQIHDFIESLP--DGYDTRVGerglKLSGGEKQR--VAIA-----RTLlknppilIFDEATSALDSRTERAIQAAL 537
|
170
....*....|....*...
gi 110225379 1165 LKYKPGRTIL-----LST 1177
Cdd:COG5265 538 REVARGRTTLviahrLST 555
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1026-1199 |
1.14e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1026 GAGKTTTMSILTGLFP-PTSGSATIYGH--DIRTEMDEIRKNLGMCP--------------QHNVLfdrLTVEEHLWFYS 1088
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkrdgivpvmgvGKNIT---LAALDRFTGGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1089 RLKSMAQEE-IRKETDKM---IEDLELSnkrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI 1164
Cdd:PRK13549 375 RIDDAAELKtILESIQRLkvkTASPELA------IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI 448
|
170 180 190
....*....|....*....|....*....|....*.
gi 110225379 1165 LKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1199
Cdd:PRK13549 449 NQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1020-1178 |
1.37e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1020 SFLGHNGAGKTTTMSILTGlfPPTSGsaTIYGhDIRT-----EMDEIRKNLGMCPQHNVLFDRLTVEEHLWF--YSRL-K 1091
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRIsgfpkKQETFARISGYCEQNDIHSPQVTVRESLIYsaFLRLpK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1092 SMAQEEIRKETDKMIEDLELSNKRHSLV-----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA----RRAIWD 1162
Cdd:PLN03140 985 EVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAaaivMRTVRN 1064
|
170
....*....|....*.
gi 110225379 1163 LIlkyKPGRTILLSTH 1178
Cdd:PLN03140 1065 TV---DTGRTVVCTIH 1077
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2048-2245 |
1.50e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2048 DMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGeafvnghsVLKDllQVQQ 2127
Cdd:PRK09544 3 SLVSLENVSVSFGQRRV-----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKR--NGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 SLGYCPQfdALFDELTAREHLQLYTRLRgiPWKDEAQVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2207
Cdd:PRK09544 68 RIGYVPQ--KLYLDTTLPLTVNRFLRLR--PGTKKEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 110225379 2208 FLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSM 2245
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1005-1198 |
3.17e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH-----DIRTEMDEIRknlgMCPQ--HNVLFDR 1077
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIR----MIFQdpSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1078 LTVEEHLWFYSRLKS-MAQEEIRKETDKMIEDLELSNKRHSLV-QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1155
Cdd:PRK15112 104 QRISQILDFPLRLNTdLEPEQREKQIIETLRQVGLLPDHASYYpHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 1156 ARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK15112 184 MRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2069-2266 |
4.26e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKtSTFKM-LTGDESTTGGEAFVNGHSVLKDLLQVQQSLgycpqFDALFDEltareh 2147
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGK-STLAMlLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-----FSAVFTD------ 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2148 LQLYTRL---RGIPwKDEAQVVKWaLEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2219
Cdd:PRK10522 406 FHLFDQLlgpEGKP-ANPALVEKW-LERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225379 2220 ARRFLWNLILDLIK-TGRSVVLTSHSMEECEaLCTRLAIMVNGRLRCL 2266
Cdd:PRK10522 484 FRREFYQVLLPLLQeMGKTIFAISHDDHYFI-HADRLLEMRNGQLSEL 530
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2050-2300 |
4.71e-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: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKD---LLQVQ 2126
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFT-----IEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEkcgYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 QSLGY-CP-------QFDALFDELTAREHLQLYTRL-----RGIPWKDEAQVVKWALEKLELTKYADKP----------- 2182
Cdd:TIGR03269 76 SKVGEpCPvcggtlePEEVDFWNLSDKLRRRIRKRIaimlqRTFALYGDDTVLDNVLEALEEIGYEGKEavgravdliem 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2183 ----------AGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEAL 2251
Cdd:TIGR03269 156 vqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVIEDL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 110225379 2252 CTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQNVKDVVRFFN 2300
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRN 284
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1994-2263 |
4.81e-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: 58.19 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1994 AMTVEGFVGFFLTIMCQYNFLRQ-------PQRLPVSTKPVEDDVDVASER-------QRVlRGDadndmVKIENLTKVY 2059
Cdd:TIGR02203 267 SLTAGDFTAFITAMIALIRPLKSltnvnapMQRGLAAAESLFTLLDSPPEKdtgtraiERA-RGD-----VEFRNVTFRY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2060 KSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ-VQQSLGYCPQFDAL 2138
Cdd:TIGR02203 341 PGRDRP---ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAsLRRQVALVSQDVVL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2139 FDELTAREhlQLYTRLRGIpwkDEAQVVKwALEKLELTKYADK-PAGTY----------SGGNKRKLSTAIALIGYPAFI 2207
Cdd:TIGR02203 418 FNDTIANN--IAYGRTEQA---DRAEIER-ALAAAYAQDFVDKlPLGLDtpigengvllSGGQRQRLAIARALLKDAPIL 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2208 FLDEPTTGMDPKARRfLWNLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRL 2263
Cdd:TIGR02203 492 ILDEATSALDNESER-LVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
991-1199 |
4.99e-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: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPpTSGSATIYGHDIRT-EMDEIRKNLGMCP 1069
Cdd:cd03289 5 VKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRlTVEEHLWFYSRLKSmaqEEIRKETDK-----MIE------DLELSNKRHslvqTLSGGMKRKLSVAIAFVG 1138
Cdd:cd03289 84 QKVFIFSG-TFRKNLDPYGKWSD---EEIWKVAEEvglksVIEqfpgqlDFVLVDGGC----VLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1139 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLK 1199
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1004-1178 |
5.00e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.26 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1004 MALNKLSLNLYENQV----VSFL--------GHNGAGKTTTMSILTGLFPPTSGSatIYGHDIRTemDEIRKNLGMCPQH 1071
Cdd:PRK13541 2 LSLHQLQFNIEQKNLfdlsITFLpsaityikGANGCGKSSLLRMIAGIMQPSSGN--IYYKNCNI--NNIAKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 NV-LFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLeLSNKrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1150
Cdd:PRK13541 78 NLgLKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDL-LDEK----CYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180
....*....|....*....|....*....
