|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
705-1285 |
3.24e-171 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 520.49 E-value: 3.24e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 705 SIFRIAALNKPEIPVLILGSISAAANGVILPIFGILISSVIKAFFQPPkklkeDTS---FWAIIFMVLGFASIIAYPAQT 781
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-----DLSallLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 782 FFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLAC 861
Cdd:COG1132 83 YLLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 862 WQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQ 941
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 942 GIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSVFRVFFALTMAAMAISQSSSLSPDSSKADVAAASIFAIMDR 1021
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1022 ESKIdPSVESGRVLDNVKGDIELRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEI 1101
Cdd:COG1132 321 PPEI-PDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1102 TLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQ 1181
Cdd:COG1132 398 LIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP-DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1182 LSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|....
gi 15226477 1262 KHDTLINiKDGVYASLVQLHLTAA 1285
Cdd:COG1132 557 THEELLA-RGGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
46-1280 |
1.12e-168 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 541.16 E-value: 1.12e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 46 VPFYKLFAFADSFDFLLMILGTLGSIGNGLGFPLMTLLFGDLIdafgeNQTNTTDKVSKVALKFVWLGIGTFAAAFLQLS 125
Cdd:PTZ00265 45 IPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIM-----KNMNLGENVNDIIFSLVLIGIFQFILSFISSF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 126 GWMISGERQAARIRSLYLKTILRQDIAFFDidTNTGEVVgRMSGDTVLIQ--DAMGEKVGKAIQLLATFVGGFVIAFVRG 203
Cdd:PTZ00265 120 CMDVVTTKILKTLKLEFLKSVFYQDGQFHD--NNPGSKL-TSDLDFYLEQvnAGIGTKFITIFTYASAFLGLYIWSLFKN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 204 WLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYN--KHLVTAY--KA 279
Cdd:PTZ00265 197 ARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNlsEKLYSKYilKA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 280 GVIEGGSTGLGLGtlflVVFCSYALAVWYGGKLIL--------DKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQ 351
Cdd:PTZ00265 277 NFMESLHIGMING----FILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 352 AAAYKMFETIERRPNIDSySTNGKVLDDIKgDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSL 431
Cdd:PTZ00265 353 EATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 432 IERFYDPQAGDVLI-DGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYG--------------KEDA--------- 487
Cdd:PTZ00265 431 IERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDGndsqenknk 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 488 --------------------TTEEIKAA--------AELANASK------FVDKLPQGLDTMVGEHGTQLSGGQKQRIAV 533
Cdd:PTZ00265 511 rnscrakcagdlndmsnttdSNELIEMRknyqtikdSEVVDVSKkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISI 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRNADMIAVIHQGkivEKGSHTELLKDP 611
Cdd:PTZ00265 591 ARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNR---ERGSTVDVDIIG 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 612 EGAYSQLIRLQEEKKSDE----NAAEEQKMSS-----IESFKQSSLRKSSLG---------RSLSKGGSSRGN------- 666
Cdd:PTZ00265 668 EDPTKDNKENNNKNNKDDnnnnNNNNNNKINNagsyiIEQGTHDALMKNKNGiyytminnqKVSSKKSSNNDNdkdsdmk 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 667 SSRHSFNMFGF-PAGIDGNVVQDQE----------EDDTTQPKTEPKKVSIFRIAALNKPEIP----------------- 718
Cdd:PTZ00265 748 SSAYKDSERGYdPDEMNGNSKHENEsasnkksckmSDENASENNAGGKLPFLRNLFKRKPKAPnnlrivyreifsykkdv 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 719 VLILGSISAAanGVILPIFGILISSVIKAFFQpPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSM 798
Cdd:PTZ00265 828 TIIALSILVA--GGLYPVFALLYAKYVSTLFD-FANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRR 904
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 799 CFEKVVHMEVGWFDEPENSSGTIGARLSADAATIR-GLVGDSLaqtvqnlssILAGLIIAFLACWQLAFVvlaMLPLI-A 876
Cdd:PTZ00265 905 LFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKtGLVNNIV---------IFTHFIVLFLVSMVMSFY---FCPIVaA 972
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 877 LNGFLYMKFMKGFSADAK-------------------------KMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKC 931
Cdd:PTZ00265 973 VLTGTYFIFMRVFAIRARltankdvekkeinqpgtvfaynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAI 1052
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 932 EGPMKNGIRQGIVSGIGFGFS----FFVlfSSYAasFYVGARLVDDGKTTFDSVFRVFFALTMAAMAISQSSSLSPDSSK 1007
Cdd:PTZ00265 1053 DYSNKGQKRKTLVNSMLWGFSqsaqLFI--NSFA--YWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSEN 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1008 ADVAAASIFAIMDRESKIDPSVESGRVLDN---VKGDIELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKS 1084
Cdd:PTZ00265 1129 AKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKS 1208
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1085 TVIALLQRFYD------------------------------------------------------PDSGEITLDGVEIKS 1110
Cdd:PTZ00265 1209 TVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICD 1288
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1111 LRLKWLRQQTGLVSQEPILFNETIRANIAYGKgGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRV 1190
Cdd:PTZ00265 1289 YNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK-EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRI 1367
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALDAESERVVQ----DALDRvmVNRTTIVVAHRLSTIKNADVIAVVKN----GVIVE-KG 1261
Cdd:PTZ00265 1368 AIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDK--ADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHG 1445
|
1450
....*....|....*....
gi 15226477 1262 KHDTLINIKDGVYASLVQL 1280
Cdd:PTZ00265 1446 THEELLSVQDGVYKKYVKL 1464
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
62-625 |
5.03e-167 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 509.71 E-value: 5.03e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 62 LMILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTntTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSL 141
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDALLAGGD--LSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 142 YLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAG 221
Cdd:COG1132 100 LFEHLLRLPLSFFD-RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 222 ALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCS 301
Cdd:COG1132 179 RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 302 YALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQAAAYKMFETIERRPNIDSySTNGKVLDDIK 381
Cdd:COG1132 259 LALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:COG1132 338 GEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:COG1132 416 IGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDP 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQLIRL 621
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRL 574
|
....
gi 15226477 622 QEEK 625
Cdd:COG1132 575 QFGE 578
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
384-622 |
1.05e-137 |
|
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: 419.25 E-value: 1.05e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKdPEGAYSQLIRLQ 622
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1042-1280 |
3.06e-135 |
|
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: 412.70 E-value: 3.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPK 1201
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINiKDGVYASLVQL 1280
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKA 237
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
112-622 |
4.88e-130 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 411.79 E-value: 4.88e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 112 LGIGTFAAAFLQLSgwmiSGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLAT 191
Cdd:TIGR02204 71 LALGTAARFYLVTW----LGERVVADIRRAVFAHLISLSPSFFD-KNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALM 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 192 FVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNK 271
Cdd:TIGR02204 146 CIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 272 HLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQ 351
Cdd:TIGR02204 226 AVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 352 AAAYKMFETIERRPNIDSYSTNGKVLDDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSL 431
Cdd:TIGR02204 306 GAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 432 IERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQG 511
Cdd:TIGR02204 386 LLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEG 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 512 LDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIA 591
Cdd:TIGR02204 466 YDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIV 545
|
490 500 510
....*....|....*....|....*....|.
gi 15226477 592 VIHQGKIVEKGSHTELLKDpEGAYSQLIRLQ 622
Cdd:TIGR02204 546 VMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
706-1279 |
1.12e-129 |
|
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: 415.77 E-value: 1.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 706 IFRIAALNKPEIPVLILGSISAAANGVILPIF-GILISSVIKAffqppkklkEDTSFW---AIIFMVLGFASIIAYPAQT 781
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFtQVVIDRVLPN---------QDLSTLwvlAIGLLLALLFEGLLRLLRS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 782 FFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSaDAATIRGLVGDSLAQTVQNLSSILAGLIIAFLAC 861
Cdd:COG2274 218 YLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES--RSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 862 WQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQ 941
Cdd:COG2274 295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 942 GIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSvfrvFFALTMAA----MAISQSSSLSPDSSKADVAAASIFA 1017
Cdd:COG2274 375 RRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQ----LIAFNILSgrflAPVAQLIGLLQRFQDAKIALERLDD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1018 IMDRESKIDPSvESGRVLDNVKGDIELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPD 1097
Cdd:COG2274 451 ILDLPPEREEG-RSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1098 SGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMVGE 1177
Cdd:COG2274 529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDP-DATDEEIIEAARLAGLHDFIEALPMGYDTVVGE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1178 RGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVI 1257
Cdd:COG2274 608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
570 580
....*....|....*....|..
gi 15226477 1258 VEKGKHDTLINiKDGVYASLVQ 1279
Cdd:COG2274 688 VEDGTHEELLA-RKGLYAELVQ 708
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
110-622 |
2.09e-124 |
|
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: 401.52 E-value: 2.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 110 VWLGIGTFAAAFLQ-----LSGWMIS--GERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSgDTVLIQDAM-GEK 181
Cdd:COG2274 196 WVLAIGLLLALLFEgllrlLRSYLLLrlGQRIDLRLSSRFFRHLLRLPLSFFE-SRSVGDLASRFR-DVESIREFLtGSL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 182 VGKAIQLLATFVGGFVIAFVrGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTG 261
Cdd:COG2274 274 LTALLDLLFVLIFLIVLFFY-SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 262 EKQAISNYNKHLVTAYKAGV-IEGGSTGLGLGTLFLVVFcSYALAVWYGGKLILDKGYTGGQVL--NIIIAVLTGSM-SL 337
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFkLRRLSNLLSTLSGLLQQL-ATVALLWLGAYLVIDGQLTLGQLIafNILSGRFLAPVaQL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 338 GQtspcLSAFAAGQAAAYKMFETIERRPNIDSYSTNGKVLDDIKGDIELKDVYFTYPARpDEQIFRGFSLFISSGTTVAL 417
Cdd:COG2274 432 IG----LLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 418 VGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAE 497
Cdd:COG2274 507 VGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAAR 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 498 LANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVV 577
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15226477 578 AHRLSTVRNADMIAVIHQGKIVEKGSHTELLKdPEGAYSQLIRLQ 622
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
707-1277 |
1.01e-123 |
|
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: 394.85 E-value: 1.01e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 707 FRIAALNKPEIPVLILGSISAAANGVILPIFGILISSVIKAFFQPPKKLKedtsFWAIIFMVLGFASI--IAYPAQTFFF 784
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSV----LWWVPLVVIGLAVLrgICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 785 AIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQL 864
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 865 AFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIV 944
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 945 SGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSvFRVFFAlTMAAM--AISQSSSLSPDSSKADVAAASIFAIMDRE 1022
Cdd:TIGR02203 237 GSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT-AMIALirPLKSLTNVNAPMQRGLAAAESLFTLLDSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1023 SKIDpsvESGRVLDNVKGDIELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEIT 1102
Cdd:TIGR02203 315 PEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1103 LDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQL 1182
Cdd:TIGR02203 391 LDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1183 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGK 1262
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGT 550
|
570
....*....|....*
gi 15226477 1263 HDTLINiKDGVYASL 1277
Cdd:TIGR02203 551 HNELLA-RNGLYAQL 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
112-619 |
1.20e-123 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 399.48 E-value: 1.20e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 112 LGIGTFAAAFLQLSGWMISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLAT 191
Cdd:TIGR00958 210 LSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD-ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 192 FVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYN- 270
Cdd:TIGR00958 289 LLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKe 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 271 --KHLVTAYKAGVIEGGStglglgtlFLVV--FCSYALAV---WYGGKLILDKGYTGGQvlniIIAVLTGSMSLGQTSPC 343
Cdd:TIGR00958 369 alEETLQLNKRKALAYAG--------YLWTtsVLGMLIQVlvlYYGGQLVLTGKVSSGN----LVSFLLYQEQLGEAVRV 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 344 LSAFAAGQAAAY----KMFETIERRPNIDSysTNGKVLDDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVG 419
Cdd:TIGR00958 437 LSYVYSGMMQAVgaseKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVG 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 420 QSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELA 499
Cdd:TIGR00958 515 PSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAA 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 500 NASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEalDRIMVNRTTVVVAH 579
Cdd:TIGR00958 595 NAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAH 672
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15226477 580 RLSTVRNADMIAVIHQGKIVEKGSHTELLKDPeGAYSQLI 619
Cdd:TIGR00958 673 RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
706-1278 |
2.66e-122 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 396.02 E-value: 2.66e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 706 IFRIAALNKPEIPVLILGS---ISAAANGVILPIFGILISSVIKAFFQPPKKLKedtsfwAIIFM-VLGFASIIAYPAQT 781
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFvflTLSSLGEMFIPFYTGRVIDTLGGDKGPPALAS------AIFFMcLLSIASSVSAGLRG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 782 FFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLAC 861
Cdd:TIGR00958 223 GSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 862 WQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQ 941
Cdd:TIGR00958 301 PRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 942 GIVsgigfgFSFFVLFSSYAASF------YVGARLVDDGKTTFDSVfrVFFAL-TMA-AMAISQSSSLSPDSSKADVAAA 1013
Cdd:TIGR00958 381 ALA------YAGYLWTTSVLGMLiqvlvlYYGGQLVLTGKVSSGNL--VSFLLyQEQlGEAVRVLSYVYSGMMQAVGASE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1014 SIFAIMDRESKIDPSVEsgRVLDNVKGDIELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRF 1093
Cdd:TIGR00958 453 KVFEYLDRKPNIPLTGT--LAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1094 YDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKgGDASESEIVSSAELSNAHGFISGLQQGYDT 1173
Cdd:TIGR00958 531 YQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL-TDTPDEEIMAAAKAANAHDFIMEFPNGYDT 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1174 MVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDalDRVMVNRTTIVVAHRLSTIKNADVIAVVK 1253
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLK 687
|
570 580
....*....|....*....|....*
gi 15226477 1254 NGVIVEKGKHDTLINiKDGVYASLV 1278
Cdd:TIGR00958 688 KGSVVEMGTHKQLME-DQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
710-1025 |
6.87e-121 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 377.56 E-value: 6.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 710 AALNKPEIPVLILGSISAAANGVILPIFGILISSVIKAFFQP-PKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAG 788
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPdDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 789 CKLVQRIRSMCFEKVVHMEVGWFDEPENSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVV 868
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 869 LAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIG 948
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 949 FGFSFFVLFSSYAASFYVGARLVDDGKTTFDSVFRVFFALTMAAMAISQSSSLSPDSSKADVAAASIFAIMDRESKI 1025
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
384-618 |
1.09e-112 |
|
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: 352.30 E-value: 1.09e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQL 618
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
764-1281 |
8.71e-111 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 360.49 E-value: 8.71e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 764 IIFMVL-GFASIIAypaqTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQ 842
Cdd:PRK11176 72 IGLMILrGITSFIS----SYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRITYDSEQVASSSSGALIT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 843 TVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIAlngFLYMKFMKGFSADAKKMYGEASQVANDAVGSI---RTVASFCA 919
Cdd:PRK11176 146 VVREGASIIGLFIMMFYYSWQLSLILIVIAPIVS---IAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLkghKEVLIFGG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 920 E-------DKVMNMYSKKcegPMK----NGIRQGIVSGIGfgfSFFVLFSSYAASFyvgaRLVDDGKT--TFDSVFRVFF 986
Cdd:PRK11176 223 QevetkrfDKVSNRMRQQ---GMKmvsaSSISDPIIQLIA---SLALAFVLYAASF----PSVMDTLTagTITVVFSSMI 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 987 ALTMAAMAISQSSSLSPdssKADVAAASIFAIMDRESKIDpsvESGRVLDNVKGDIELRHVSFKYPARpDVQIFQDLCLS 1066
Cdd:PRK11176 293 ALMRPLKSLTNVNAQFQ---RGMAACQTLFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFK 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1067 IRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGGDA 1146
Cdd:PRK11176 366 IPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQY 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1147 SESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDR 1226
Cdd:PRK11176 446 SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDE 525
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1227 VMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINiKDGVYAslvQLH 1281
Cdd:PRK11176 526 LQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA-QNGVYA---QLH 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
48-622 |
2.16e-108 |
|
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: 353.64 E-value: 2.16e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 48 FYKLFAFADSFDFLLmILGTLGSIGNGLGFPLMTLLFGDLID-AFGENQTNTTDKVS-KVALKFVWLGIGTFAAAFL--Q 123
Cdd:TIGR02203 2 FRRLWSYVRPYKAGL-VLAGVAMILVAATESTLAALLKPLLDdGFGGRDRSVLWWVPlVVIGLAVLRGICSFVSTYLlsW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 124 LSGWMISGerqaarIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRG 203
Cdd:TIGR02203 81 VSNKVVRD------IRVRMFEKLLGLPVSFFD-RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 204 WLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKhlVTAYKAGVIE 283
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDA--VSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 284 GGSTGLGLGTLFLVVFCSYALAV--WYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQAAAYKMFETI 361
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVvlFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 362 ERRPNIDsysTNGKVLDDIKGDIELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAG 441
Cdd:TIGR02203 312 DSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 442 DVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGK-EDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHG 520
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 521 TQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVE 600
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
570 580
....*....|....*....|..