gi 110225379 1151 GVDPYARRAIWDLI-LKYKPGRTILLSTH 1178
Cdd:PRK13541 153 NLSKENRDLLNNLIvMKANSGGIVLLSSH 181
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2047-2274 |
5.90e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DL 2122
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCI-----FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2123 LQVQQSLGYCPQFDALFDELTA--------REHLQLytrlrgiPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRK- 2193
Cdd:PRK11831 80 YTVRKRMSMLFQSGALFTDMNVfdnvayplREHTQL-------PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2194 -LSTAIALigYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2271
Cdd:PRK11831 153 aLARAIAL--EPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
...
gi 110225379 2272 LKN 2274
Cdd:PRK11831 231 LQA 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
991-1199 |
6.79e-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: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFpPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1069
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1070 QHNVLFDRlTVEEHLWFYSRlksMAQEEIRKETDK-----MIE------DLELSNKRHslvqTLSGGMKRKLSVAIAFVG 1138
Cdd:TIGR01271 1299 QKVFIFSG-TFRKNLDPYEQ---WSDEEIWKVAEEvglksVIEqfpdklDFVLVDGGY----VLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1139 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLK 1199
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV-EALLECQQFLVIEGSSVK 1430
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
2073-2244 |
8.24e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2073 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKdllqVQQS-LGYCPQFDALFDELTAREHLQLY 2151
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPyCTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 TRLRgipwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2231
Cdd:PRK13541 95 SEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|...
gi 110225379 2232 IKTGRSVVLTSHS 2244
Cdd:PRK13541 170 ANSGGIVLLSSHL 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1009-1206 |
8.39e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1009 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP----TSGS----------ATIYGHDIRTEMDEIRKNLGmcPQHNVl 1074
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRvlldgkpvapCALRGRKIATIMQNPRSAFN--PLHTM- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1075 fdRLTVEEHLWFYSRLKSMAQeeirketdkMIEDLE---LSNKRHSLVQ---TLSGGMKRKLSVAIAFVGGSRAIILDEP 1148
Cdd:PRK10418 99 --HTHARETCLALGKPADDAT---------LTAALEavgLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 1149 TAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS--PLF 1206
Cdd:PRK10418 168 TTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDveTLF 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2050-2260 |
9.33e-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: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQS 2128
Cdd:cd03254 3 IEFENVNFSYDEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDElTAREHLQLytrlrGIPWKDEAQVVKWA--------LEKLE--LTKYADKPAGTYSGGNKRKLSTAI 2198
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRL-----GRPNATDEEVIEAAkeagahdfIMKLPngYDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2199 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHsmeecealctRLAIMVN 2260
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAH----------RLSTIKN 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
991-1182 |
9.42e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 991 VDKLTKVYKNDKK----MALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAtiyghDIRTEMDEIRKNLG 1066
Cdd:PRK13545 21 FDKLKDLFFRSKDgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1067 mcpqhnvLFDRLTVEEHLWFYSRLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:PRK13545 96 -------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 110225379 1147 EPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDE 1182
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEqGKTIFFISHSLSQ 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1005-1255 |
9.73e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDI----RTEMDEIR-KNLGMCPQhnvlfD 1076
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRaEQISMIFQ-----D 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 RLT-------VEEHLWFYSRL-KSMAQEEIRKETDKMIEDLEL--SNKRHSLV-QTLSGGMKRKLSVAIAFVGGSRAIIL 1145
Cdd:PRK09473 106 PMTslnpymrVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMpeARKRMKMYpHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1146 DEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGA--YGDGY---- 1215
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNArdVFYQPShpYSIGLlnav 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1216 -RL-----TLVKQPAEPgtsqePGLASSPSGCPRLSSC--------SEPQVSQF 1255
Cdd:PRK09473 266 pRLdaegeSLLTIPGNP-----PNLLRLPKGCPFQPRCphameicsSAPPLEEF 314
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2033-2272 |
9.75e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2033 VASERQRVLRGDADNDM----VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-DESTT 2107
Cdd:PRK14271 1 MACERLGGQSGAADVDAaapaMAAVNLTLGFAGKTV-----LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2108 G----GEAFVNGHSVL--KDLLQVQQSLGYC-----PQFDALFDELTA--REH-LQLYTRLRGIPWKDEAQVVKWALEKL 2173
Cdd:PRK14271 76 GyrysGDVLLGGRSIFnyRDVLEFRRRVGMLfqrpnPFPMSIMDNVLAgvRAHkLVPRKEFRGVAQARLTEVGLWDAVKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2174 ELTkyaDKPAgTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTgRSVVLTSHSMEECEALCT 2253
Cdd:PRK14271 156 RLS---DSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISD 230
|
250
....*....|....*....
gi 110225379 2254 RLAIMVNGRLRCLGSIQHL 2272
Cdd:PRK14271 231 RAALFFDGRLVEEGPTEQL 249
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
999-1197 |
1.23e-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: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 999 KNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtemdeirknLGMCPQ-------- 1070
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQepwiqngt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1071 --HNVLFDRltVEEHLWFYSRLKSMAQEEirketdkmieDLE-LSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAI 1143
Cdd:cd03250 82 irENILFGK--PFDEERYEKVIKACALEP----------DLEiLPDGDLTEIGekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1144 ILDEPTAGVDPYARRAIWD-LILKY-KPGRTILLSTHHMdeaDLLG--DRIAIISHGK 1197
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) ... |
1015-1212 |
1.42e-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: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1015 ENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatiygHDIRTEMDEIRKNLGMCPQHN----VLFDRLTVEEHLWFYSRL 1090
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-----FDDPPDWDEILDEFRGSELQNyftkLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1091 KSMAQ---EEIRKETDK------MIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR---- 1157
Cdd:cd03236 100 PKAVKgkvGELLKKKDErgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaa 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 1158 RAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIaiishgklkCC--GSPlflkGAYG 1212
Cdd:cd03236 180 RLIRELA---EDDNYVLVVEHDLAVLDYLSDYI---------HClyGEP----GAYG 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2077-2272 |
1.92e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.03 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTG-DESTTG----GEAFVNGHSVLKDLLQVQQSLGYCPQFDalfdeltarEHlQLY 2151
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGlLQPTSGtvtiGERVITAGKKNKKLKPLRKKVGIVFQFP---------EH-QLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2152 --TRLR---------GIPWKDEAQVVKWALEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2219
Cdd:PRK13634 100 eeTVEKdicfgpmnfGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2220 ARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2272
Cdd:PRK13634 180 GRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2051-2268 |
1.95e-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: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2051 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDEST--TGGEAFVNGHSVLkdllqvqqs 2128
Cdd:cd03217 2 EIKDLHVSVGGKEI-----LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDIT--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 lgycpqfdalfdeltareHLQLYTRLR---GIPWKDEAQV--VKWAleklELTKYADKpagTYSGGNKRKLSTAIALIGY 2203
Cdd:cd03217 68 ------------------DLPPEERARlgiFLAFQYPPEIpgVKNA----DFLRYVNE---GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAL-CTRLAIMVNGRLRCLGS 2268
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
978-1154 |
2.10e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 978 MEEEPTHLPLVVCVDKLTkvYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT- 1056
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1057 EMDEIRKNLGMCPQhnvLFDRLTVEEHLWFysrLKSMAQEEIRKETDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAF 1136
Cdd:PRK13543 79 DRSRFMAYLGHLPG---LKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLW 152
|
170
....*....|....*...
gi 110225379 1137 VGGSRAIILDEPTAGVDP 1154
Cdd:PRK13543 153 LSPAPLWLLDEPYANLDL 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
950-1198 |
3.01e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 950 WAHTPRLSVMEEDQACAME-----SRHFEETrgmeeepTHLP--LVVCVDKLTKVykndKKMALNKLSLNLYENQVVSFL 1022
Cdd:PRK10982 212 WIATQPLAGLTMDKIIAMMvgrslTQRFPDK-------ENKPgeVILEVRNLTSL----RQPSIRDVSFDLHKGEILGIA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1023 GHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEI----------RKNLGMCPQHNVLFDRL--TVEEHLwfyS 1088
Cdd:PRK10982 281 GLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAInhgfalvteeRRSTGIYAYLDIGFNSLisNIRNYK---N 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1089 RLKSMAQEEIRKETDKMIEDLELSNKRHS-LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY 1167
Cdd:PRK10982 358 KVGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL 437
|
250 260 270
....*....|....*....|....*....|....
gi 110225379 1168 -KPGRTILLSTHHMDEadLLG--DRIAIISHGKL 1198
Cdd:PRK10982 438 aKKDKGIIIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2075-2246 |
3.80e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.82 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2075 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKDLLQVQQSLGYCPQFDA-----LFDELT-AREHL 2148
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG----QTINLVRDKDGQLKVADKnqlrlLRTRLTmVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2149 QLYTRLRGIPWKDEAQVVKWALEKLEL----TKYADK------PAGTY----SGGNKRKLSTAIALIGYPAFIFLDEPTT 2214
Cdd:PRK10619 102 NLWSHMTVLENVMEAPIQVLGLSKQEAreraVKYLAKvgiderAQGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190
....*....|....*....|....*....|..
gi 110225379 2215 GMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2246
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2047-2243 |
3.94e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAfvnghSVLKDLlqvq 2126
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRII-----LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAKGI---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2127 qSLGYCPQFDALFdeLTAREH-LQLYTRLrgIPWKDEAQvvkwalekleLTKY-------ADK---PAGTYSGGNKRKLS 2195
Cdd:PRK10636 376 -KLGYFAQHQLEF--LRADESpLQHLARL--APQELEQK----------LRDYlggfgfqGDKvteETRRFSGGEKARLV 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110225379 2196 TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2243
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVSH 485
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2050-2243 |
4.99e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkdllqvqqSL 2129
Cdd:PRK11819 325 IEAENLSKSFGDR-----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT-IKIGETV---------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQF-DALFDELTArehlqlytrlrgipWkdeaQVVKWALEKLELTKY---------------AD--KPAGTYSGGNK 2191
Cdd:PRK11819 390 AYVDQSrDALDPNKTV--------------W----EEISGGLDIIKVGNReipsrayvgrfnfkgGDqqKKVGVLSGGER 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2192 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2243
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PGCAVVISH 500
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
998-1153 |
8.26e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1076
Cdd:PLN03130 1247 YRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 ---RLTVE---EH----LWfYSRLKSMAQEEIRKETDKMieDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIILD 1146
Cdd:PLN03130 1327 gtvRFNLDpfnEHndadLW-ESLERAHLKDVIRRNSLGL--DAEVSEAG----ENFSVGQRQLLSLARALLRRSKILVLD 1399
|
....*..
gi 110225379 1147 EPTAGVD 1153
Cdd:PLN03130 1400 EATAAVD 1406
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2182-2246 |
8.80e-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: 8.80e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2182 PAGTYSGGNKRKLSTAIALI---GYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2246
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2047-2263 |
9.40e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2047 NDMVKIENLTkVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTST----FKMLTGDESTTGGEAFVNGHSVLKDL 2122
Cdd:PRK10418 2 PQQIELRNIA-LQAAQPL-----VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2123 LQ------VQQSlgycPQ--FDALfdeLTAREHLQLYTRLRGIPwKDEAQVVKwALEKLELTKyADKPAGTY----SGGN 2190
Cdd:PRK10418 76 LRgrkiatIMQN----PRsaFNPL---HTMHTHARETCLALGKP-ADDATLTA-ALEAVGLEN-AARVLKLYpfemSGGM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2191 KRKLSTAIALIGYPAFIFLDEPTTGMDPKAR-RFLwNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRL 2263
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQaRIL-DLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2029-2254 |
1.12e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2029 DDVDvASERQR-VLRGDADNDM----VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD 2103
Cdd:PRK15064 295 EEVK-PSSRQNpFIRFEQDKKLhrnaLEVENLTKGFDNGPL-----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2104 ESTTGGEafvnghsvlkdllqVQQS----LGYCPQ-----FDalfDELTAREHLQLYTRLrgipwKDEAQVVKWALEKLE 2174
Cdd:PRK15064 369 LEPDSGT--------------VKWSenanIGYYAQdhaydFE---NDLTLFDWMSQWRQE-----GDDEQAVRGTLGRLL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2175 LTK-YADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLwNLILDLIKTgrSVVLTSHSMEECEALCT 2253
Cdd:PRK15064 427 FSQdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL-NMALEKYEG--TLIFVSHDREFVSSLAT 503
|
.