gi 15226477 601 KGSHTELLkDPEGAYSQLIRLQ 622
Cdd:TIGR02203 548 RGTHNELL-ARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1042-1277 |
3.55e-108 |
|
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: 339.98 E-value: 3.55e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPK 1201
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRP-GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINiKDGVYASL 1277
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKL 233
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
63-345 |
4.56e-106 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 337.14 E-value: 4.56e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTNTTDK------VSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAA 136
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeflddVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 137 RIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD-KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 217 LVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFL 296
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15226477 297 VVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLS 345
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQ 288
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
356-634 |
3.13e-104 |
|
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: 343.34 E-value: 3.13e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 356 KMFETIERRPNIDSySTNGKVLDDIKGDIELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF 435
Cdd:COG5265 331 RMFDLLDQPPEVAD-APDAPPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 436 YDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTM 515
Cdd:COG5265 408 YDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTR 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 516 VGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQ 595
Cdd:COG5265 488 VGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEA 567
|
250 260 270
....*....|....*....|....*....|....*....
gi 15226477 596 GKIVEKGSHTELLKDpEGAYSQLIRLQEEKKSDENAAEE 634
Cdd:COG5265 568 GRIVERGTHAELLAQ-GGLYAQMWARQQEEEEAEEALAA 605
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1016-1280 |
9.94e-104 |
|
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: 341.80 E-value: 9.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1016 FAIMDRESKIDPSVESgRVLDNVKGDIELRHVSFKYpaRPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYD 1095
Cdd:COG5265 333 FDLLDQPPEVADAPDA-PPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1096 PDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMV 1175
Cdd:COG5265 410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP-DASEEEVEAAARAAQIHDFIESLPDGYDTRV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1176 GERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNG 1255
Cdd:COG5265 489 GERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAG 568
|
250 260
....*....|....*....|....*
gi 15226477 1256 VIVEKGKHDTLINiKDGVYASLVQL 1280
Cdd:COG5265 569 RIVERGTHAELLA-QGGLYAQMWAR 592
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1042-1277 |
1.31e-100 |
|
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: 319.56 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPK 1201
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRP-DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINiKDGVYASL 1277
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEM 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
384-622 |
2.76e-99 |
|
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: 316.09 E-value: 2.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLkDPEGAYSQLIRLQ 622
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
373-622 |
2.58e-97 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 323.51 E-value: 2.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 373 NGK-VLDDIKGDIELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLK 451
Cdd:PRK11176 330 EGKrVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 452 EFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDA-TTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQR 530
Cdd:PRK11176 409 DYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 531 IAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
250
....*....|..
gi 15226477 611 pEGAYSQLIRLQ 622
Cdd:PRK11176 569 -NGVYAQLHKMQ 579
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
382-609 |
7.39e-95 |
|
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: 303.76 E-value: 7.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
708-1267 |
2.25e-94 |
|
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: 314.77 E-value: 2.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 708 RIAALNKPEIPVLILGSISAAANGVILPIFGILISSVIKAFFQPPKKLkeDTSFWAIIFMVLGFA--SIIAYpAQTFFFA 785
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPL--SALLPLLGLLLAVLLlrALLAW-LRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 786 IAGCKLVQRIRSMCFEKVVHMEVGWFDEPenSSGTIGARLSADAATIRGLVGDSLAQTVqnLSSILAGLIIAFLAC--WQ 863
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLLTEGVEALDGYFARYLPQLF--LAALVPLLILVAVFPldWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 864 LAFVVLAMLPLIALngFLYMkFMKGFSADAKKMYGEASQVAN---DAVGSIRTVASFCAEDKVMNMYSKKCEG----PMK 936
Cdd:COG4988 160 SGLILLVTAPLIPL--FMIL-VGKGAAKASRRQWRALARLSGhflDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrTMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 937 ngirqgiVSGIGFgFSFFVL-FSSY----AASFYVGARLVDdGKTTFdsvFRVFFAL-------------------TMAA 992
Cdd:COG4988 237 -------VLRVAF-LSSAVLeFFASlsiaLVAVYIGFRLLG-GSLTL---FAALFVLllapefflplrdlgsfyhaRANG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 993 MAisqssslspdsskadvAAASIFAIMDREskiDPSVESGRVLDNVKG--DIELRHVSFKYPARPdvQIFQDLCLSIRAG 1070
Cdd:COG4988 305 IA----------------AAEKIFALLDAP---EPAAPAGTAPLPAAGppSIELEDVSFSYPGGR--PALDGLSLTIPPG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1071 KTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESE 1150
Cdd:COG4988 364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRP-DASDEE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1151 IVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN 1230
Cdd:COG4988 443 LEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG 522
|
570 580 590
....*....|....*....|....*....|....*..
gi 15226477 1231 RTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLI 1267
Cdd:COG4988 523 RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
722-1278 |
1.87e-92 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 310.35 E-value: 1.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 722 LGSISAAANgVILPIFG----ILISSVIKAffqppkkLKEDTSFWAIIFM--VLGFASIIAYpaqtFFFAIAGCKLVQRI 795
Cdd:PRK13657 20 LGILLAVAN-VLLAAATfaepILFGRIIDA-------ISGKGDIFPLLAAwaGFGLFNIIAG----VLVARHADRLAHRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 796 RS--MC--FEKVVHMEVGWFDEpENSSGTIGARLSAdaatIRGLVGDSLAQTVQNLSSILAGLI---IAFLACWQLAFVV 868
Cdd:PRK13657 88 RLavLTeyFERIIQLPLAWHSQ-RGSGRALHTLLRG----TDALFGLWLEFMREHLATLVALVVllpLALFMNWRLSLVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 869 LAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFC---AEDKVMNMYSKK---CEGPMKNGirQG 942
Cdd:PRK13657 163 VVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQALRDIADNllaAQMPVLSW--WA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 943 IVSGIGFGFSFFvlfsSYAASFYVGARLVDDGKTTFDSVfrVFFaLTMAAMAISQSSSLSPDSSKADVAAA--------- 1013
Cdd:PRK13657 241 LASVLNRAASTI----TMLAILVLGAALVQKGQLRVGEV--VAF-VGFATLLIGRLDQVVAFINQVFMAAPkleeffeve 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1014 -SIFAIMDRESKIDPSvesgrvldNVKGDIELRHVSFKYPARPdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQR 1092
Cdd:PRK13657 314 dAVPDVRDPPGAIDLG--------RVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1093 FYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYD 1172
Cdd:PRK13657 384 VFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHDFIERKPDGYD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1173 TMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVV 1252
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVF 542
|
570 580
....*....|....*....|....*.
gi 15226477 1253 KNGVIVEKGKHDTLINiKDGVYASLV 1278
Cdd:PRK13657 543 DNGRVVESGSFDELVA-RGGRFAALL 567
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1040-1271 |
1.04e-90 |
|
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: 292.21 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYpaRPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQ 1119
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKD 1199
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRP-NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1200 PKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKD 1271
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
356-609 |
1.12e-90 |
|
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: 304.37 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 356 KMFETIERrPNIDSYSTNGKVLDDIKGDIELKDVYFTYPARpdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF 435
Cdd:COG4988 310 KIFALLDA-PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 436 YDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTM 515
Cdd:COG4988 387 LPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 516 VGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQ 595
Cdd:COG4988 467 LGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDD 546
|
250
....*....|....
gi 15226477 596 GKIVEKGSHTELLK 609
Cdd:COG4988 547 GRIVEQGTHEELLA 560
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
377-635 |
2.54e-89 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 301.49 E-value: 2.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 377 LDDIKGDIELKDVYFTYPARPdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLK 456
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 457 WIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARA 536
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLkDPEGAYS 616
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV-ARGGRFA 564
|
250 260
....*....|....*....|...
gi 15226477 617 QLIR----LQEEKKSDENAAEEQ 635
Cdd:PRK13657 565 ALLRaqgmLQEDERRKQPAAEGA 587
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
378-598 |
1.36e-85 |
|
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: 277.81 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 378 DDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKW 457
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 458 IRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKI 598
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1042-1280 |
1.84e-85 |
|
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: 277.83 E-value: 1.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYpaRPD-VQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQT 1120
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFNETIRANIAYGKGGdASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDP 1200
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG-MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1201 KVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINiKDGVYASLVQL 1280
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLYQL 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
384-622 |
7.28e-84 |
|
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: 273.59 E-value: 7.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYpaRPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKI 462
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 543 ILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLkDPEGAYSQLIRLQ 622
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
847-1280 |
1.31e-83 |
|
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: 284.74 E-value: 1.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 847 LSSILAGLIIAFLAcWQLAFVVLAMLPLIALNG-FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMN 925
Cdd:COG4987 141 LVILAAVAFLAFFS-PALALVLALGLLLAGLLLpLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 926 MYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGktTFDSVFRVFFALT-MAAM-AISQSSSLSP 1003
Cdd:COG4987 220 RLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAG--ALSGPLLALLVLAaLALFeALAPLPAAAQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1004 DSSKADVAAASIFAIMDRESKIDPSVESGRVLDNVkgDIELRHVSFKYPARPDvQIFQDLCLSIRAGKTVALVGESGSGK 1083
Cdd:COG4987 298 HLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGP--SLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1084 STVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGF 1163
Cdd:COG4987 375 STLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP-DATDEELWAALERVGLGDW 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1164 ISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTI 1243
Cdd:COG4987 454 LAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL 533
|
410 420 430
....*....|....*....|....*....|....*..
gi 15226477 1244 KNADVIAVVKNGVIVEKGKHDTLINiKDGVYASLVQL 1280
Cdd:COG4987 534 ERMDRILVLEDGRIVEQGTHEELLA-QNGRYRQLYQR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1036-1257 |
2.39e-83 |
|
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: 271.65 E-value: 2.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1036 DNVKGDIELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKW 1115
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 LRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARA 1195
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQ-SCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1196 IVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVI 1257
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
382-621 |
5.54e-83 |
|
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: 283.20 E-value: 5.54e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYPARPdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:COG4987 332 PSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:COG4987 411 IAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPeGAYSQLIRL 621
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQR 569
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1042-1255 |
4.91e-79 |
|
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: 257.31 E-value: 4.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNETIRANIaygkggdaseseivssaelsnahgfisglqqgydtmvgergiqLSGGQKQRVAIARAIVKDPK 1201
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNG 1255
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
160-624 |
2.53e-78 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 273.54 E-value: 2.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 160 TGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGgFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAY 239
Cdd:TIGR01846 235 VGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVF-LAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 240 AKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYT 319
Cdd:TIGR01846 314 AAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 320 GGQVLNIiiavltgSMSLGQ-TSPCLSAFAAgqaaaYKMFE----TIERRPNI-----DSYSTNGKVLDDIKGDIELKDV 389
Cdd:TIGR01846 394 PGQLVAF-------NMLAGRvTQPVLRLAQL-----WQDFQqtgiALERLGDIlnsptEPRSAGLAALPELRGAITFENI 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 390 YFTYpaRPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQE 468
Cdd:TIGR01846 462 RFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 469 PVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:TIGR01846 540 NVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDE 619
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 549 ATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQLIRLQEE 624
Cdd:TIGR01846 620 ATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-QGLYARLWQQQSG 694
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
384-597 |
2.98e-78 |
|
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: 255.00 E-value: 2.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGK 597
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
720-1015 |
9.34e-78 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 258.94 E-value: 9.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 720 LILGSISAAANGVILPIFGILISSVIKAF------FQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQ 793
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 794 RIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLP 873
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 874 LIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSF 953
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 954 FVLFSSYAASFYVGARLVDDGKTTFDSVFRVFFALTMAAMAISQSSSLSPDSSKADVAAASI 1015
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
59-367 |
1.08e-71 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 242.36 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 59 DFLLMILGTLGSIGNGLGFPLMTLLFGDLIDAFGE-NQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAAR 137
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLpDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 138 IRSLYLKTILRQDIAFFDIDTN-TGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18578 87 LRKLAFRAILRQDIAWFDDPENsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 217 LVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFL 296
Cdd:cd18578 167 LLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQS 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 297 VVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQAAAYKMFETIERRPNI 367
Cdd:cd18578 247 LTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
382-602 |
2.93e-71 |
|
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: 237.49 E-value: 2.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYPARPDEQIfRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 602
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
704-1279 |
6.47e-71 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 249.04 E-value: 6.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 704 VSIFRIAALNKPEIPVLILGSISAAANGVILPI-FGILISSVIKaffqppkklKEDTSFWAIIFMVLGFASIIAYPAqtf 782
Cdd:TIGR01192 8 VRALSYLNVHKNRVLLIVIANITLAAITIAEPIlFGRIIDAISS---------KSDVLPTLALWAGFGVFNTIAYVL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 783 fFAIAGCKLVQRIRSM----CFEKVVHMEVGWFDEpENSSGTIGARLSAdAATIRGLVGDSLAQTVQNLSSILAGLIIAF 858
Cdd:TIGR01192 76 -VAREADRLAHGRRATllteAFGRIISMPLSWHQQ-RGTSNALHTLLRA-TETLFGLWLEFMRQHLATFVALFLLIPTAF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 859 LACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASF---CAEDKVMNMYSKK---CE 932
Cdd:TIGR01192 153 AMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYnriEAETSALKQFTNNllsAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 933 GPMKNGirQGIVSGIGFGFSFFvlfsSYAASFYVGARLVDDGKTtfdSVFRVFFALTMAAMAISQSSSLSPDSSKADVAA 1012
Cdd:TIGR01192 233 YPVLDW--WALASGLNRMASTI----SMMCILVIGTVLVIKGEL---SVGEVIAFIGFANLLIGRLDQMSGFITQIFEAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1013 ASIFAIMDRESKIDPSVESG--RVLDNVKGDIELRHVSFKYPARPdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALL 1090
Cdd:TIGR01192 304 AKLEDFFDLEDSVFQREEPAdaPELPNVKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1091 QRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGGdASESEIVSSAELSNAHGFISGLQQG 1170
Cdd:TIGR01192 382 QRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREG-ATDEEVYEAAKAAAAHDFILKRSNG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1171 YDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIA 1250
Cdd:TIGR01192 461 YDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVL 540
|
570 580
....*....|....*....|....*....