gi 110225379 2254 R 2254
Cdd:PRK15064 504 R 504
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2069-2243 |
1.26e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 53.63 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLlqvQQSLGYCPQfDA-LFDElT 2143
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdltLESL---RRQIGVVPQ-DTfLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2144 AREHLQLytrlrGIPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEP 2212
Cdd:COG1132 430 IRENIRY-----GRPDATDEEVEE-AAKAAQAHEFIEAlPDGydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190
....*....|....*....|....*....|.
gi 110225379 2213 TTGMDPKARRFLWNLILDLIKtGRSVVLTSH 2243
Cdd:COG1132 504 TSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2069-2262 |
1.26e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG----DES-----------TTGGEAFVNGHS-VLKDLLQVQQS---- 2128
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyqkDSGsilfqgkeidfKSSKEALENGISmVHQELNLVLQRsvmd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 ---LGYCPQFDALFDeltareHLQLYTRLRGIpwkdeaqvvkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2205
Cdd:PRK10982 93 nmwLGRYPTKGMFVD------QDKMYRDTKAI------------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2206 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2262
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2062-2272 |
1.34e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2062 RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKtstfkmltgdeSTTG----------GEAFVNGHSVlkDLLQVQQSLGY 2131
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGK-----------STTGlallrlinsqGEIWFDGQPL--HNLNRRQLLPV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2132 CPQFDALFDE----LTAR--------EHLQLYTRLRGiPWKDEAQVVKwALEKLEL---TKYadKPAGTYSGGNKRKLST 2196
Cdd:PRK15134 361 RHRIQVVFQDpnssLNPRlnvlqiieEGLRVHQPTLS-AAQREQQVIA-VMEEVGLdpeTRH--RYPAEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2197 AIALIGYPAFIFLDEPTTGMDpkarRFLWNLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2271
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLD----KTVQAQILALLKSlqqkhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
.
gi 110225379 2272 L 2272
Cdd:PRK15134 513 V 513
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1006-1197 |
1.38e-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: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1006 LNKLSLN----LYENQVVSFL-------GHNGAGKTTTMS----ILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMC 1068
Cdd:cd03240 1 IDKLSIRnirsFHERSEIEFFspltlivGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIRegEVRAQVKLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 PQHNVLFDR-LTVEEHLWFYSrlksmaQEEIRKETDKMIEdlelsnkrhslvqTLSGGMKRKLSV----AIAFVGGSRA- 1142
Cdd:cd03240 81 NGKKYTITRsLAILENVIFCH------QGESNWPLLDMRG-------------RCSGGEKVLASLiirlALAETFGSNCg 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 1143 -IILDEPTAGVDPYARR-AIWDLI--LKYKPGRTILLSTHHMDEADLLGD--RIAIISHGK 1197
Cdd:cd03240 142 iLALDEPTTNLDEENIEeSLAEIIeeRKSQKNFQLIVITHDEELVDAADHiyRVEKDGRQK 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
2061-2268 |
1.73e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2061 SRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTG--------GEAFVNGHSVLK-DLLQVQQSLGY 2131
Cdd:PRK13547 10 ARRHRAIL--RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAiDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2132 CPQ-----FDALFDELT-------AREHLQLYTRLRGIPWKdeaqvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2199
Cdd:PRK13547 88 LPQaaqpaFAFSAREIVllgryphARRAGALTHRDGEIAWQ--------ALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2200 L---------IGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECEALCTRLAIMVNGRLRCLGS 2268
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1005-1153 |
1.94e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMDEIRKNLGMCPQHNV--LFDRL 1078
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1079 TV----EEHLWFYSrlKSMAQEEIRKETDKMIEDLEL-SNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:PRK15079 116 TIgeiiAEPLRTYH--PKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2050-2281 |
2.64e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKDLLQVQQSL 2129
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLD-----IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRFGDGYM 2281
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFVAGFI 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2070-2247 |
2.66e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.87 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2070 VDRLCLGVRPGEcFGLL-GVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREH 2147
Cdd:PRK10247 23 LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2148 LQLYTRLRGIpwKDEAQVVKWALEKLELTKYA-DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2226
Cdd:PRK10247 101 LIFPWQIRNQ--QPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170 180
....*....|....*....|..
gi 110225379 2227 LILDLIK-TGRSVVLTSHSMEE 2247
Cdd:PRK10247 179 IIHRYVReQNIAVLWVTHDKDE 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2077-2217 |
3.53e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTsTF-KMLTGDESTTGGEafvnghsVLKDLlqvqqSLGYCPQFDALFDELTAREHL-QLYTRL 2154
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKT-TFaKLLAGVLKPDEGE-------VDPEL-----KISYKPQYIKPDYDGTVEDLLrSITDDL 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 2155 RGIPWKDEaqvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALiGYPAFIF-LDEPTTGMD 2217
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 ... |
2075-2243 |
4.13e-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: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2075 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkDLLQVQQ-----SLGYCPQFDALFDElTAREHLQ 2149
Cdd:cd03253 22 FTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ----DIREVTLdslrrAIGVVPQDTVLFND-TIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2150 lYTRLRGipwkDEAQVVKWA--------LEKLElTKYADKPA--GTY-SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2218
Cdd:cd03253 97 -YGRPDA----TDEEVIEAAkaaqihdkIMRFP-DGYDTIVGerGLKlSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180
....*....|....*....|....*
gi 110225379 2219 KARRFLWNLILDLIKtGRSVVLTSH 2243
Cdd:cd03253 171 HTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2050-2217 |
4.16e-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: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKigriLAVDRlclG-VRPGECFGLLGVNGAGKTsTF-KMLTGDESTTGGEafvnghsvlkdlLQVQQ 2127
Cdd:COG1245 342 VEYPDLTKSYGGFS----LEVEG---GeIREGEVLGIVGPNGIGKT-TFaKILAGVLKPDEGE------------VDEDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 SLGYCPQFDALFDELTAREHL--QLYTRLRGIPWKDEaqvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALiGYPA 2205
Cdd:COG1245 402 KISYKPQYISPDYDGTVEEFLrsANTDDFGSSYYKTE------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACL-SRDA 474
|
170
....*....|...
gi 110225379 2206 FIF-LDEPTTGMD 2217
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) ... |
2077-2221 |
4.24e-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: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2077 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkdllqvqqslGYCPQFDALFDELTAREHLQLYTRLRG 2156
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 2157 IP--WKDEaqvvkwALEKLELTKYADKPAGTYSGGNKRKlsTAIAL-IGYPAFIFL-DEPTTGMDPKAR 2221
Cdd:cd03237 91 THpyFKTE------IAKPLQIEQILDREVPELSGGELQR--VAIAAcLSKDADIYLlDEPSAYLDVEQR 151
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2049-2221 |
6.76e-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: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV------LKDL 2122
Cdd:PRK11650 3 GLKLQAVRKSYD----GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepaDRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2123 LQVQQSlgYcpqfdALFDELTAREHLQLYTRLRGIPwKDE-AQVVKWALEKLELTKYAD-KPAgTYSGGNKRKLSTAIAL 2200
Cdd:PRK11650 79 AMVFQN--Y-----ALYPHMSVRENMAYGLKIRGMP-KAEiEERVAEAARILELEPLLDrKPR-ELSGGQRQRVAMGRAI 149
|
170 180
....*....|....*....|..
gi 110225379 2201 IGYPA-FIFlDEPTTGMDPKAR 2221
Cdd:PRK11650 150 VREPAvFLF-DEPLSNLDAKLR 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
989-1284 |
7.28e-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: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 989 VCVDKLTKVYKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMc 1068
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSL- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1069 pQHNVLFDRLTVEEHlwFYSRLKSMAqeeirketdkMIEDLEL--SNKRHSLVQ---TLSGGMKRKLSVAIAFVGGSRAI 1143
Cdd:TIGR00957 716 -RENILFGKALNEKY--YQQVLEACA----------LLPDLEIlpSGDRTEIGEkgvNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1144 ILDEPTAGVDPYARRAIWDLILKYK---PGRTILLSTHHMDEADLLgDRIAIISHGKLKCCGS-PLFLK--GAYGDGYRl 1217
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSyQELLQrdGAFAEFLR- 860
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110225379 1218 tlVKQPAEPGTSQEPGLASSPSGCPRLSSCSEPQVS-------QFIRKHVASSLLVSDTSTELSyilPSEAVKK 1284
Cdd:TIGR00957 861 --TYAPDEQQGHLEDSWTALVSGEGKEAKLIENGMLvtdvvgkQLQRQLSASSSDSGDQSRHHG---SSAELQK 929
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2050-2218 |
1.07e-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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTST----FKMLtgdeSTTGGEAFVNGHSVLK-DLLQ 2124
Cdd:cd03244 3 IEFKNVSLRYRP---NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKiGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQQSLGYCPQFDALFDElTAREHLQLYTRlrgipwKDEAQVVKwALEKLELTKYADKPAGT-----------YSGGNKRK 2193
Cdd:cd03244 76 LRSRISIIPQDPVLFSG-TIRSNLDPFGE------YSDEELWQ-ALERVGLKEFVESLPGGldtvveeggenLSVGQRQL 147
|
170 180
....*....|....*....|....*
gi 110225379 2194 LSTAIALIGYPAFIFLDEPTTGMDP 2218
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDP 172
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1115-1178 |
1.24e-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: 1.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1115 RHSLVQTLSGGMKRKLSVAIAFVGGSRA----IILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTH 1178
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILALASLKprplYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITH 139
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2078-2243 |
1.65e-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: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2078 RPGECFGLLGVNGAGKTSTFKMLTGD------------------ESTTGGEAfvngHSVLKDLLQVQQSLGYCPQF-DAL 2138
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswdevlKRFRGTEL----QDYFKKLANGEIKVAHKPQYvDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2139 FDEL--TAREHLQLYtrlrgipwkDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2216
Cdd:COG1245 173 PKVFkgTVRELLEKV---------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*..
gi 110225379 2217 DPKARRFLWNLILDLIKTGRSVVLTSH 2243
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2075-2243 |
1.82e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2075 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQ-----------------VQQSLGYCPQFDA 2137
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvydfvaegIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2138 LFDELT---AREHLQLYTRLRGI-----PWKDEAQVvKWALEKLELTkyADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:PRK11147 104 ISHLVEtdpSEKNLNELAKLQEQldhhnLWQLENRI-NEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLL 180
|
170 180 190
....*....|....*....|....*....|....