gi 15226477 1251 VVKNGVIVEKGKHDTLINiKDGVYASLVQ 1279
Cdd:TIGR01192 541 FLDQGRLIEKGSFQELIQ-KDGRFYKLLR 568
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
158-1279 |
1.23e-69 |
|
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: 257.57 E-value: 1.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 158 TNTGEVVGRMSGDTVLIQDamgekvgkaiqlLATFVG-------GFVIAFVRGWL-LTLVMLSSIPLLVMAGALLAIVIA 229
Cdd:TIGR00957 412 STVGEIVNLMSVDAQRFMD------------LATYINmiwsaplQVILALYFLWLnLGPSVLAGVAVMVLMVPLNAVMAM 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 230 KTASRgQTAYAKAA----TVVEQTIGSIRTVASFTGE----KQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCS 301
Cdd:TIGR00957 480 KTKTY-QVAHMKSKdnriKLMNEILNGIKVLKLYAWElaflDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALIT 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 302 YALAVWYGGKLILD--KGYTGGQVLNI-----------IIAVLTGSMSLGQTSPCLSAFAAGQaaaykmfETIERRPnid 368
Cdd:TIGR00957 559 FAVYVTVDENNILDaeKAFVSLALFNIlrfplnilpmvISSIVQASVSLKRLRIFLSHEELEP-------DSIERRT--- 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 369 systngkVLDDIKGDIELKDVYFTYpARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGi 448
Cdd:TIGR00957 629 -------IKPGEGNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG- 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 449 nlkefqlkwirsKIGLVSQEPVLFTASIKDNIAYGK---EDATTEEIKAAAELANaskfVDKLPQGLDTMVGEHGTQLSG 525
Cdd:TIGR00957 700 ------------SVAYVPQQAWIQNDSLRENILFGKalnEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSG 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEAL---DRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 602
Cdd:TIGR00957 764 GQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 603 SHTELLkDPEGAYSQLIRLQEEKKSDENAAEEQKMSSIESFKQSSLRKSS----------LGRSLSKGGSSRGNSSRHsf 672
Cdd:TIGR00957 844 SYQELL-QRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLIENGmlvtdvvgkqLQRQLSASSSDSGDQSRH-- 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 673 nmfgfpagidgnvVQDQEEDDTTQPKTEPKKVSIFRIAALNKPEIPVLILGSISAAANGVILPIFGILISSV-------- 744
Cdd:TIGR00957 921 -------------HGSSAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVsalasnyw 987
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 745 IKAFFQPP--KKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIG 822
Cdd:TIGR00957 988 LSLWTDDPmvNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFER--TPSGNLV 1065
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 823 ARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACwQLAFVVLamlPLIALNGFLYMKFMKGFSADAKKMYGEASQ 902
Cdd:TIGR00957 1066 NRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLAT-PIAAVII---PPLGLLYFFVQRFYVASSRQLKRLESVSRS 1141
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 903 VA----NDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKnGIRQGIVS------GIGFGFSFFVLFssyAASFYVGARLVD 972
Cdd:TIGR00957 1142 PVyshfNETLLGVSVIRAFEEQERFIHQSDLKVDENQK-AYYPSIVAnrwlavRLECVGNCIVLF---AALFAVISRHSL 1217
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 973 DGKTTFDSV---FRVFFALT-MAAMAISQSSSLSPDSSKADVAAASIFAIMDRESKIDPSVESGRvldnvkGDIELRHVS 1048
Cdd:TIGR00957 1218 SAGLVGLSVsysLQVTFYLNwLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPR------GRVEFRNYC 1291
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1049 FKYpaRPDVQ-IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEP 1127
Cdd:TIGR00957 1292 LRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDP 1369
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1128 ILFNETIRANIayGKGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDE 1207
Cdd:TIGR00957 1370 VLFSGSLRMNL--DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1208 ATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKdGVYASLVQ 1279
Cdd:TIGR00957 1448 ATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
373-620 |
1.46e-66 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 236.71 E-value: 1.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 373 NGKVLDDIKGDIELKDVYFTYPArpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKE 452
Cdd:TIGR01192 324 DAPELPNVKGAVEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 453 FQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIA 532
Cdd:TIGR01192 402 VTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpE 612
Cdd:TIGR01192 482 IARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK-D 560
|
....*...
gi 15226477 613 GAYSQLIR 620
Cdd:TIGR01192 561 GRFYKLLR 568
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1040-1261 |
3.64e-66 |
|
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: 222.85 E-value: 3.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYPARPDVQIfQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQ 1119
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILFNETIRANIAYGkGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKD 1199
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1200 PKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
718-1252 |
1.52e-64 |
|
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: 229.10 E-value: 1.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 718 PVLILGSISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYpAQTFFFAIAGCKLVQRIRS 797
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGW-LQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 798 MCFEKVVHMEVGWfdepenssgtIGARLSADAATI--RGLvgDSLA------QTVQNLSSI--LAGLIIAFLACWQLAFV 867
Cdd:TIGR02857 82 RLLEAVAALGPRW----------LQGRPSGELATLalEGV--EALDgyfaryLPQLVLAVIvpLAILAAVFPQDWISGLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 868 VLAMLPLIALngflymkFM----KGFSADAKKMYGEASQVAN---DAVGSIRTVASFCAED-------KVMNMYSKKCeg 933
Cdd:TIGR02857 150 LLLTAPLIPI-------FMiligWAAQAAARKQWAALSRLSGhflDRLRGLPTLKLFGRAKaqaaairRSSEEYRERT-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 934 pMKNgIRQGIVSGigFGFSFFVLFSSYAASFYVGARLVDdGKTTFdsvFRVFFALTMAAMA---ISQSSSLSPDSSKADV 1010
Cdd:TIGR02857 221 -MRV-LRIAFLSS--AVLELFATLSVALVAVYIGFRLLA-GDLDL---ATGLFVLLLAPEFylpLRQLGAQYHARADGVA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1011 AAASIFAIMDRESKIDPSVESgrVLDNVKGDIELRHVSFKYPARPDVqiFQDLCLSIRAGKTVALVGESGSGKSTVIALL 1090
Cdd:TIGR02857 293 AAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1091 QRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQG 1170
Cdd:TIGR02857 369 LGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARP-DASDAEIREALERAGLDEFVAALPQG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1171 YDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIA 1250
Cdd:TIGR02857 448 LDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
|
..
gi 15226477 1251 VV 1252
Cdd:TIGR02857 528 VL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
382-603 |
3.47e-63 |
|
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: 214.28 E-value: 3.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYpaRPDEQ-IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFTASIKDNIAYGKEdATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 541 PRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGS 603
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
359-620 |
1.04e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 225.09 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 359 ETIERRPNIdSYSTNGKVLDDiKGDIELKDVYFTYPARPDeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDP 438
Cdd:PRK11160 316 EITEQKPEV-TFPTTSTAAAD-QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 439 QAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKlPQGLDTMVGE 518
Cdd:PRK11160 393 QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 519 HGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKI 598
Cdd:PRK11160 472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
250 260
....*....|....*....|..
gi 15226477 599 VEKGSHTELLKDpEGAYSQLIR 620
Cdd:PRK11160 552 IEQGTHQELLAQ-QGRYYQLKQ 572
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1040-1261 |
2.84e-62 |
|
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: 211.58 E-value: 2.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYpaRPDVQ-IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQ 1118
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNETIRANIA-YGKggdASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIV 1197
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpFGE---YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1198 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
384-593 |
1.08e-61 |
|
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: 220.62 E-value: 1.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:TIGR02857 322 LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVI 593
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
382-622 |
2.25e-61 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 223.68 E-value: 2.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYpaRPD-EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:TIGR03797 450 GAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFTASIKDNIAyGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:TIGR03797 528 QLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRK 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 541 PRILLLDEATSALDAESERVVQEALDRIMVNRttVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQLIR 620
Cdd:TIGR03797 607 PRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR-EGLFAQLAR 683
|
..
gi 15226477 621 LQ 622
Cdd:TIGR03797 684 RQ 685
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
406-624 |
5.48e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 220.10 E-value: 5.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYdPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKE 485
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 486 DATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEAL 565
Cdd:PRK11174 449 DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 566 DRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPeGAYSQLIRLQEE 624
Cdd:PRK11174 529 NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLAHRQE 586
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
107-634 |
1.67e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 218.43 E-value: 1.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 107 LKFVWLgIGTFAAAFlQLsgwmisgerqAARIRSLYLKTILRQDIAFFdIDTNTGEVVGRMSGDTVLIQDAMGEKVgkaI 186
Cdd:PRK10789 52 LRYVWR-VLLFGASY-QL----------AVELREDFYRQLSRQHPEFY-LRHRTGDLMARATNDVDRVVFAAGEGV---L 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 187 QLLATFVGGFVIAFVR----GWLLTLvmLSSIPLLVMAgallaIVIAKTASR-------GQTAYAKAATVVEQTIGSIRT 255
Cdd:PRK10789 116 TLVDSLVMGCAVLIVMstqiSWQLTL--LALLPMPVMA-----IMIKRYGDQlherfklAQAAFSSLNDRTQESLTSIRM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 256 VASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVwyggklildkgyTGGQVLniiiaVLTGSM 335
Cdd:PRK10789 189 IKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAI------------GGGSWM-----VVNGSL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 336 SLGQ-TS----------PCLSAFAagqaaaykMFETIER--------------RPNIDSYStngKVLDDIKGDIELKDVY 390
Cdd:PRK10789 252 TLGQlTSfvmylglmiwPMLALAW--------MFNIVERgsaaysriramlaeAPVVKDGS---EPVPEGRGELDVNIRQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 391 FTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPV 470
Cdd:PRK10789 321 FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 LFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEAT 550
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 551 SALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPeGAYSQLIRLQ--EEKKSD 628
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQqlEAALDD 558
|
....*.
gi 15226477 629 ENAAEE 634
Cdd:PRK10789 559 APEIRE 564
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
763-1282 |
4.81e-60 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 217.66 E-value: 4.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 763 AIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFD-EPensSGTIGARLSADAATIRGLVGDSLA 841
Cdd:PRK10790 68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDtQP---VGQLISRVTNDTEVIRDLYVTVVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 842 QTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKF-------MKGFSADAKKMYGEasqVAN--DAVGSIR 912
Cdd:PRK10790 145 TVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYstpivrrVRAYLADINDGFNE---VINgmSVIQQFR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 913 TVASFcaeDKVMN----------MYSKKCEG----PMKNGIRQGIVSG--IGFGFS------FFVLfssYAASFYVGaRL 970
Cdd:PRK10790 222 QQARF---GERMGeasrshymarMQTLRLDGfllrPLLSLFSALILCGllMLFGFSasgtieVGVL---YAFISYLG-RL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 971 VDD--GKTTFDSVFRvffaltmaamaisqssslspdssKADVAAASIFAIMDRESKidPSVESGRVLDNvkGDIELRHVS 1048
Cdd:PRK10790 295 NEPliELTTQQSMLQ-----------------------QAVVAGERVFELMDGPRQ--QYGNDDRPLQS--GRIDIDNVS 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1049 FKYpaRPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPI 1128
Cdd:PRK10790 348 FAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPV 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1129 LFNETIRANIAYGKggDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEA 1208
Cdd:PRK10790 426 VLADTFLANVTLGR--DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1209 TSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINiKDGVYASLVQLHL 1282
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA-AQGRYWQMYQLQL 576
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
817-1279 |
6.91e-59 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 216.36 E-value: 6.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 817 SSGTIGARLSAdAATIRGLVGDSLAQTVqnLSSILA--GLIIAFLACWQLAFVVLAMLPLIAL----NGFLYMKFMKGFS 890
Cdd:TIGR03797 231 STGDLASRAMG-ISQIRRILSGSTLTTL--LSGIFAllNLGLMFYYSWKLALVAVALALVAIAvtlvLGLLQVRKERRLL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 891 ADAKKMYGEASQVANdAVGSIRTVAsfcAEDKV----MNMYSKKCEGPMKNGIRQGIVSGIGFGFSFF---VLFssYAAS 963
Cdd:TIGR03797 308 ELSGKISGLTVQLIN-GISKLRVAG---AENRAfarwAKLFSRQRKLELSAQRIENLLTVFNAVLPVLtsaALF--AAAI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 964 FYVGARLVDDGK-TTFDSVFRVFF-ALTMAAMAIsqssslspdsskadVAAASIFAIMDRESKI---DPSVESGRVL-DN 1037
Cdd:TIGR03797 382 SLLGGAGLSLGSfLAFNTAFGSFSgAVTQLSNTL--------------ISILAVIPLWERAKPIleaLPEVDEAKTDpGK 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1038 VKGDIELRHVSFKYpaRPD-VQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWL 1116
Cdd:TIGR03797 448 LSGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1117 RQQTGLVSQEPILFNETIRANIAygkgGDASES--EIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIAR 1194
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSGSIFENIA----GGAPLTldEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIAR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRttIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINiKDGVY 1274
Cdd:TIGR03797 602 ALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REGLF 678
|
....*
gi 15226477 1275 ASLVQ 1279
Cdd:TIGR03797 679 AQLAR 683
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
384-1279 |
7.77e-59 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 223.46 E-value: 7.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIdginlkefqlkwIRSKIG 463
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIAYGKE-DATTEEikAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 543 ILLLDEATSALDAESER-VVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEgAYSQLIR- 620
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRqVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP-LFQKLMEn 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 621 --LQEEKKSDENAAEEQKMSS--IESFKQSSLRKSSLGRSLSKGGSSrgnssrhsfnmfgfpagidgnVVQDQEEDDTtq 696
Cdd:PLN03130 840 agKMEEYVEENGEEEDDQTSSkpVANGNANNLKKDSSSKKKSKEGKS---------------------VLIKQEERET-- 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 697 pktepkKVSIFRIAALNKPEipvliLGSISAAAngvILPIFGILI------SSVIKAFFQPPKKLKEDTS-FWAIIFMVL 769
Cdd:PLN03130 897 ------GVVSWKVLERYKNA-----LGGAWVVM---ILFLCYVLTevfrvsSSTWLSEWTDQGTPKTHGPlFYNLIYALL 962
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 770 GFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDS----LAQTVQ 845
Cdd:PLN03130 963 SFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHT--NPLGRIINRFAKDLGDIDRNVAVFvnmfLGQIFQ 1040
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 846 NLSS-ILAGlIIAFLACWqlafvvlAMLPLIALNGFLYMKFmKGFSADAKKM-----------YGEAsqvandaVGSIRT 913
Cdd:PLN03130 1041 LLSTfVLIG-IVSTISLW-------AIMPLLVLFYGAYLYY-QSTAREVKRLdsitrspvyaqFGEA-------LNGLST 1104
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 914 VASFCAEDKVMNMYSKKcegpMKNGIRQGIVSgigfgfsffvlfssYAASFYVGARLVDDGKTT--FDSVFRVF------ 985
Cdd:PLN03130 1105 IRAYKAYDRMAEINGRS----MDNNIRFTLVN--------------MSSNRWLAIRLETLGGLMiwLTASFAVMqngrae 1166
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 986 ----FALTMAAM---AISQSSSLSPDSSKADVAAASIFAI------MDRESKIDPSVESGRVLDN--VKGDIELRHVSFK 1050
Cdd:PLN03130 1167 nqaaFASTMGLLlsyALNITSLLTAVLRLASLAENSLNAVervgtyIDLPSEAPLVIENNRPPPGwpSSGSIKFEDVVLR 1246
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1051 YpaRPDVQ-IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPIL 1129
Cdd:PLN03130 1247 Y--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL 1324
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1130 FNETIRANI-AYGKGGDASESEIVSSAELSNAhgfISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEA 1208
Cdd:PLN03130 1325 FSGTVRFNLdPFNEHNDADLWESLERAHLKDV---IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 1209 TSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKDGVYASLVQ 1279
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1011-1279 |
5.25e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 211.22 E-value: 5.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1011 AAASIFAIMDRESKIDPSVESGRVLDnvKGDIELRHVSFKYPARPDvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALL 1090
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1091 QRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRAN--IAYGKGGDASESEIVSSAELSNAhgfisgLQ 1168
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNllLAAPNASDEALIEVLQQVGLEKL------LE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1169 --QGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNA 1246
Cdd:PRK11160 461 ddKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF 540
|
250 260 270
....*....|....*....|....*....|...
gi 15226477 1247 DVIAVVKNGVIVEKGKHDTLINiKDGVYASLVQ 1279
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLA-QQGRYYQLKQ 572
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
63-342 |
1.45e-57 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 201.74 E-value: 1.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAF---GENQTNTT---------------DKVSKVALKFVWLGIGTFAAAFLQL 124
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtngGMTNITGNssglnssagpfekleEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 125 SGWMISGERQAARIRSLYLKTILRQDIAFFDIDTnTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGW 204
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVND-TGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 205 LLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEG 284
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 285 GSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSP 342
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVP 297
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
382-622 |
2.48e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 209.57 E-value: 2.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTASIKDNIAYGKeDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQLIRL 621
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMYQL 574
|
.