gi 110225379 2210 DEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2243
Cdd:PRK11147 181 DEPTNHLDIETIEWLEGFLKTF---QGSIIFISH 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2049-2231 |
1.90e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSR----KIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKDLL 2123
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2124 QVQQSLGYCPQfdalfDELTAREHLQLYTRLRGIPWKDEAQVVKWALEK---LELTKYADKP--AGTY----SGGNKRKL 2194
Cdd:PRK15112 84 YRSQRIRMIFQ-----DPSTSLNPRQRISQILDFPLRLNTDLEPEQREKqiiETLRQVGLLPdhASYYphmlAPGQKQRL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 110225379 2195 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2231
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1981-2274 |
2.13e-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: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1981 SPFEWDIVTrglvAMTVEGFVgffLTIMCQYNFLRQPQRLPV---STKPVEDDVDVASERQRVLRGDADNDMVKIENLTK 2057
Cdd:TIGR01271 1153 STLQWAVNS----SIDVDGLM---RSVSRVFKFIDLPQEEPRpsgGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTA 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2058 VYKSRkiGRILAVDrLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTgGEAFVNGHSVLKDLLQV-QQSLGYCPQFD 2136
Cdd:TIGR01271 1226 KYTEA--GRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTwRKAFGVIPQKV 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2137 ALFDElTAREHLQLYTRlrgipWKDEaQVVKWALE---KLELTKYADK-----PAGTY--SGGNKRKLSTAIALIGYPAF 2206
Cdd:TIGR01271 1302 FIFSG-TFRKNLDPYEQ-----WSDE-EIWKVAEEvglKSVIEQFPDKldfvlVDGGYvlSNGHKQLMCLARSILSKAKI 1374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110225379 2207 IFLDEPTTGMDPkarrFLWNLILDLIKTGRS---VVLTSHSME---ECEALctrlaIMVNG-RLRCLGSIQHLKN 2274
Cdd:TIGR01271 1375 LLLDEPSAHLDP----VTLQIIRKTLKQSFSnctVILSEHRVEallECQQF-----LVIEGsSVKQYDSIQKLLN 1440
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2069-2217 |
2.17e-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: 49.74 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2069 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREH 2147
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 2148 LQLYTRlRGIPWKDEAQVVKWA-----LEKLEL---TKYADKpAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD 2217
Cdd:TIGR01193 568 LLLGAK-ENVSQDEIWAACEIAeikddIENMPLgyqTELSEE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2050-2243 |
2.58e-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: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKDL-LQ-VQQ 2127
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPIL--KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLnLRwLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2128 SLGYCPQFDALFDeLTAREHLQLytrlrGIPWKDEAQVVKwALEKLELTKYADKPAGTY-----------SGGNKRKLST 2196
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENIRY-----GKPDATDEEVEE-AAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110225379 2197 AIALIGYPAFIFLDEPTTGMDPKARRflwnLI---LDLIKTGRSVVLTSH 2243
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEK----LVqeaLDRAMKGRTTIVIAH 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2050-2243 |
2.65e-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: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKDLlqv 2125
Cdd:cd03251 1 VEFKNVTFRYPGDGP---PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdytLASL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2126 QQSLGYCPQFDALFDElTAREHLqLYtrlrGIPWKDEAQVVKwALEKLELTKYADK-PAG----------TYSGGNKRKL 2194
Cdd:cd03251 75 RRQIGLVSQDVFLFND-TVAENI-AY----GRPGATREEVEE-AARAANAHEFIMElPEGydtvigergvKLSGGQRQRI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110225379 2195 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSH 2243
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAH 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2065-2272 |
3.85e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.86 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2065 GRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDELT 2143
Cdd:PRK10575 23 GRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2144 AREhlqlytrLRGI---PW--------KDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEP 2212
Cdd:PRK10575 102 VRE-------LVAIgryPWhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110225379 2213 TTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2272
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1005-1198 |
3.87e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1005 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIRKNLGMCPQ--HNVLFDRL 1078
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1079 TVEEHLWFYSRLKSMAQ-EEIRKETDKMIEDLELSnKRHSL--VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1155
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLL-PEHAWryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110225379 1156 ARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKL 1198
Cdd:PRK10261 498 IRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2050-2246 |
3.93e-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: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTkvYKSRKiGRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAfvnGHSVLKDLLQVQQsL 2129
Cdd:cd03223 1 IELENLS--LATPD-GRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGEDLLFLPQ-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2130 GYCPQfdalfdeLTAREHLqLYtrlrgiPWKDEaqvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFL 2209
Cdd:cd03223 73 PYLPL-------GTLREQL-IY------PWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110225379 2210 DEPTTGMDPKARRFLWNLILD----LIKTGRSVVLTS-HSME 2246
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKElgitVISVGHRPSLWKfHDRV 157
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
988-1203 |
3.93e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 988 VVCVDKLTKVYKNDKKM--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---------- 1055
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1056 ----TEMDEIR-KNLGMCPQH-----NVLFdrlTVEEHLWFYSRL-KSMAQEEIRKETDKMIEDLELSNKRHSLVQ---T 1121
Cdd:PRK10261 92 eqsaAQMRHVRgADMAMIFQEpmtslNPVF---TVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1122 LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1199
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....
gi 110225379 1200 CCGS 1203
Cdd:PRK10261 249 ETGS 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2012-2291 |
4.89e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2012 NFLRQPQRLPVSTKPVE---DDVDVASE------RQRVLRGDADNDMVKIENLTKVYKSrkiGRILAVDRLCLGVRPGEC 2082
Cdd:PLN03232 1188 GVLRQASKAENSLNSVErvgNYIDLPSEataiieNNRPVSGWPSRGSIKFEDVHLRYRP---GLPPVLHGLSFFVSPSEK 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2083 FGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQSLGYCPQFDALFDElTAREHLQlytrlrgiPWKD 2161
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSG-TVRFNID--------PFSE 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2162 EAQVVKW-ALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2229
Cdd:PLN03232 1336 HNDADLWeALERAHIKDVIDRnPFGldaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR 1415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2230 DLIKTGrSVVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQN 2291
Cdd:PLN03232 1416 EEFKSC-TMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2050-2247 |
4.93e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.34 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT------GDESTTGGEAFVNGH----SVL 2119
Cdd:PRK14258 8 IKVNNLSFYYDTQKI-----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNiyerRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2120 KDLLQVQQSLGYcPQFDaLFdELTAREHLQLYTRLRGipWKDEAQ---VVKWALEKLEL----TKYADKPAGTYSGGNKR 2192
Cdd:PRK14258 83 LNRLRRQVSMVH-PKPN-LF-PMSVYDNVAYGVKIVG--WRPKLEiddIVESALKDADLwdeiKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2193 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEE 2247
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1007-1242 |
6.16e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1007 NKLSLNLYENQVVSFLGHNGAGKT-TTMSILTGL-FPP---TSGSATIYGHDI----RTEMDEIRKN-LGMCPQH----- 1071
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLlhasEQTLRGVRGNkIAMIFQEpmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 NVLFdrlTVEEHLW-FYSRLKSMAQEEIRKEtdkMIEDLELSNKRHS------LVQTLSGGMKRKLSVAIAFVGGSRAII 1144
Cdd:PRK15134 106 NPLH---TLEKQLYeVLSLHRGMRREAARGE---ILNCLDRVGIRQAakrltdYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1145 LDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKlkccgsplflkgAYGDGYRLTLVKQ 1222
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR------------CVEQNRAATLFSA 247
|
250 260
....*....|....*....|
gi 110225379 1223 PAEPGTSQEpgLASSPSGCP 1242
Cdd:PRK15134 248 PTHPYTQKL--LNSEPSGDP 265
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1000-1198 |
6.16e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1000 NDKKMaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTG--LFPPTSGSATIYGHDIRTEMDEIRKNLG--MCPQH---- 1071
Cdd:CHL00131 18 NENEI-LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGifLAFQYpiei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1072 ----NVLFDRLTveehlwFYSRLKSMAQEEIRKetdkmIEDLELSNKRHSLV------------QTLSGGMKRK---LSV 1132
Cdd:CHL00131 97 pgvsNADFLRLA------YNSKRKFQGLPELDP-----LEFLEIINEKLKLVgmdpsflsrnvnEGFSGGEKKRneiLQM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110225379 1133 AIAfvgGSRAIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEAD-LLGDRIAIISHGKL 1198
Cdd:CHL00131 166 ALL---DSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDyIKPDYVHVMQNGKI 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2180-2263 |
7.53e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2180 DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMV 2259
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
....
gi 110225379 2260 NGRL 2263
Cdd:NF040905 479 EGRI 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1022-1153 |
1.15e-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: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1022 LGHNGAGKTTTMSILTGL---FPPTSGSATIY-GHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMA--- 1094
Cdd:TIGR00956 93 LGRPGSGCSTLLKTIASNtdgFHIGVEGVITYdGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQnrp 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110225379 1095 -----QEEIRKETDKMIEDLELSNKRHS-----LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:TIGR00956 173 dgvsrEEYAKHIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1001-1153 |
1.35e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1001 DKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPpTSGSATIYGHDI----RTEMDEIRKNLGMCPQ--HNVL 1074
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1075 FDRLTV----EEHLWFYSRLKSMAQEEIRkeTDKMIEDLELS-NKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1149
Cdd:PRK15134 376 NPRLNVlqiiEEGLRVHQPTLSAAQREQQ--VIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
....
gi 110225379 1150 AGVD 1153
Cdd:PRK15134 454 SSLD 457
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
2085-2269 |
1.49e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.41 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2085 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsVLKD------LLQVQQSLGYCPQfDA-LFDELTAREHLQlYtrlrGI 2157
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDaekgicLPPEKRRIGYVFQ-DArLFPHYKVRGNLR-Y----GM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2158 PWKDEAQ---VVKW-ALEKLeLTKYadkPAgTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD-PKARR---FLWNLIL 2229
Cdd:PRK11144 102 AKSMVAQfdkIVALlGIEPL-LDRY---PG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKREllpYLERLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110225379 2230 DlIKTgrSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2269
Cdd:PRK11144 177 E-INI--PILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2049-2243 |
1.71e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.03 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2049 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----DLLQ 2124
Cdd:PRK10535 4 LLELKDIRRSYPSGE-EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2125 VQ-QSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2203
Cdd:PRK10535 83 LRrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2243
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2059-2247 |
1.76e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2059 YKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESttggEAFVNgHSVL--------KDLLQVQQSLG 2130
Cdd:PRK10938 270 YNDRPI-----LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP----QGYSN-DLTLfgrrrgsgETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2131 YcpqfdalfdeLTAREHL--QLYTRLR-----------GI----PWKDEAQVVKWaLEKLELTKY-ADKPAGTYSGGNKR 2192
Cdd:PRK10938 340 Y----------VSSSLHLdyRVSTSVRnvilsgffdsiGIyqavSDRQQKLAQQW-LDILGIDKRtADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110225379 2193 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVL-TSHSMEE 2247
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAED 464
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2204-2308 |
2.22e-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: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2204 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEecealctrLAIMVNgrlrcLGSIQHLKNRFGDGYMIT 2283
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH--------LLSEVP-----LENIRRLRRDSGGTTSTK 254
|
90 100
....*....|....*....|....*
gi 110225379 2284 VRTKSSQNVKDVVRFFNRNFPEAML 2308
Cdd:COG3593 255 LIDLDDEDLRKLLRYLGVTRSELLF 279
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
981-1160 |
2.38e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 981 EPTHLP-LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIRtemd 1059
Cdd:PRK10636 304 APESLPnPLLKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1060 eirknLGMCPQHNVLFDRLTvEEHLWFYSRLKSmaqeeirKETDKMIEDLE-----LSNKRHSLVQTLSGGMKRKLSVAI 1134
Cdd:PRK10636 377 -----LGYFAQHQLEFLRAD-ESPLQHLARLAP-------QELEQKLRDYLggfgfQGDKVTEETRRFSGGEKARLVLAL 443
|
170 180
....*....|....*....|....*.
gi 110225379 1135 AFVGGSRAIILDEPTAGVDPYARRAI 1160
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1019-1246 |
2.48e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1019 VSFLGHNGAGKTTTMSILTGLFPPTSGSATIyghdirtemdeIRKNLGMCPQHNVLFDRlTVEEHLWFYSRLKSMAQEEI 1098
Cdd:PLN03130 646 VAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TVRDNILFGSPFDPERYERA 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1099 RKETdKMIEDLELSnKRHSLVQ------TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYK-PGR 1171
Cdd:PLN03130 714 IDVT-ALQHDLDLL-PGGDLTEigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElRGK 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1172 TILLST---HHMDEAdllgDRIAIISHGKLK--------CCGSPLFLKGAYGDGYRLTLVKQPAE---PGTSQEPGLASS 1237
Cdd:PLN03130 792 TRVLVTnqlHFLSQV----DRIILVHEGMIKeegtyeelSNNGPLFQKLMENAGKMEEYVEENGEeedDQTSSKPVANGN 867
|
....*....