gi 15226477 622 Q 622
Cdd:PRK10790 575 Q 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1011-1268 |
2.15e-56 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 206.10 E-value: 2.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1011 AAASIFAIMDRES----KI------DPSVESG-RVLDNVKGDIELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGES 1079
Cdd:PRK10789 272 ALAWMFNIVERGSaaysRIramlaeAPVVKDGsEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPT 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1080 GSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSN 1159
Cdd:PRK10789 351 GSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRP-DATQQEIEHVARLAS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1160 AHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHR 1239
Cdd:PRK10789 430 VHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHR 509
|
250 260
....*....|....*....|....*....
gi 15226477 1240 LSTIKNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK10789 510 LSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
720-1015 |
5.69e-56 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 197.11 E-value: 5.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 720 LILGSISAAANGVILPIFGILISSVIKAFFQ------------------PPKKLKEDTSFWAIIFMVLGFASIIAYPAQT 781
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNggmtnitgnssglnssagPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 782 FFFAIAGCKLVQRIRSMCFEKVVHMEVGWFdePENSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLAC 861
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 862 WQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQ 941
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 942 GIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSVFRVFFALTMAAMAISQSSSLSPDSSKADVAAASI 1015
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
384-1279 |
1.60e-55 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 212.53 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVS--LIERfydPQAGDVLIDginlkefqlkwIRSK 461
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISamLGEL---SHAETSSVV-----------IRGS 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTASIKDNIAYGkEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:PLN03232 681 VAYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 542 RILLLDEATSALDAE-SERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpegaySQLIr 620
Cdd:PLN03232 760 DIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-----GSLF- 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 621 lqeeKKSDENAAeeqKMSSIESFKQSSLRKSSLGRSLSKGGSSRGNSSRHSfnmfgfpaGIDG-NVVQDQEEDDTTqpkt 699
Cdd:PLN03232 834 ----KKLMENAG---KMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQ--------GKRGrSVLVKQEERETG---- 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 700 epkkvsifrIAALNkpeipVLILGSISAAANGVILPIFGI-LISSVIK-------AFFQPPKKLKE-DTSFWAIIFMVLG 770
Cdd:PLN03232 895 ---------IISWN-----VLMRYNKAVGGLWVVMILLVCyLTTEVLRvssstwlSIWTDQSTPKSySPGFYIVVYALLG 960
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 771 FASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDS----LAQTVQN 846
Cdd:PLN03232 961 FGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIGDIDRNVANLmnmfMNQLWQL 1038
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 847 LSSILAGLIIAFLACWqlafvvlAMLPLIALNGFLYMkFMKGFSADAKKM-----------YGEASqvanDAVGSIRtva 915
Cdd:PLN03232 1039 LSTFALIGTVSTISLW-------AIMPLLILFYAAYL-YYQSTSREVRRLdsvtrspiyaqFGEAL----NGLSSIR--- 1103
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 916 SFCAEDKVMNMYSKKcegpMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGAR--LVDDGKTTFDSVFRVFFALTMAaM 993
Cdd:PLN03232 1104 AYKAYDRMAKINGKS----MDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATfaVLRNGNAENQAGFASTMGLLLS-Y 1178
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 994 AISQSSSLSPDSSKADVAAASIFAIMDRESKIDPSVESGRVLDN--------VKGDIELRHVSFKY-PARPDVqiFQDLC 1064
Cdd:PLN03232 1179 TLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENnrpvsgwpSRGSIKFEDVHLRYrPGLPPV--LHGLS 1256
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANI-AYGKG 1143
Cdd:PLN03232 1257 FFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEH 1336
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1144 GDASESEIVSSAELSNAhgfISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDA 1223
Cdd:PLN03232 1337 NDADLWEALERAHIKDV---IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1224 LDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKDGVYASLVQ 1279
Cdd:PLN03232 1414 IREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
720-993 |
3.95e-55 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 193.24 E-value: 3.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 720 LILGSISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMC 799
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 800 FEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNG 879
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 880 FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSS 959
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 15226477 960 YAASFYVGARLVDDGKTTFDS--VFRVFFALTMAAM 993
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
60-619 |
5.54e-55 |
|
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: 204.97 E-value: 5.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSignglgfplmtLLFGDLIDAFGENQTNTTDKVSKVALKFVWL--GIGTFAAAFLQlsgwMISGERQAAR 137
Cdd:TIGR01193 166 IIVTLISIAGS-----------YYLQKIIDTYIPHKMMGTLGIISIGLIIAYIiqQILSYIQIFLL----NVLGQRLSID 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 138 IRSLYLKTILRQDIAFFDIdTNTGEVVGRMSgDTVLIQDAMGEKVGKAIQLLATFVG-GFVIAFvRGWLLTLVMLSSIPL 216
Cdd:TIGR01193 231 IILSYIKHLFELPMSFFST-RRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIvGLFLVR-QNMLLFLLSLLSIPV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 217 LvmagALLAIVIAKTASRGQTAYAKAATVVEQTI----GSIRTVASFTGEKQA-------ISNYNKHLVTAYKAGVIEGG 285
Cdd:TIGR01193 308 Y----AVIIILFKRTFNKLNHDAMQANAVLNSSIiedlNGIETIKSLTSEAERyskidseFGDYLNKSFKYQKADQGQQA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 286 STGLGLGTLFLVVfcsyalaVWYGGKLILDKGYTGGQVL--NIIIAVLTGSM-SLGQTSPCLSAFAAGQAAAYKMF--ET 360
Cdd:TIGR01193 384 IKAVTKLILNVVI-------LWTGAYLVMRGKLTLGQLItfNALLSYFLTPLeNIINLQPKLQAARVANNRLNEVYlvDS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 361 IERRPNIDSYSTNgkvlddIKGDIELKDVYFTYPArpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA 440
Cdd:TIGR01193 457 EFINKKKRTELNN------LNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 441 GDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYG-KEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEH 519
Cdd:TIGR01193 529 GEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEE 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 520 GTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRiMVNRTTVVVAHRLSTVRNADMIAVIHQGKIV 599
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
570 580
....*....|....*....|
gi 15226477 600 EKGSHTELLKDpEGAYSQLI 619
Cdd:TIGR01193 688 EQGSHDELLDR-NGFYASLI 706
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1011-1277 |
2.15e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 200.84 E-value: 2.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1011 AAASIFAIMDREskiDPSVESGRVLDNVKGDIELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALL 1090
Cdd:PRK11174 320 AAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1091 QRFYdPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGgDASESEIVSSAELSNAHGFISGLQQG 1170
Cdd:PRK11174 397 LGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP-DASDEQLQQALENAWVSEFLPLLPQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1171 YDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIA 1250
Cdd:PRK11174 475 LDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIW 554
|
250 260
....*....|....*....|....*..
gi 15226477 1251 VVKNGVIVEKGKHDTLINiKDGVYASL 1277
Cdd:PRK11174 555 VMQDGQIVQQGDYAELSQ-AGGLFATL 580
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
63-335 |
2.63e-53 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 188.24 E-value: 2.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLY 142
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 143 LKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGA 222
Cdd:pfam00664 81 FKKILRQPMSFFD-TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 223 LLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSY 302
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 15226477 303 ALAVWYGGKLILDKGYTGGQ--VLNIIIAVLTGSM 335
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
393-1279 |
9.87e-53 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 203.47 E-value: 9.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 393 YPARPDEqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVlidginlkefqlkWIRSKIGLVSQEPVLF 472
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 473 TASIKDNIAYGKEDAtteeikaAAELANASKF------VDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLL 546
Cdd:PTZ00243 734 NATVRGNILFFDEED-------AARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 547 DEATSALDAE-SERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDP--EGAYSQLIRLQE 623
Cdd:PTZ00243 807 DDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSlyATLAAELKENKD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 624 EKKSDENAaEEQKMSSIESFKQSSLRKSSLGRSLSKGGSSRGnssrhsfnmfgFPAgIDGNVVQDQEEDDTTQP-KTepk 702
Cdd:PTZ00243 887 SKEGDADA-EVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAA-----------LDA-AAGRLMTREEKASGSVPwST--- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 703 KVSIFRIAAlnkpeipvlilgsiSAAANGVILPIFG----ILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYP 778
Cdd:PTZ00243 951 YVAYLRFCG--------------GLHAAGFVLATFAvtelVTVSSGVWLSMWSTRSFKLSAATYLYVYLGIVLLGTFSVP 1016
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 779 AQTFFFAIA---GCKLVQRIrsmCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLI 855
Cdd:PTZ00243 1017 LRFFLSYEAmrrGSRNMHRD---LLRSVSRGTMSFFDT--TPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSIL 1091
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 856 IAFLAcwqLAFVVLAMLPLialnGFLYMKFMKGFSADAKKMYGEASqVANDAVGSI--------RTVASFCAEDKVMN-- 925
Cdd:PTZ00243 1092 VTSAS---QPFVLVALVPC----GYLYYRLMQFYNSANREIRRIKS-VAKSPVFTLleealqgsATITAYGKAHLVMQea 1163
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 926 ------MYSKkceGPMKNGIRQGIvsGIGFGFSFFVLFSSYAASFYVGARLVddgkTTFDSVFRVFFALTMAAMAISQSS 999
Cdd:PTZ00243 1164 lrrldvVYSC---SYLENVANRWL--GVRVEFLSNIVVTVIALIGVIGTMLR----ATSQEIGLVSLSLTMAMQTTATLN 1234
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1000 SLSPDSSKADVAAASIFAIM------DRES--KIDPSV-----ESGRVLDnVKGDIELRHVSFKYPARPDVQ----IFQD 1062
Cdd:PTZ00243 1235 WLVRQVATVEADMNSVERLLyytdevPHEDmpELDEEVdalerRTGMAAD-VTGTVVIEPASPTSAAPHPVQagslVFEG 1313
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1063 LCLSIRAG---------------KTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEP 1127
Cdd:PTZ00243 1314 VQMRYREGlplvlrgvsfriaprEKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP 1393
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1128 ILFNETIRANIayGKGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVK-DPKVLLLD 1206
Cdd:PTZ00243 1394 VLFDGTVRQNV--DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMD 1471
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1207 EATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKDGVYASLVQ 1279
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVE 1544
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
381-609 |
7.93e-52 |
|
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: 192.66 E-value: 7.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 381 KGDIELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKefqlKWIRS 460
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 K----IGLVSQEPVLFTASIKDNIAyGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARA 536
Cdd:COG4618 403 ElgrhIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
384-612 |
2.28e-50 |
|
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: 177.91 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPV--LFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
95-581 |
3.91e-50 |
|
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: 186.80 E-value: 3.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 95 QTNTTDKVSKVALKFVWLGigtFAAAFLQLSGWMIS----------------GERQAARIRSL--YLKTILRQDIAF--- 153
Cdd:TIGR02868 9 KPRRRRLALAVLLGALALG---SAVALLGVSAWLISraaemppvlylsvaavAVRAFGIGRAVfrYLERLVGHDAALrsl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 154 -------FDIDT----------NTGEVVGRMSGDTvliqDAMGEKVGKAIQ--LLATFVGGFVIAFVrGWLLT---LVML 211
Cdd:TIGR02868 86 galrvrvYERLArqalagrrrlRRGDLLGRLGADV----DALQDLYVRVIVpaGVALVVGAAAVAAI-AVLSVpaaLILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 212 SSIPLLVMAGALLAIVIAKTA----SRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGViegGST 287
Cdd:TIGR02868 161 AGLLLAGFVAPLVSLRAARAAeqalARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAA---AAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 288 GLGLGTLFLVVFCSYALAVWYGGKlildkGYTGGQVLNIIIAV-----LTGSMSLGQTSPCLSAFAAGQAAAYKMFETIE 362
Cdd:TIGR02868 238 ALGAALTLLAAGLAVLGALWAGGP-----AVADGRLAPVTLAVlvllpLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 363 -RRPNIDSYSTNGKVLDDIKGDIELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAG 441
Cdd:TIGR02868 313 aAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 442 DVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGT 521
Cdd:TIGR02868 391 EVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGA 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 522 QLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRL 581
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
819-1278 |
6.30e-50 |
|
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: 189.95 E-value: 6.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 819 GTIGARLSaDAATIRGLVGDSLAQTVQNLSSILA-GLIIAFLACwQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKkmy 897
Cdd:TIGR01193 253 GEIVSRFT-DASSIIDALASTILSLFLDMWILVIvGLFLVRQNM-LLFLLSLLSIPVYAVIIILFKRTFNKLNHDAM--- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 898 gEASQVANDA----VGSIRTVASFCAED----KVMNMYSKKCEGPMKN----GIRQGIVSGIGFGFSFFVLfssyaasfY 965
Cdd:TIGR01193 328 -QANAVLNSSiiedLNGIETIKSLTSEAerysKIDSEFGDYLNKSFKYqkadQGQQAIKAVTKLILNVVIL--------W 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 966 VGARLVDDGKTTFDSVFRVFFALTMAAMAISQSSSLSPDSSKADVAAASIFAIMDRESKIDPSVESGRvLDNVKGDIELR 1045
Cdd:TIGR01193 399 TGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTE-LNNLNGDIVIN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1046 HVSFKYPArpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQ 1125
Cdd:TIGR01193 478 DVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1126 EPILFNETIRANIAYGKGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLL 1205
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1206 DEATSALDAESERVVQDALDRvMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINiKDGVYASLV 1278
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD-RNGFYASLI 706
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1039-1281 |
1.12e-48 |
|
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: 183.03 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1039 KGDIELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQ 1118
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNETIRANIAygKGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVK 1198
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIA--RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKhdtliniKDGVYASL 1277
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP-------RDEVLARL 557
|
....
gi 15226477 1278 VQLH 1281
Cdd:COG4618 558 ARPA 561
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
980-1240 |
2.16e-47 |
|
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: 178.71 E-value: 2.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 980 SVFRVFFALTMAAMAISQSSSlspdsskadvAAASIFAIMDRESKI-DPSVESGRVLDNVKGDIELRHVSFKYPARPDVq 1058
Cdd:TIGR02868 282 AAFEAFAALPAAAQQLTRVRA----------AAERIVEVLDAAGPVaEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPV- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1059 iFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANI 1138
Cdd:TIGR02868 351 -LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1139 AYGKGgDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESER 1218
Cdd:TIGR02868 430 RLARP-DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
250 260
....*....|....*....|..
gi 15226477 1219 VVQDALDRVMVNRTTIVVAHRL 1240
Cdd:TIGR02868 509 ELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1042-1266 |
1.64e-46 |
|
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: 166.59 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYD-----PDSGEITLDGVEIKSLRLK-- 1114
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WLRQQTGLVSQEPILFNETIRANIAYG-----KGGDASESEIVSSAeLSNAhgfisglqqGYDTMVGER--GIQLSGGQK 1187
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgIKLKEELDERVEEA-LRKA---------ALWDEVKDRlhALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1188 QRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTL 1266
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1042-1261 |
3.18e-46 |
|
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: 164.02 E-value: 3.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRlKWLRQQTG 1121
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNETIRANIaygkggdaseseivssaelsnahgfisglqqgydtmvgerGIQLSGGQKQRVAIARAIVKDPK 1201
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
381-609 |
3.92e-46 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 175.23 E-value: 3.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 381 KGDIELKDVYFTyPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:TIGR01842 314 EGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 541 PRILLLDEATSALDAESERVVQEALDRIMVNR-TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
384-617 |
5.76e-46 |
|
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: 173.94 E-value: 5.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE--QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWI 458
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 459 RSKIGLVSQEPV--LFTA-SIKDNIAYG---KEDATTEEIKA-AAELANA----SKFVDKLPQgldtmvgehgtQLSGGQ 527
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAERRErVAELLERvglpPDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 528 KQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSH 604
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
250
....*....|...
gi 15226477 605 TELLKDPEGAYSQ 617
Cdd:COG1123 490 EEVFANPQHPYTR 502
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1042-1238 |
5.80e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.60 E-value: 5.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNETIRANIAYG---KGGDASESEIvssaelsnahgfISGLQQ-GYDTMVGERGI-QLSGGQKQRVAIARAI 1196
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPfqlRERKFDRERA------------LELLERlGLPPDILDKPVeRLSGGERQRLALIRAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15226477 1197 VKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAH 1238
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
384-603 |
2.22e-45 |
|
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: 163.51 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYD-----PQAGDVLIDG--INLKEFQLK 456
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 457 WIRSKIGLVSQEPVLFTASIKDNIAYG-------KEDATTEEIKAAAELANASKFV-DKLpqgldtmvgeHGTQLSGGQK 528
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVkDRL----------HALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 529 QRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS 603
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGP 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1042-1262 |
2.47e-45 |
|
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: 163.27 E-value: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPI--LFNETIRANIAYG---KGGDASE-SEIVSSAeLSnAHGfISGLQqgydtmvgERGI-QLSGGQKQRVAIAR 1194
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenLGLPREEiRERVEEA-LE-LVG-LEHLA--------DRPPhELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KNADVIAVVKNGVIVEKGK 1262
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGT 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
384-598 |
3.60e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 162.29 E-value: 3.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIA----YGKEDATTEEIKAAAELANaskfvdkLPQG-LDTMVGEhgtqLSGGQKQRIAVARAIL 538
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLG-------LPPDiLDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAH--RLSTvRNADMIAVIHQGKI 598
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpEQIE-RVADRVLTLEAGRL 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
384-602 |
1.98e-44 |
|
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: 159.02 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQlKWIRSKIG 463
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIaygkedatteeikaaaelanaskfvdklpqgldtmvgehGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 602
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
385-597 |
2.26e-44 |
|
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: 159.94 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGL 464
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 VSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARA 536
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGK 597
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
384-612 |
2.51e-44 |
|
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: 160.82 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIR 459
Cdd:cd03258 2 IELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 460 SKIGLVSQEPVLFTA-SIKDNIAYGKEDATTE--EIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIA 532
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPkaEIEERVlellELVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
....*
gi 15226477 608 LKDPE 612
Cdd:cd03258 229 FANPQ 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1042-1257 |
6.95e-44 |
|
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: 156.99 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYP--ARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQ 1119
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILFNETIRANIaygkggdaseseivssaelsnahgfisglqqgydtmvgergiqLSGGQKQRVAIARAIVKD 1199
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1200 PKVLLLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLSTIKNADVIAVVKNGVI 1257
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
384-598 |
7.51e-44 |
|
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: 156.99 E-value: 7.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 544 LLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTVRNADMIAVIHQGKI 598
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1042-1261 |
2.53e-43 |
|
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: 166.23 E-value: 2.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARP--DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL---RLKWL 1116
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1117 RQQTGLVSQEPIL-FNE--TIRANIA-----YGKGGDASESEIVssAELsnahgfisgLQQ-GYDTMVGERGI-QLSGGQ 1186
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAeplrlHGLLSRAERRERV--AEL---------LERvGLPPDLADRYPhELSGGQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1187 KQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1043-1255 |
2.55e-43 |
|
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: 156.86 E-value: 2.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGL 1122
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1123 VSQEP--ILFNETIRANIAYG-KGGDASESEIVSSAELSNAHGFISGLQqgydtmvgERGI-QLSGGQKQRVAIARAIVK 1198
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGlENLGLPEEEIEERVEEALELVGLEGLR--------DRSPfTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTIKN-ADVIAVVKNG 1255
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1035-1267 |
5.59e-43 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 165.98 E-value: 5.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1035 LDNVKGDIELRHVSFKyPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLK 1114
Cdd:TIGR01842 310 LPEPEGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WLRQQTGLVSQEPILFNETIRANIAygKGGDASESE-IVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIA 1193
Cdd:TIGR01842 389 TFGKHIGYLPQDVELFPGTVAENIA--RFGENADPEkIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1194 RAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR-TTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLI 1267
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1042-1259 |
6.29e-43 |
|
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: 157.27 E-value: 6.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARP-DVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRfydPDSGEITLDGVEIKSLRLKWLR 1117
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 QQTGLVSQEPIL-FN--ETIRANIA---YGKGGDASESEIVSSAELsnahgfiSGLQQGYdtmVGERGIQLSGGQKQRVA 1191
Cdd:COG1124 79 RRVQMVFQDPYAsLHprHTVDRILAeplRIHGLPDREERIAELLEQ-------VGLPPSF---LDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAeserVVQ----DALDRVMVNR--TTIVVAHRLSTIKN-ADVIAVVKNGVIVE 1259
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVE 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
382-603 |
7.86e-43 |
|
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: 155.26 E-value: 7.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYpaRPD-EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:cd03369 5 GEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFTASIKDNI-AYGKEDatTEEIKAAAElanaskfvdklpqgldtmVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 540 DPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGS 603
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
384-617 |
9.80e-43 |
|
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: 156.50 E-value: 9.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEQ-IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKI 462
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEPvlfTAS------IKDNIA-----YGKEDATTEEIKAAAELANASKFVDKLPqgldtmvgeHgtQLSGGQKQRI 531
Cdd:COG1124 82 QMVFQDP---YASlhprhtVDRILAeplriHGLPDREERIAELLEQVGLPPSFLDRYP---------H--QLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 532 AVARAILKDPRILLLDEATSALDAeserVVQ----EALDRIMVNR--TTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSH 604
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTV 223
|
250
....*....|...
gi 15226477 605 TELLKDPEGAYSQ 617
Cdd:COG1124 224 ADLLAGPKHPYTR 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1041-1261 |
3.20e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.72 E-value: 3.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1041 DIELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL----Rlkwl 1116
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppekR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1117 rqQTGLVSQEPILF-NETIRANIAYG-KGGDASESEI---VSSA-ELSNahgfISGLqqgydtmvGERGI-QLSGGQKQR 1189
Cdd:COG3842 78 --NVGMVFQDYALFpHLTVAENVAFGlRMRGVPKAEIrarVAELlELVG----LEGL--------ADRYPhQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLS---TIknADVIAVVKNGVIVEKG 1261
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1042-1255 |
4.50e-42 |
|
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: 151.96 E-value: 4.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR--LKWLRQQ 1119
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILF-NETIRANIAYGkggdaseseivssaelsnahgfisglqqgydtmvgergiqLSGGQKQRVAIARAIVK 1198
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLS-TIKNADVIAVVKNG 1255
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
384-602 |
5.14e-42 |
|
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: 153.82 E-value: 5.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQLKWIR 459
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 460 SKIGLVSQEPvlFTA-----SIKDNIA-----YGKEDATTEEIKAAAELA----NASKFVDKLPQgldtmvgehgtQLSG 525
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAeplriHGKLSKKEARKEAVLLLLvgvgLPEEVLNRYPH-----------ELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
79-338 |
7.58e-42 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 155.87 E-value: 7.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 79 LMTLLFGDLIDAFgENQTNTTDKVSKVALK---FVWLGIGTFAAAFLQLSGWM--ISGERQAARIRSLYLKTILRQDIAF 153
Cdd:cd18780 14 ALPYFFGQVIDAV-TNHSGSGGEEALRALNqavLILLGVVLIGSIATFLRSWLftLAGERVVARLRKRLFSAIIAQEIAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 154 FDIdTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTAS 233
Cdd:cd18780 93 FDV-TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 234 RGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLI 313
Cdd:cd18780 172 KFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLV 251
|
250 260
....*....|....*....|....*
gi 15226477 314 LDKGYTGGQVLNIIIAVLTGSMSLG 338
Cdd:cd18780 252 IDGELTTGLLTSFLLYTLTVAMSFA 276
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1042-1259 |
9.35e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.89 E-value: 9.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPA-RPDVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRfydPDSGEITLDGVEIKSL----RL 1113
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1114 KWLRQQTGLVSQEPILFNE-TIRANIAYG---KGGDASES-----EIVSSAELSN-AHGFISglqqgydtmvgergiQLS 1183
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALPlllAGVSRKERrerarELLERVGLGDrLDHRPS---------------QLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1184 GGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKNADVIAVVKNGVIVE 1259
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
60-345 |
1.03e-41 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 155.03 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIgnglgfpLMTLLFGDLIDAFGENQTntTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIR 139
Cdd:cd18557 2 LLFLLISSAAQL-------LLPYLIGRLIDTIIKGGD--LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 140 SLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVM 219
Cdd:cd18557 73 RDLFSSLLRQEIAFFD-KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 220 AGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVF 299
Cdd:cd18557 152 ASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15226477 300 CSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLS 345
Cdd:cd18557 232 LSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLA 277
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1042-1261 |
1.93e-41 |
|
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: 151.52 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwlRQQTG 1121
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILF-NETIRANIAYG-KGGDASESEIVSSAELSNAHGFISGLQQGYDTmvgergiQLSGGQKQRVAIARAIVKD 1199
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPH-------ELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1200 PKVLLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLS-TIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1040-1261 |
1.96e-41 |
|
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: 151.41 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYpaRPDV-QIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQ 1118
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNETIRANI-AYGKggdASESEIVSSAELSnahgfisglqqgydtmvgERGIQLSGGQKQRVAIARAIV 1197
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDE---YSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1198 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1042-1261 |
2.40e-41 |
|
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: 151.89 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPD-VQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL---RLKWLR 1117
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 QQTGLVSQEPIL-FN--ETIRANIA-----YGKGGDASESEIVSSAELSnahgfisGLQQGyDTMVGERGIQLSGGQKQR 1189
Cdd:cd03257 82 KEIQMVFQDPMSsLNprMTIGEQIAeplriHGKLSKKEARKEAVLLLLV-------GVGLP-EEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1042-1262 |
2.88e-41 |
|
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: 151.96 E-value: 2.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARP-DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLR 1117
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 QQTGLVSQEPILFN-ETIRANIAYG-KGGDASESEIVSSA-ELSNAHGfISGLQQGYDTmvgergiQLSGGQKQRVAIAR 1194
Cdd:cd03258 82 RRIGMIFQHFNLLSsRTVFENVALPlEIAGVPKAEIEERVlELLELVG-LEDKADAYPA-------QLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR----TTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGK 1262
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRD--INRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
384-609 |
3.16e-41 |
|
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: 151.89 E-value: 3.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRS 460
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFTA-SIKDNIAYGKEDATT---EEIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIA 532
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRlseEEIREIVleklEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1060-1210 |
3.45e-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: 148.56 E-value: 3.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1060 FQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNE-TIRANI 1138
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1139 AYGkGGDASESEIVSSAELSNAHGFIsGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1210
Cdd:pfam00005 81 RLG-LLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1042-1261 |
3.94e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 154.85 E-value: 3.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARP-DVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRfydPDSGEITLDGVEIKSL---RLK 1114
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALserELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WLRQQTGLVSQEPILFNE-TIRANIAY-----GKggdaSESEI---VssAELsnahgfisgLQqgydtMVG--ERG---- 1179
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALpleiaGV----PKAEIrkrV--AEL---------LE-----LVGlsDKAdayp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1180 IQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNRT---TIVVA-HRLSTIKN-ADVIAVVKN 1254
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD--INRElglTIVLItHEMDVVRRiCDRVAVLEN 216
|
....*..
gi 15226477 1255 GVIVEKG 1261
Cdd:COG1135 217 GRIVEQG 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
384-609 |
4.62e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.37 E-value: 4.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTA-SIKDNI-----AYGKEDATTEEikAAAELAnasKFVDkLPQGLDTMVGehgtQLSGGQKQRIAVARAI 537
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARE--RIDELL---ELFG-LTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
384-602 |
1.41e-40 |
|
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: 149.21 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLkeFQLKWIRSKIG 463
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARA 536
Cdd:cd03259 76 MVFQDYALFPhLTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKG 602
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
384-612 |
2.09e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 150.66 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKW-IRSKI 462
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEP--VLFTASIKDNIAYGKEDA--TTEEIKA----AAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVA 534
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLgvPREEMRKrvdeALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
384-611 |
2.40e-40 |
|
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: 149.76 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFT-ASIKDNIA-------YGKedattEEIKA-AAELAnasKFVDKLPQGLdtmVGEHGTQLSGGQKQRIAVA 534
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIAlvpkllkWPK-----EKIRErADELL---ALVGLDPAEF---ADRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 535 RAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
112-620 |
2.85e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 163.22 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 112 LGIGTFAAAFLQlSGWMISGERQAA-RIRSLYLKTILRQDIAFFDidTN-TGEVVGRMSGDTVLIQ----DAMGEKVGKA 185
Cdd:PLN03232 959 LGFGQVAVTFTN-SFWLISSSLHAAkRLHDAMLNSILRAPMLFFH--TNpTGRVINRFSKDIGDIDrnvaNLMNMFMNQL 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 186 IQLLATFVggfviafVRGWLLTLVMLSSIPLLVMAGAllAIVIAKTASRG---------QTAYAKAATVVeQTIGSIRTV 256
Cdd:PLN03232 1036 WQLLSTFA-------LIGTVSTISLWAIMPLLILFYA--AYLYYQSTSREvrrldsvtrSPIYAQFGEAL-NGLSSIRAY 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 257 ASF-----TGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVfcSYAlavwyggklILDKGYTGGQVLNIIIAVL 331
Cdd:PLN03232 1106 KAYdrmakINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTA--TFA---------VLRNGNAENQAGFASTMGL 1174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 332 TGSMSLGQTSpCLSAFAAGQAAAYKMFETIERRPN-IDSYSTNGKVLDD--------IKGDIELKDVYFTY-PARPdeQI 401
Cdd:PLN03232 1175 LLSYTLNITT-LLSGVLRQASKAENSLNSVERVGNyIDLPSEATAIIENnrpvsgwpSRGSIKFEDVHLRYrPGLP--PV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIA 481
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 482 YGKE--DATTEEikaAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 559
Cdd:PLN03232 1332 PFSEhnDADLWE---ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 560 VVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLIR 620
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
384-612 |
4.11e-40 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 152.15 E-value: 4.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI---ERfydPQAGDVLIDGIN---LKEFQLK 456
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDltaLSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 457 WIRSKIGLVSQEPVLFTA-SIKDNIAYGKEDA--TTEEIKA-AAELAnasKFVdklpqGLDTMVGEHGTQLSGGQKQRIA 532
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALPLEIAgvPKAEIRKrVAELL---ELV-----GLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDV 228
|
....*
gi 15226477 608 LKDPE 612
Cdd:COG1135 229 FANPQ 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1042-1268 |
4.52e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.67 E-value: 4.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWlRQQTG 1121
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANI-----AYGKGGDASESEIVSSAELSnahgfisGLQQGYDTMVGergiQLSGGQKQRVAIARA 1195
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELF-------GLTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1196 IVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1042-1255 |
9.42e-40 |
|
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: 146.46 E-value: 9.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQ--IFQDLCLSIRAGKTVALVGESGSGKSTVI-ALLQRFyDPDSGEITLDGveikslrlkwlrq 1118
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLsALLGEL-EKLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNETIRANIAYGKGGDASE-SEIVSSAELSNAhgfISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIV 1197
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEERyEKVIKACALEPD---LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1198 KDPKVLLLDEATSALDAES-----ERVVQDALdrvMVNRTTIVVAHRLSTIKNADVIAVVKNG 1255
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
384-612 |
9.66e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.83 E-value: 9.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL--KEFQLKWIRSK 461
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFT-ASIKDNIAYG--------KEDAtteEIKAAAELanaskfvDKLpqGLDTMVGEHGTQLSGGQKQRIA 532
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEA---EERAMELL-------ERV--GLADKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAEserVVQEALDrIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTE 606
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEE 222
|
....*.