gi 110225379 1238 PSGCPRLSS 1246
Cdd:PLN03130 868 ANNLKKDSS 876
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1009-1178 |
2.96e-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: 45.94 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1009 LSLNLYENQVVsFL-GHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRknlgmcpQH-------NVLFDRLT 1079
Cdd:COG4615 351 IDLTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYR-------QLfsavfsdFHLFDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1080 VEEhlwfysrlksmaQEEIRKETDKMIEDLELSNK------RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1153
Cdd:COG4615 423 GLD------------GEADPARARELLERLELDHKvsvedgRFSTTD-LSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180 190
....*....|....*....|....*....|
gi 110225379 1154 PYARRAIWDLILkykP-----GRTILLSTH 1178
Cdd:COG4615 490 PEFRRVFYTELL---PelkarGKTVIAISH 516
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2180-2244 |
3.60e-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: 3.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110225379 2180 DKPAGTYSGGNKR--KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHS 2244
Cdd:cd03238 82 GQKLSTLSGGELQrvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2070-2274 |
4.09e-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: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2070 VDRLCLGVRPGECFGLLGVNGAGKTSTF----KMLtgdesTTGGEAFVNGHSVLKDLLQV-QQSLGYCPQFDALFDElTA 2144
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLsaflRLL-----NTEGDIQIDGVSWNSVPLQKwRKAFGVIPQKVFIFSG-TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2145 REHLQLYTRlrgipWKDEaQVVKWALE---KLELTKYADK-----PAGTY--SGGNKRKLSTAIALIGYPAFIFLDEPTT 2214
Cdd:cd03289 94 RKNLDPYGK-----WSDE-EIWKVAEEvglKSVIEQFPGQldfvlVDGGCvlSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2215 GMDPKARRFLwNLILDLIKTGRSVVLTSHSMeecEAL--CTRLAIMVNGRLRCLGSIQHLKN 2274
Cdd:cd03289 168 HLDPITYQVI-RKTLKQAFADCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLLN 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2073-2243 |
5.18e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2073 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGdeSTTG-GEAFVNGHSvLKDLLQVQQSL--GY-CPQFDALFdELTAREHL 2148
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG--LLPGsGSIQFAGQP-LEAWSAAELARhrAYlSQQQTPPF-AMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2149 QLYtrlrgIPWKDEAQVVKWALEKL-ELTKYADK---PAGTYSGGN-KRKLSTAIALIGYPA------FIFLDEPTTGMD 2217
Cdd:PRK03695 91 TLH-----QPDKTRTEAVASALNEVaEALGLDDKlgrSVNQLSGGEwQRVRLAAVVLQVWPDinpagqLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*.
gi 110225379 2218 PKARRFLWNLILDLIKTGRSVVLTSH 2243
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2045-2230 |
6.03e-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: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2045 ADNDMVKIENLTkVYKSRkiGRILaVDRLCLGVRPGEcfGLL--GVNGAGKTSTFKMLTG-DESTTGgeafvnghsvlkd 2121
Cdd:COG4178 358 SEDGALALEDLT-LRTPD--GRPL-LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGlWPYGSG------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2122 llqvqqSLGYCPQFDALFdeLTAREHLQLYTrLRGI--------PWKDEAqvVKWALEKLELTKYADKP------AGTYS 2187
Cdd:COG4178 419 ------RIARPAGARVLF--LPQRPYLPLGT-LREAllypataeAFSDAE--LREALEAVGLGHLAERLdeeadwDQVLS 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110225379 2188 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2230
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
2187-2243 |
6.16e-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: 6.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110225379 2187 SGGNKRKLSTAIAL-----IGYPaFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2243
Cdd:cd03227 79 SGGEKELSALALILalaslKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
987-1049 |
9.52e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 9.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110225379 987 LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI 1049
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 ... |
2050-2217 |
2.17e-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: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2050 VKIENLTKVYKSrKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-DLLQVQQS 2128
Cdd:cd03369 7 IEVENLSVRYAP-DLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2129 LGYCPQFDALFDElTAREHLQLYTRLrgipwkDEAQVvkwaLEKLELTKYADkpagTYSGGNKRKLSTAIALIGYPAFIF 2208
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDPFDEY------SDEEI----YGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLV 148
|
....*....
gi 110225379 2209 LDEPTTGMD 2217
Cdd:cd03369 149 LDEATASID 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
998-1221 |
2.46e-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: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 998 YKNDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVLFD 1076
Cdd:cd03288 29 YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSIILQDPILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1077 rltveehlwfySRLKSMAQEEIRKETDKMIEDLELSNKRhSLVQTLSGGM--------------KRKL-SVAIAFVGGSR 1141
Cdd:cd03288 109 -----------GSIRFNLDPECKCTDDRLWEALEIAQLK-NMVKSLPGGLdavvteggenfsvgQRQLfCLARAFVRKSS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1142 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPLFLKgAYGDGYRLTLVK 1221
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENLL-AQEDGVFASLVR 254
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
987-1149 |
3.19e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 987 LVVCVDKLTKVYknDKKMALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatiyghdIR-TEmdeiRKNL 1065
Cdd:PRK15064 318 NALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKwSE----NANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1066 GMCPQ-HNVLFDR-LTVEEhlWfysrlksMAQEEIRKETDKMI-----------EDLelsNKRhslVQTLSGGMKRKLSV 1132
Cdd:PRK15064 385 GYYAQdHAYDFENdLTLFD--W-------MSQWRQEGDDEQAVrgtlgrllfsqDDI---KKS---VKVLSGGEKGRMLF 449
|
170
....*....|....*..
gi 110225379 1133 AIAFVGGSRAIILDEPT 1149
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPT 466
|
|
| MelB |
COG2211 |
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]; |
705-830 |
4.73e-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: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 705 MMPLCMVISWVYSVAMTIQHIVAEKEH-RLKEVMKTMgLNNAVHWVAWFITGFVQLSISVTAlTAILKYGQVLMHSHVLI 783
Cdd:COG2211 188 IFAVLGLLAFLLTFFGTKERPVPEEEKvSLKESLKAL-LKNRPFLLLLLAYLLFFLALALVA-ALLLYYFKYVLGLSAAL 265
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 110225379 784 IWLFLAVYAVATIMFCFLVSVL---YSKAKLASAcGGIIYFLSYVPYMYV 830
Cdd:COG2211 266 VGLLLALYFLAALLGAPLWPRLakrFGKKKAFII-GLLLAALGLLLLFFL 314
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2193-2275 |
7.15e-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: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 2193 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2271
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 110225379 2272 LKNR 2275
Cdd:COG4170 246 ILKS 249
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1116-1197 |
8.99e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110225379 1116 HSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAII 1193
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
....
gi 110225379 1194 SHGK 1197
Cdd:PRK15093 233 YCGQ 236
|
|
| |