gi 15226477 607 LLKDPE 612
Cdd:COG1126 223 FFENPQ 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1042-1257 |
1.16e-39 |
|
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: 146.87 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPD-VQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRfydPDSGEITLDGVEIKSL----RL 1113
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLsekeLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1114 KWLRQQTGLVSQEPILFNE-TIRANIAYG---KGGDASESEIVSSAELSNAhgfisGLQQGYDTMVGergiQLSGGQKQR 1189
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDlTALENVELPlllAGVPKKERRERAEELLERV-----GLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKNADVIAVVKNGVI 1257
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
384-609 |
1.17e-39 |
|
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: 147.43 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRS 460
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFTA-SIKDNIAYG-KE--DATTEEIKAAAELanaskfvdKLpqgldTMVGEHGT------QLSGGQKQR 530
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREhtDLSEAEIRELVLE--------KL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 531 IAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 15226477 608 LK 609
Cdd:COG1127 230 LA 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1042-1268 |
1.19e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.45 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI--KSLRLKWLRQQ 1119
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILF-NETIRANIAYG----KGGDASESEIVSSAELsnahgfisglqqgydTMVG--ERG----IQLSGGQKQ 1188
Cdd:COG1126 79 VGMVFQQFNLFpHLTVLENVTLApikvKKMSKAEAEERAMELL---------------ERVGlaDKAdaypAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1189 RVAIARAIVKDPKVLLLDEATSALDAEserVVQDALDrVMVN-----RTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGK 1262
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
....*.
gi 15226477 1263 HDTLIN 1268
Cdd:COG1126 220 PEEFFE 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
384-600 |
1.72e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.34 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKST---VVSLIERfydPQAGDVLIDGIN---LKEFQL- 455
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDissLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 456 KWIRSKIGLVSQEPVLF-TASIKDNIA----YGKEDATtEEIKAAAELANA---SKFVDKLPqgldtmvgehgTQLSGGQ 527
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLpELTALENVAlpllLAGVSRK-ERRERARELLERvglGDRLDHRP-----------SQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 528 KQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRNADMIAVIHQGKIVE 600
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1042-1271 |
2.65e-39 |
|
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: 146.11 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL---RLKWLRQ 1118
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNE-TIRANIAYG--KGGDASESEIVSSAELsnahgfisGLQqgydtMVGERGI------QLSGGQKQR 1189
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTRLSEEEIREIVLE--------KLE-----AVGLRGAedlypaELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGKHDTL 1266
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
....*
gi 15226477 1267 INIKD 1271
Cdd:cd03261 225 RASDD 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1042-1271 |
2.68e-39 |
|
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: 146.28 E-value: 2.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLRQ 1118
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNE-TIRANIAYG--KGGDASESEIVSSAELSnahgfisgLQqgydtMVGERGI------QLSGGQKQR 1189
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlrEHTDLSEAEIRELVLEK--------LE-----LVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAESERVV-------QDALdrvmvNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
250
....*....|
gi 15226477 1262 KHDTLINIKD 1271
Cdd:COG1127 225 TPEELLASDD 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
384-597 |
4.63e-39 |
|
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: 144.53 E-value: 4.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEQ--IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIerfydpqagdvlidginLKEFQLK----W 457
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-----------------LGELEKLsgsvS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 458 IRSKIGLVSQEPVLFTASIKDNIAYGKE-DattEE-----IKAAAELANaskfVDKLPQGLDTMVGEHGTQLSGGQKQRI 531
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENILFGKPfD---EEryekvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 532 AVARAILKDPRILLLDEATSALDAES-----ERVVQEALdriMVNRTTVVVAHRLSTVRNADMIAVIHQGK 597
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1042-1261 |
6.67e-39 |
|
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: 145.39 E-value: 6.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWlRQQTG 1121
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILF-NETIRANI-----AYGKGGDASESEIVSSAELSnahgfisGLQQGYDTMVGErgiqLSGGQKQRVAIARA 1195
Cdd:COG4555 78 VLPDERGLYdRLTVRENIryfaeLYGLFDEELKKRIEELIELL-------GLEEFLDRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1196 IVKDPKVLLLDEATSALDAESERVVQDALDRVM-VNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1042-1238 |
8.78e-39 |
|
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: 144.15 E-value: 8.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYP-ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRlkwlrQQT 1120
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFN-ETIRANIAYG---KGGDASESEivssaelSNAHGFISglqqgydtMVGERGI------QLSGGQKQRV 1190
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQGVPKAEAR-------ERAEELLE--------LVGLSGFenayphQLSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMV-NRTTIV-VAH 1238
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTH 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1042-1274 |
1.12e-38 |
|
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: 145.19 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPIL-FNETIRANIAYG----KGGDASES----EIVSSA-ELSNAHGFIsglqqgydtmvgERGI-QLSGGQKQRV 1190
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphLGLFGRPSaedrEAVEEAlERTGLEHLA------------DRPVdELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALD----AESERVVQD-ALDRvmvNRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKGKHD 1264
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRlARER---GRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPE 223
|
250
....*....|...
gi 15226477 1265 TLI---NIKDgVY 1274
Cdd:COG1120 224 EVLtpeLLEE-VY 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
384-613 |
2.21e-38 |
|
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: 151.59 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA---GDVLIDGINLKEFQLKWIRS 460
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEP--VLFTASIKDNIAYGKE--DATTEEIKAAAElaNASKFVdklpqGLDTMVGEHGTQLSGGQKQRIAVARA 536
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVL--ELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEG 613
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
384-597 |
2.39e-38 |
|
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: 141.56 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL--KEFQLKWIRSK 461
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFT-ASIKDNIAYGkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKD 540
Cdd:cd03229 78 IGMVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 541 PRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGK 597
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
384-612 |
3.95e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.36 E-value: 3.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEP--VLFTASIKDNIAYGKEDA--TTEEIKA----AAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvPPKKMKDiiddLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA--HRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
402-551 |
4.56e-38 |
|
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: 139.71 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLF-TASIKDNI 480
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 481 AYGKEDATTEEIKAAAELANASKFVDkLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATS 551
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
384-600 |
4.61e-38 |
|
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: 142.23 E-value: 4.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlkwIRSKI 462
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVV-VAHRLS-TVRNADMIAVIHQ--GKIVE 600
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1042-1261 |
9.04e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.67 E-value: 9.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRfydPDSGEITLDGVEIKSlRLKWLRQ 1118
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDLFT-NLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILF-NETIRANIAYG-KGGDASESEIVSSAE--LSNAHgfISGLQQGYDTmvgergiQLSGGQKQRVAIAR 1194
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFGlRVRPPSKAEIRARVEelLELVQ--LEGLADRYPS-------QLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1195 AIVKDPKVLLLDEATSALDA----ESERVVQDALDRvmVNRTTIVVAH------RLstiknADVIAVVKNGVIVEKG 1261
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
382-620 |
1.05e-37 |
|
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: 142.36 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYPA--RPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIR 459
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 460 SKIGLVSQEPVLFTASIKDNIAYGKEdATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 540 DPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLI 619
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
.
gi 15226477 620 R 620
Cdd:cd03288 254 R 254
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1043-1255 |
1.12e-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: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGL 1122
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1123 VSQepilfnetiraniaygkggdaseseivssaelsnahgfisglqqgydtmvgergiqLSGGQKQRVAIARAIVKDPKV 1202
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1203 LLLDEATSALDAESERVVQDALDRVMV-NRTTIVVAHRLSTIKNA-DVIAVVKNG 1255
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
725-977 |
1.12e-37 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 143.47 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 725 ISAAANGVILPIFGILISSVIKaffqppKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVV 804
Cdd:cd18557 7 ISSAAQLLLPYLIGRLIDTIIK------GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 805 HMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMK 884
Cdd:cd18557 81 RQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 885 FMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASF 964
Cdd:cd18557 159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVL 238
|
250
....*....|...
gi 15226477 965 YVGARLVDDGKTT 977
Cdd:cd18557 239 WYGGYLVLSGQLT 251
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
725-977 |
3.20e-37 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 142.39 E-value: 3.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 725 ISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVV 804
Cdd:cd18780 7 VSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 805 HMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMK 884
Cdd:cd18780 87 AQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 885 FMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASF 964
Cdd:cd18780 165 YVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVL 244
|
250
....*....|...
gi 15226477 965 YVGARLVDDGKTT 977
Cdd:cd18780 245 WYGGRLVIDGELT 257
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1042-1257 |
3.79e-37 |
|
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: 137.91 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwLRQQTG 1121
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILfnetiraniaygkggdaseseivssaelsnahgfisglqqgYDTMVGERGIQLSGGQKQRVAIARAIVKDPK 1201
Cdd:cd03230 77 YLPEEPSL-----------------------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTIKN-ADVIAVVKNGVI 1257
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1042-1268 |
8.97e-37 |
|
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: 146.59 E-value: 8.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPD---SGEITLDGVEIKSLRLKWLRQ 1118
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPI--LFNETIRANIAYG-KGGDASESEIVSSAelsnahgfISGLQQ-GYDTMVGERGIQLSGGQKQRVAIAR 1194
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEAlENLGLSRAEARARV--------LELLEAvGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1042-1238 |
9.36e-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: 139.84 E-value: 9.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARP-DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRlkwlrQQT 1120
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFN-ETIRANIAYG-KGGDASESEIVSSAE--LSnahgfisglqqgydtMVGERGI------QLSGGQKQRV 1190
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlELRGVPKAERRERARelLE---------------LVGLAGFedayphQLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTIV-VAH 1238
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTH 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
382-641 |
1.03e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 151.81 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYpaRPD-EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFTASIKDNIAYGKE--DATTEEikaAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEhnDADLWE---SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQL 618
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
250 260 270
....*....|....*....|....*....|....*
gi 15226477 619 IR------------LQEEKKSDENAAEEQKMSSIE 641
Cdd:PLN03130 1471 VQstgaanaqylrsLVFGGDEDRLAREESKALDGQ 1505
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1067-1281 |
1.35e-36 |
|
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: 139.27 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1067 IRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANI-AYGKGGD 1145
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLdPECKCTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1146 ASESEIVSSAELSNahgFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALD 1225
Cdd:cd03288 124 DRLWEALEIAQLKN---MVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1226 RVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKDGVYASLVQLH 1281
Cdd:cd03288 201 TAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1042-1258 |
1.62e-36 |
|
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: 138.47 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQ--- 1118
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNE-TIRANIAYGKGGD----ASESEIVSSAELSNAhgfISGLQQ-GYDTMVGERGIQLSGGQKQRVAI 1192
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGRLGRrstwRSLFGLFPKEEKQRA---LAALERvGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1193 ARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIK-NADVIAVVKNGVIV 1258
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
384-608 |
2.07e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 138.64 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVL-FTASIKDNIAYG------------KEDAttEEIKAAAELANASKFVDKLpqgldtmVgehgTQLSGGQKQR 530
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgrpsAEDR--EAVEEALERTGLEHLADRP-------V----DELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 531 IAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 15226477 608 L 608
Cdd:COG1120 226 L 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
383-611 |
2.51e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.39 E-value: 2.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 383 DIELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQlkwiR 459
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvTGLPPEK----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 460 sKIGLVSQEPVLF---TasIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQR 530
Cdd:COG3842 78 -NVGMVFQDYALFphlT--VAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYP-----------HQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 531 IAVARAILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHT 605
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPE 221
|
....*.
gi 15226477 606 ELLKDP 611
Cdd:COG3842 222 EIYERP 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1042-1258 |
2.81e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 137.88 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLRQ 1118
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNE-TIRANIAYGKGGD----ASESEIVSSAELSNAHGFIS--GLQQGYDTMVGergiQLSGGQKQRVA 1191
Cdd:COG3638 81 RIGMIFQQFNLVPRlSVLTNVLAGRLGRtstwRSLLGLFPPEDRERALEALErvGLADKAYQRAD----QLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR----TTIVVAHRLSTIKN-ADVIAVVKNGVIV 1258
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRR--IARedgiTVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
385-597 |
3.79e-36 |
|
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: 134.29 E-value: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGL 464
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 VSQepvlftasikdniaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRIL 544
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 545 LLDEATSALDAESERVVQEALDRIMV-NRTTVVVAHRLSTVRNA-DMIAVIHQGK 597
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1042-1262 |
4.02e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.72 E-value: 4.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLK---WLRQ 1118
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQE-PILFNETIRANIAY-----GKggdaSESEI---VSSAeLSNAhgfisGLQQGYDTMVgergIQLSGGQKQR 1189
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGK----SRKEIrrrVREV-LDLV-----GLSDKAKALP----HELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAE-SERVVqDALDRvmVNR--TTIVVA-HRLSTIKNAD--VIaVVKNGVIVEKGK 1262
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEE--INRrgTTVLIAtHDLELVDRMPkrVL-ELEDGRLVRDEA 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
384-609 |
4.89e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.22 E-value: 4.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEP--VLFTASIKDNIAYGKE------DATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLEnigvprEEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 536 AILKDPRILLLDEATSALDAESErvvQEALD--RIMVNRTTVVV---AHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
384-598 |
1.03e-35 |
|
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: 135.31 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF----QLKWI 458
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 459 RSKIGLVSQEPVL---FTAsiKDNIAYGKEDATTEEIKAAAELANASKFVDkLPQGLDTMVGehgtQLSGGQKQRIAVAR 535
Cdd:cd03255 81 RRHIGFVFQSFNLlpdLTA--LENVELPLLLAGVPKKERRERAEELLERVG-LGDRLNHYPS----ELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRNADMIAVIHQGKI 598
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
384-612 |
1.04e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 139.51 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI---ERfydPQAGDVLIDG----INL--KEfq 454
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGrdlfTNLppRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 455 lkwiRsKIGLVSQEPVLF-TASIKDNIAYG--KEDATTEEIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQ 527
Cdd:COG1118 75 ----R-RVGFVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRARVeellELVQLEGLADRYP-----------SQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 528 KQRIAVARAILKDPRILLLDEATSALDA----ESERVVQEALDRImvNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKG 602
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|
gi 15226477 603 SHTELLKDPE 612
Cdd:COG1118 217 TPDEVYDRPA 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-1240 |
1.12e-35 |
|
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: 148.13 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwirsKIGLVSQEPVLFTASIKDNI 480
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 481 AYG---KEDATTEEIKAAAELANASKFvdklPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 557
Cdd:TIGR01271 508 IFGlsyDEYRYTSVIKACQLEEDIALF----PEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 558 ERVVQEA-LDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLIRLQEekkSDENAAEEQK 636
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEA---FDNFSAERRN 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 637 MSSIESFKQSSL------------RKSSLGRSLSKGGSSRGNS-------SRHSFNMFGF-PAGIDGNvvqdQEEDDTTQ 696
Cdd:TIGR01271 661 SILTETLRRVSIdgdstvfsgpetIKQSFKQPPPEFAEKRKQSiilnpiaSARKFSFVQMgPQKAQAT----TIEDAVRE 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 697 PKTepKKVSIFRIAALNKPEIP------------------VLILGSISAAANGVILPifgiLISSVIKAFFQPP------ 752
Cdd:TIGR01271 737 PSE--RKFSLVPEDEQGEESLPrgnqyhhglqhqaqrrqsVLQLMTHSNRGENRREQ----LQTSFRKKSSITQqnelas 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 753 ------KKLKEDTSF------------------------------------------WAIIFMVLGFA------------ 772
Cdd:TIGR01271 811 eldiysRRLSKDSVYeiseeineedlkecfaderenvfetttwntylryittnrnlvFVLIFCLVIFLaevaasllglwl 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 773 -------------------------SIIAYPAQTFFF---------------AIAGCKLVQRIrsMCFEKVVH--MEVGW 810
Cdd:TIGR01271 891 itdnpsapnyvdqqhanasspdvqkPVIITPTSAYYIfyiyvgtadsvlalgFFRGLPLVHTL--LTVSKRLHeqMLHSV 968
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 811 FDEPENS-----SGTIGARLSADAATIRGLVGDSLAQTVQnLSSILAGlIIAFLACWQlAFVVLAMLPLIALNGFLYMKF 885
Cdd:TIGR01271 969 LQAPMAVlntmkAGRILNRFTKDMAIIDDMLPLTLFDFIQ-LTLIVLG-AIFVVSVLQ-PYIFIAAIPVAVIFIMLRAYF 1045
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 886 MKGfSADAKKMYGEA-SQVANDAVGSIR---TVASFCAEDKVMNMYSKKCEGPMKN-----------GIRQGIVsgigfg 950
Cdd:TIGR01271 1046 LRT-SQQLKQLESEArSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwflylstlrwfQMRIDII------ 1118
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 951 fsfFVLFSSYAASFYVGARLVDDGkttfdsvfRVFFALTMAAMAISQSSSLSPDSSKADVAAASIfaimDRESK-IDPSV 1029
Cdd:TIGR01271 1119 ---FVFFFIAVTFIAIGTNQDGEG--------EVGIILTLAMNILSTLQWAVNSSIDVDGLMRSV----SRVFKfIDLPQ 1183
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1030 ESGRVLDNVKGD-------IELRHVSFKYPA--RPDVQ------------IFQDLCLSIRAGKTVALVGESGSGKSTVIA 1088
Cdd:TIGR01271 1184 EEPRPSGGGGKYqlstvlvIENPHAQKCWPSggQMDVQgltakyteagraVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1089 LLQRFYDPDsGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANI-AYGKggdASESEIVSSAELSNAHGFISGL 1167
Cdd:TIGR01271 1264 ALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQ---WSDEEIWKVAEEVGLKSVIEQF 1339
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1168 QQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRL 1240
Cdd:TIGR01271 1340 PDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1042-1268 |
1.34e-35 |
|
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: 135.89 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPA-RPDVQifqDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQT 1120
Cdd:cd03295 1 IEFENVTKRYGGgKKAVN---NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILF-NETIRANIA-------YGKGG-DASESEIVSSAELSNAHgfisgLQQGYDTmvgergiQLSGGQKQRVA 1191
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIAlvpkllkWPKEKiRERADELLALVGLDPAE-----FADRYPH-------ELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRL-STIKNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
384-579 |
1.65e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.37 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlkwIRSKI 462
Cdd:COG1116 8 LELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVV-VAH 579
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTH 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1042-1266 |
2.10e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.22 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLK--WLRQQ 1119
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILFNETIRANIaYGKGG-----DASESEIVSSA-ELSNAHGFIsglqqgyDTMVGErgiqLSGGQKQRVAIA 1193
Cdd:COG1121 84 AEVDWDFPITVRDVVLMGR-YGRRGlfrrpSRADREAVDEAlERVGLEDLA-------DRPIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1194 RAIVKDPKVLLLDEATSALDAESERVVQDALDR-VMVNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGKHDTL 1266
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLVAHGPPEEVL 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
384-612 |
2.27e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.55 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYD--PQA---GDVLIDGINL--KEFQLK 456
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 457 WIRSKIGLVSQEPVLFTASIKDNIAYG------KEDATTEEI-----KAAA---ELAnaskfvDKLpqgldtmvGEHGTQ 522
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIveeslRKAAlwdEVK------DRL--------KKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 523 LSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEK 601
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEF 234
|
250
....*....|.
gi 15226477 602 GSHTELLKDPE 612
Cdd:COG1117 235 GPTEQIFTNPK 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
384-609 |
2.52e-35 |
|
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: 134.99 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLF-TASIKDNIAY------GKEDATTEEIKAAAELANASKFVDKLpqgldtmVGEhgtqLSGGQKQRIAVARA 536
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRYfaelygLFDEELKKRIEELIELLGLEEFLDRR-------VGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
384-598 |
5.09e-35 |
|
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: 133.04 E-value: 5.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLKWIRSK 461
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFT-ASIKDNIAYG-----KEDatteeiKAAAElANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVAR 535
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLApikvkGMS------KAEAE-ERALELLEKV--GLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 536 AILKDPRILLLDEATSALDAEserVVQEALDrIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKI 598
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1043-1261 |
1.77e-34 |
|
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: 130.25 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGL 1122
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1123 VSQepilfnetiraniaygkggdaseseivsSAELSNAHGFIsglqqgydtmvgERGI-QLSGGQKQRVAIARAIVKDPK 1201
Cdd:cd03214 78 VPQ----------------------------ALELLGLAHLA------------DRPFnELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
385-602 |
1.81e-34 |
|
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: 130.25 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGL 464
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 VSQepvlftasikdniaygkedatteeikaAAELANASKFVDKlpqgldtmvgeHGTQLSGGQKQRIAVARAILKDPRIL 544
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADR-----------PFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 545 LLDEATSALDAES-----ERVVQEALDRimvNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKG 602
Cdd:cd03214 120 LLDEPTSHLDIAHqiellELLRRLARER---GKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
384-611 |
1.99e-34 |
|
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: 134.80 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA---GDVLIDGINLKEF---QLK 456
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 457 WIRSK-IGLVSQEPvlFTA-----SIKDNIAYG---KEDATTEEIKAAAE-------LANASKFVDKLPqgldtmvgeHg 520
Cdd:COG0444 82 KIRGReIQMIFQDP--MTSlnpvmTVGDQIAEPlriHGGLSKAEARERAIellervgLPDPERRLDRYP---------H- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 521 tQLSGGQKQRIAVARAILKDPRILLLDEATSALDAeserVVQ----EALDRIMVNR-TTVV-VAHRLSTVRN-ADMIAVI 593
Cdd:COG0444 150 -ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaqilNLLKDLQRELgLAILfITHDLGVVAEiADRVAVM 224
|
250
....*....|....*...
gi 15226477 594 HQGKIVEKGSHTELLKDP 611
Cdd:COG0444 225 YAGRIVEEGPVEELFENP 242
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
384-606 |
2.38e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRS 460
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQE-PVLFTASIKDNIAY-----GKEDATTEE-IKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAV 533
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 534 ARAILKDPRILLLDEATSALDAE-SERVVqEALDRImvNR--TTVVVA-HRLSTVRNADM-IAVIHQGKIVEKGSHTE 606
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEI--NRrgTTVLIAtHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
384-598 |
4.16e-34 |
|
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: 129.05 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwIRSKIG 463
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLF-TASIKDNIaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtQLSGGQKQRIAVARAILKDPR 542
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 543 ILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKI 598
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
719-995 |
4.18e-34 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 133.06 E-value: 4.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 719 VLILGSISAAANGVILPIFGILISSVIkaffqpPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSM 798
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVI------PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 799 CFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALN 878
Cdd:cd07346 78 LFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 879 GFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFS 958
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 15226477 959 SYAASFYVGARLVDDGKTTFDSVFRVFFALTMAAMAI 995
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPI 272
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
406-615 |
5.74e-34 |
|
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: 132.00 E-value: 5.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQLKWIRSK-IGLVSQEPVLFT-ASIKDNI 480
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSRKELRELRRKkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 481 AYGKE----DATTEEIKA--AAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 554
Cdd:cd03294 124 AFGLEvqgvPRAEREERAaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 555 AESERVVQEALDRI--MVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1042-1257 |
6.79e-34 |
|
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: 129.96 E-value: 6.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKW--LRQQ 1119
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILF-NETIRANIAYG----KGGDASESEIVSSAEL------SNAHGFISglqqgydtmvgergiQLSGGQKQ 1188
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLApikvKGMSKAEAEERALELLekvglaDKADAYPA---------------QLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1189 RVAIARAIVKDPKVLLLDEATSALDAEserVVQDALDrVMVN-----RTTIVVAHRLSTIKN-ADVIAVVKNGVI 1257
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
384-611 |
6.88e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 134.16 E-value: 6.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIR 459
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 460 SKIGLVSQEPVLFTA-SIKDNIAYGKEDATT--EEIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIA 532
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLELAGTpkAEIKARVtellELVGLSDKADRYP-----------AQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
....
gi 15226477 608 LKDP 611
Cdd:PRK11153 229 FSHP 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
384-612 |
7.43e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.78 E-value: 7.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGShTELLKDPE 612
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1061-1268 |
3.71e-33 |
|
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: 129.69 E-value: 3.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQ----QTGLVSQEPILF-NETIR 1135
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1136 ANIAYG---KGGDASESEIVSSAELSNAhgfisGLQQGYDTMVGErgiqLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1212
Cdd:cd03294 121 ENVAFGlevQGVPRAEREERAAEALELV-----GLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1213 DAESERVVQDALDRV--MVNRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:cd03294 192 DPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
384-598 |
5.50e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.28 E-value: 5.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlkwIRSKIG 463
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVL---FTASIKDNIA------------YGKEDAttEEIKAAAELANASKFVDKLpqgldtmVGEhgtqLSGGQK 528
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLmgrygrrglfrrPSRADR--EAVDEALERVGLEDLADRP-------IGE----LSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 529 QRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTVR-NADMIAVIHQGKI 598
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVReYFDRVLLLNRGLV 217
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
720-974 |
8.42e-33 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 129.56 E-value: 8.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 720 LILGSISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFwAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMC 799
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTF-ALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 800 FEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNG 879
Cdd:cd18573 81 FKSILRQDAAFFDK--NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 880 FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSS 959
Cdd:cd18573 159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
|
250
....*....|....*
gi 15226477 960 YAASFYVGARLVDDG 974
Cdd:cd18573 239 LLSVLYYGGSLVASG 253
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1042-1261 |
1.03e-32 |
|
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: 127.35 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIksLRLKWLRQQTG 1121
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANIAYG---KGGDASE-----SEIVSSAELSN-AHGFISglqqgydtmvgergiQLSGGQKQRVA 1191
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlKKLPKAEikervAEALDLVQLEGyANRKPS---------------QLSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1040-1258 |
1.66e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.19 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLqrfYDPDSGEITLDGVEIKSLRLKwl 1116
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGL---EDPTSGEILIGGRDVTDLPPK-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1117 RQQTGLVSQEPILF-NETIRANIAYG-KGGDASESEI---VSSAelsnAHgfISGLQQGYDTMVGergiQLSGGQKQRVA 1191
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIAFPlKLRKVPKAEIdrrVREA----AE--LLGLEDLLDRKPK----QLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAESeRV--------VQDALdrvmvNRTTIVVAHRLS---TIknADVIAVVKNGVIV 1258
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQ 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1042-1266 |
2.19e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.08 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYD--PD---SGEITLDGVEI--KSLRLK 1114
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WLRQQTGLVSQEPILFNETIRANIAYG--KGGDASES---EIVSSAelsnahgfisgLQQgydtmVG----------ERG 1179
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrLHGIKSKSeldEIVEES-----------LRK-----AAlwdevkdrlkKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1180 IQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAH------RLStiknaDVIAVVK 1253
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFY 227
|
250
....*....|...
gi 15226477 1254 NGVIVEKGKHDTL 1266
Cdd:COG1117 228 LGELVEFGPTEQI 240
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1042-1262 |
3.81e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 125.87 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLRQ 1118
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQE-PILFNETIRANIAYG----KGGDASESEIVSSAELSNAhgfISGLQQ-GYDTMVGERGIQLSGGQKQRVAI 1192
Cdd:TIGR02315 80 RIGMIFQHyNLIERLTVLENVLHGrlgyKPTWRSLLGRFSEEDKERA---LSALERvGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1193 ARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGK 1262
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKyADRIVGLKAGEIVFDGA 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
403-611 |
4.21e-32 |
|
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: 125.53 E-value: 4.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqLKWIRSKIGLVSQEPVLFT-ASIKDNIA 481
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFPhMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 482 YGKEDATTEEIKAAAELANASKFVdklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVV 561
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15226477 562 QEALDRIM-VNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:cd03299 169 REELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1042-1261 |
4.91e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.77 E-value: 4.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYP-ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLR 1117
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 QQTGLVSQEpilFN----ETIRANIAY-----GKggdaSESEIVSS-AELSNAHGfISGLQQGYDTmvgergiQLSGGQK 1187
Cdd:PRK11153 82 RQIGMIFQH---FNllssRTVFDNVALplelaGT----PKAEIKARvTELLELVG-LSDKADRYPA-------QLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1188 QRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNRT---TIV-VAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKD--INRElglTIVlITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1042-1251 |
8.50e-32 |
|
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: 123.74 E-value: 8.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRfydPDSGEITLDGVEIKSLRLKWlRQ 1118
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllrILAGLLP---PSAGEVLWNGEPIRDAREDY-RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNE-TIRANIAY---GKGGDASESEIVSSAELSnahgfisGLQQGYDTMVGergiQLSGGQKQRVAIAR 1194
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFwaaLYGLRADREAIDEALEAV-------GLAGLADLPVR----QLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTIKNADVIAV 1251
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
404-617 |
1.01e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.16 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRSKIGLVSQEPvlfTAS----- 475
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDP---YASlnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 -IKDNIAYG---KEDATTEEIKA-AAELanaskfvdklpqgLDtMVG---EHGT----QLSGGQKQRIAVARAILKDPRI 543
Cdd:COG4608 113 tVGDIIAEPlriHGLASKAERRErVAEL-------------LE-LVGlrpEHADryphEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 544 LLLDEATSALD----AEserVV------QEALdrimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:COG4608 179 IVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARPL 250
|
....*
gi 15226477 613 GAYSQ 617
Cdd:COG4608 251 HPYTQ 255
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
384-608 |
1.07e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.10 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpdEQIFRgFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKefQLKWIRSKIG 463
Cdd:COG3840 2 LRLDDLTYRYG----DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTA-SIKDNIAYGKEDA---TTEE---IKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARA 536
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGLRPGlklTAEQraqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 537 ILKDPRILLLDEATSALD----AESERVVQEALDRimVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELL 608
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1271 |
1.09e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.49 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEP--ILFNETIRANIAYG---KGGDASE--SEIVSSAELSNAHGFISGLQQgydtmvgergiQLSGGQKQRVAIAR 1194
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGlenKKVPPKKmkDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKD 1271
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
384-607 |
2.11e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.84 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEP--VLFTASIKDNIAYGKE------DATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVAR 535
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLEnkgiphEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 536 AILKDPRILLLDEATSALDAESE----RVVQEALDRimVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
384-612 |
2.13e-31 |
|
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: 123.50 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKefQLKWIRSKIG 463
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARA 536
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEEP 222
|
.
gi 15226477 612 E 612
Cdd:cd03300 223 A 223
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
64-336 |
2.83e-31 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 124.90 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 64 ILGTLGSIGNGLGFPLmtlLFGDLIDAFgeNQTNTTDKVSKVALkfVWLGIGTFAAAFLQLSGWMIS--GERQAARIRSL 141
Cdd:cd18576 2 LILLLLSSAIGLVFPL---LAGQLIDAA--LGGGDTASLNQIAL--LLLGLFLLQAVFSFFRIYLFArvGERVVADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 142 YLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAG 221
Cdd:cd18576 75 LYRHLQRLPLSFFH-ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 222 ALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCS 301
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 15226477 302 YALAVWYGGKLILDKGYTGGQVLNIII--AVLTGSMS 336
Cdd:cd18576 234 IVAVLWYGGRLVLAGELTAGDLVAFLLytLFIAGSIG 270
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
382-611 |
3.03e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.34 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSK 461
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLF-TASIKDNIAYG----KEDAttEEIKA----AAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIA 532
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPK--AEIDRrvreAAELLGLEDLLDRKP-----------KQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESeRV--------VQEALdrimvNRTTVVVAH------RLstvrnADMIAVIHQGKI 598
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRI 212
|
250
....*....|...
gi 15226477 599 VEKGSHTELLKDP 611
Cdd:COG3839 213 QQVGTPEELYDRP 225
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
725-975 |
3.13e-31 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 124.58 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 725 ISAAANgVILPIF-GILISSVIKAffqppkklKEDTSFW-AIIFMV-LGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFE 801
Cdd:cd18572 7 VAALSE-LAIPHYtGAVIDAVVAD--------GSREAFYrAVLLLLlLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 802 KVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFL 881
Cdd:cd18572 78 SLLRQDIAFFDA--TKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 882 YMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYA 961
Cdd:cd18572 156 YGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQV 235
|
250
....*....|....
gi 15226477 962 ASFYVGARLVDDGK 975
Cdd:cd18572 236 LVLFYGGHLVLSGR 249
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
403-615 |
4.16e-31 |
|
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: 122.83 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIGLVSQEPVLFT-ASIKDNIA 481
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 482 YGKEDATTEEIKAAAELANASKFVDKLPQgLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDA----ES 557
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRAKVHELLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 558 ERVVQEALDRIMVnrTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:cd03296 176 RRWLRRLHDELHV--TTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1062-1262 |
4.36e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.39 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1062 DLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI--KSLRLKWLRQQTGLVSQEP--ILFNETIRAN 1137
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1138 IAYG-KGGDASESEIVSSAELSNAhgfISGLQqgYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES 1216
Cdd:PRK13637 105 IAFGpINLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1217 ErvvQDALDRVM-----VNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGK 1262
Cdd:PRK13637 180 R---DEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1042-1262 |
4.38e-31 |
|
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: 121.75 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLRQ 1118
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQE-PILFNETIRANIAY-----GKGGDASESEIVSSAELSnahgfisGLQQGYDTMVGErgiqLSGGQKQRVAI 1192
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFalevtGVPPREIRKRVPAALELV-------GLSHKHRALPAE----LSGGEQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1193 ARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HrlstikNADVIAVVKNGVIV-EKGK 1262
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtH------AKELVDTTRHRVIAlERGK 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
384-602 |
7.31e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 121.21 E-value: 7.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIG 463
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARA 536
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKG 602
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1042-1262 |
7.84e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 122.92 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKW-LRQQT 1120
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEP--ILFNETIRANIAYG---KGGDASE-SEIVSSAelsnahgfisgLQQgydtmVG-----ERG-IQLSGGQKQ 1188
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGlenLGVPREEmRKRVDEA-----------LKL-----VGmedfrDREpHLLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1189 RVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGK 1262
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
384-623 |
8.82e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 8.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLK--EFQLKWIRSK 461
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLF---TASikDNIAYGKEDaTTEEIKAAAElANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PRK09493 79 AGMVFQQFYLFphlTAL--ENVMFGPLR-VRGASKEEAE-KQARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 539 KDPRILLLDEATSALDAESE----RVVQEALDRIMvnrTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEg 613
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGM---TMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPP- 228
|
250
....*....|
gi 15226477 614 aySQliRLQE 623
Cdd:PRK09493 229 --SQ--RLQE 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
384-607 |
1.50e-30 |
|
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: 121.14 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPArpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGI---NLKEFQLKWIRS 460
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFT-ASIKDNIAYGKEDATT-----------EEIKAAAELanaskfVDKLpqGLDTMVGEHGTQLSGGQK 528
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRRStwrslfglfpkEEKQRALAA------LERV--GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 529 QRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVR-NADMIAVIHQGKIVEKGSHT 605
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 15226477 606 EL 607
Cdd:cd03256 231 EL 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1042-1268 |
2.09e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLK--WLRQQ 1119
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILFNE-TIRANIAYG----KGGDASESEIVSSAELSNAhgfisGLQQGYDTMVGErgiqLSGGQKQRVAIAR 1194
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGplrvRGASKEEAEKQARELLAKV-----GLAERAHHYPSE----LSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESE----RVVQDALDRVMvnrTTIVVAHRLS-TIKNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGM---TMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
385-578 |
2.35e-30 |
|
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: 119.67 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARPDeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLkwiRSKIGL 464
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 VSQEP--VLFTASIKDNIAYGKEDAtteeikaAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKEL-------DAGNEQAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 15226477 543 ILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA 578
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI 182
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1043-1257 |
3.85e-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: 119.18 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLK--WLRQQT 1120
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFNETIRANIAYGKGG----DASESEIVSSAelsnahgfisgLQqgydtMVG-----ERGI-QLSGGQKQRV 1190
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLYGHKGLfrrlSKADKAKVDEA-----------LE-----RVGlselaDRQIgELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLSTI-KNADVIAVVKNGVI 1257
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1046-1268 |
5.31e-30 |
|
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: 122.08 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1046 HVSFKYPARPdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDP---DSGEITLDGVEIKSL---RLKWLR-Q 1118
Cdd:COG0444 8 KVYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLsekELRKIRgR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPIL-FN----------ETIRANiaygkgGDASESEIVSSA-ELsnahgfisgLQqgydtMVG----ERGI-- 1180
Cdd:COG0444 87 EIQMIFQDPMTsLNpvmtvgdqiaEPLRIH------GGLSKAEARERAiEL---------LE-----RVGlpdpERRLdr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1181 ---QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAeserVVQ----DALDRVMVNR-TTIV-VAHRLSTIKN-ADVIA 1250
Cdd:COG0444 147 yphELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaqilNLLKDLQRELgLAILfITHDLGVVAEiADRVA 222
|
250
....*....|....*...
gi 15226477 1251 VVKNGVIVEKGKHDTLIN 1268
Cdd:COG0444 223 VMYAGRIVEEGPVEELFE 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1062-1262 |
6.07e-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: 119.36 E-value: 6.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1062 DLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLrlKWLRQQTGLVSQEPILF-NETIRANIAY 1140
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1141 G-KGGDASESEIvsSAELSNAHGFIsglqqGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERV 1219
Cdd:cd03299 95 GlKKRKVDKKEI--ERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15226477 1220 VQDALDRVM--VNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGK 1262
Cdd:cd03299 168 LREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1042-1261 |
6.16e-30 |
|
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: 119.37 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwlRQQTG 1121
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANIAYG-----KGGDASESEIvsSAELSNAHGFI--SGLQQGYDTmvgergiQLSGGQKQRVAIA 1193
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlrvkpRSERPPEAEI--RAKVHELLKLVqlDWLADRYPA-------QLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 1194 RAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
384-578 |
7.01e-30 |
|
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: 118.28 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGI---NLKEFQLKWIRS 460
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQE-PVLFTASIKDNIAYGKE--DATTEEI----KAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAV 533
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEvtGVPPREIrkrvPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226477 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA 578
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1042-1269 |
7.12e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.09 E-value: 7.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpdVQIFQ-DLclSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRlkwlrqqt 1120
Cdd:COG3840 2 LRLDDLTYRYG----DFPLRfDL--TIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 glVSQEP--ILFNE-------TIRANIAYG-----KGGDASESEIVSSAElsnahgfisglQQGYDTMVGERGIQLSGGQ 1186
Cdd:COG3840 68 --PAERPvsMLFQEnnlfphlTVAQNIGLGlrpglKLTAEQRAQVEQALE-----------RVGLAGLLDRLPGQLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1187 KQRVAIARAIVKDPKVLLLDEATSALD----AESERVVQDALDRvmVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADG 212
|
....*...
gi 15226477 1262 KHDTLINI 1269
Cdd:COG3840 213 PTAALLDG 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
384-612 |
1.04e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.29 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGD---VLIDGINLKEFQLKWIRS 460
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEP--VLFTASIKDNIAYGKED---ATTEEIKAAAELAN---ASKFVDKLPQgldtmvgehgtQLSGGQKQRIA 532
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENravPRPEMIKIVRDVLAdvgMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMV--NRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
..
gi 15226477 611 PE 612
Cdd:PRK13640 234 VE 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1065-1266 |
1.52e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLRQQTGLVSQEPilF---N--ETIRA 1136
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YaslNprMTVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1137 NIA-----YGKGGDASESEIVssAELsnahgfisgLQqgydtMVGERG-------IQLSGGQKQRVAIARAIVKDPKVLL 1204
Cdd:COG4608 117 IIAeplriHGLASKAERRERV--AEL---------LE-----LVGLRPehadrypHEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1205 LDEATSALD----AEserVV------QDALdrvmvNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTL 1266
Cdd:COG4608 181 CDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1042-1261 |
1.95e-29 |
|
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: 116.97 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwlRQQTG 1121
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILF-NETIRANIAYG-KGGDASESEIV----SSAELSNahgfISGLQQGYDTmvgergiQLSGGQKQRVAIARA 1195
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlKLRKVPKDEIDervrEVAELLQ----IEHLLDRKPK-------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1196 IVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAH-RLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
384-649 |
3.09e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.55 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYP-ARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF-QLKWIRSK 461
Cdd:PRK13644 2 IRLENVSYSYPdGTP---ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEP--VLFTASIKDNIAYGKEDATTE--EIKAAAELANASKfvdklpqGLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEI-------GLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAY- 615
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTl 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 15226477 616 ----SQLIRLQEEKKSDENAAEEQKMSSIESFKQSSLR 649
Cdd:PRK13644 232 gltpPSLIELAENLKMHGVVIPWENTSSPSSFAEEICR 269
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
384-612 |
3.55e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.61 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTY-PARPDEQI-FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL--KEFQLKWIR 459
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 460 SKIGLVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANAS--KFVDKLPqgldtmvgehgTQLSGGQKQ 529
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGpinlglSEEEIENRVKRAMNIVGLDyeDYKDKSP-----------FELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 530 RIAVARAILKDPRILLLDEATSALDAESErvvQEALDRIM-----VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS 603
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
....*....
gi 15226477 604 HTELLKDPE 612
Cdd:PRK13637 229 PREVFKEVE 237
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
385-598 |
4.15e-29 |
|
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: 116.09 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFqlkwiRSKIGL 464
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 VSQEPVL---FTASIKDNIA------------YGKEDAttEEIKAAAELANASKFVDKlpqgldtmvgeHGTQLSGGQKQ 529
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglyghkglfrrLSKADK--AKVDEALERVGLSELADR-----------QIGELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 530 RIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTV-RNADMIAVIHQGKI 598
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
112-322 |
4.26e-29 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 118.41 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 112 LGIGTFAAAFLqlSGW-----MISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAI 186
Cdd:cd18572 42 LLLLSVLSGLF--SGLrggcfSYAGTRLVRRLRRDLFRSLLRQDIAFFD-ATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 187 QLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAI 266
Cdd:cd18572 119 RNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 267 SNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQ 322
Cdd:cd18572 199 RRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1042-1249 |
5.72e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.35 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNETIRANIA--YGKGGDASESEIvssaelsnahgFISGLQQ-GYDTMVGERGI-QLSGGQKQRVAIARAIV 1197
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAI-----------FLDDLERfALPDTILTKNIaELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1198 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIV--VAHRLSTIKNAD-VI 1249
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADkVI 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1042-1261 |
7.65e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.05 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwlRQQTG 1121
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILF-NETIRANIAYG-KGGDASESEI---VSSAeLSNAHgfisgLQQgydtMVGERGIQLSGGQKQRVAIARAI 1196
Cdd:PRK09452 90 TVFQSYALFpHMTVFENVAFGlRMQKTPAAEItprVMEA-LRMVQ-----LEE----FAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1197 VKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAH-RLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
404-602 |
9.88e-29 |
|
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: 115.08 E-value: 9.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFIS---SGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWI----RSKIGLVSQEPVLFT-AS 475
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqQRKIGLVFQQYALFPhLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYGKEDATTEEIKaaaelanasKFVDKLPQ--GLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:cd03297 92 VRENLAFGLKRKRNREDR---------ISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226477 554 DAESERVVQEALDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKG 602
Cdd:cd03297 163 DRALRLQLLPELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
68-345 |
1.33e-28 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 117.23 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 68 LGSIGNGLGFPLmtlLFGDLIDAFGENQTNTTD-KVSKVALKFVWLGIGTFAAAFLQLSGWM--ISGERQAARIRSLYLK 144
Cdd:cd18573 6 LVSSAVTMSVPF---AIGKLIDVASKESGDIEIfGLSLKTFALALLGVFVVGAAANFGRVYLlrIAGERIVARLRKRLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 145 TILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALL 224
Cdd:cd18573 83 SILRQDAAFFD-KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 225 AIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYAL 304
Cdd:cd18573 162 GRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLS 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15226477 305 AVWYGGKLILDKGYTGGQVLNIII-AVLTGSmSLGQTSPCLS 345
Cdd:cd18573 242 VLYYGGSLVASGELTVGDLTSFLMyAVYVGS-SVSGLSSFYS 282
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1042-1261 |
1.60e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.65 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYP--ARPDVQifqDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQ 1119
Cdd:PRK13635 6 IRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPIlfNE----TIRANIAYGkggdaseseivssaeLSNahgfiSGLQQgyDTMVgER--------GIQ------ 1181
Cdd:PRK13635 83 VGMVFQNPD--NQfvgaTVQDDVAFG---------------LEN-----IGVPR--EEMV-ERvdqalrqvGMEdflnre 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1182 ---LSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALdRVMVNRTTIVV---AHRLSTIKNADVIAVVKNG 1255
Cdd:PRK13635 138 phrLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETV-RQLKEQKGITVlsiTHDLDEAAQADRVIVMNKG 216
|
....*.
gi 15226477 1256 VIVEKG 1261
Cdd:PRK13635 217 EILEEG 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
383-612 |
2.29e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 383 DIELKDVYFTYPAR-PdeqiFRGFSLF-----ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KE 452
Cdd:PRK13634 2 DITFQKVEHRYQYKtP----FERRALYdvnvsIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 453 FQLKWIRSKIGLVSQ--EPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVdklpqGLDTMVGEHGT-QLSGGQKQ 529
Cdd:PRK13634 78 KKLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELV-----GLPEELLARSPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 530 RIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTE 606
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232
|
....*.
gi 15226477 607 LLKDPE 612
Cdd:PRK13634 233 IFADPD 238
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1070-1261 |
2.53e-28 |
|
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: 113.93 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1070 GKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI----KSLRLKWLRQQTGLVSQEPILF-NETIRANIAYGKGG 1144
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1145 DASESEIVSSAELSNAHGfISGLQQGYDTmvgergiQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDAL 1224
Cdd:cd03297 103 KRNREDRISVDELLDLLG-LDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15226477 1225 DRVM--VNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKG 1261
Cdd:cd03297 175 KQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
720-992 |
3.95e-28 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 115.66 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 720 LILGSISAAANGVILPIFGILISSVIKAFFQPPkkLKEDTSFWAIIFMVLGFASIIaypaQTFFFAIAGCKLVQRIRSMC 799
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTAS--LNQIALLLLGLFLLQAVFSFF----RIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 800 FEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNG 879
Cdd:cd18576 76 YRHLQRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 880 FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSS 959
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250 260 270
....*....|....*....|....*....|....
gi 15226477 960 YAASFYVGARLVDDGKTTFDSVFR-VFFALTMAA 992
Cdd:cd18576 234 IVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG 267
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
384-612 |
4.53e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.19 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEP--VLFTASIKDNIAYGKED---ATTEEIKAAAELANASKFVDklpqgldtMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgiPREEMIKRVDEALLAVNMLD--------FKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 539 KDPRILLLDEATSALD----AESERVVQEALDRIMVnrTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
384-602 |
4.69e-28 |
|
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: 113.06 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTvALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEP-----------VLFTASIKDnIAYGKEDAtteEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIA 532
Cdd:cd03264 76 YLPQEFgvypnftvrefLDYIAWLKG-IPSKEVKA---RVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1042-1258 |
6.34e-28 |
|
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: 110.98 E-value: 6.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveikslrlkwlrqqtg 1121
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 lvsqEPILFNETIRANiaygkggdaseseivssaelsnahgfisglqqgydtmvgERGI----QLSGGQKQRVAIARAIV 1197
Cdd:cd03216 62 ----KEVSFASPRDAR---------------------------------------RAGIamvyQLSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1198 KDPKVLLLDEATSAL-DAESERVVqDALDRVMVNRTTIV-VAHRLSTIKN-ADVIAVVKNGVIV 1258
Cdd:cd03216 99 RNARLLILDEPTAALtPAEVERLF-KVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1042-1255 |
8.85e-28 |
|
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: 112.60 E-value: 8.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQIfQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwLRQQTG 1121
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANIA-YG--KGGdaSESEIVSSAELSnAHGFisGLQQGYDTMVGergiQLSGGQKQRVAIARAIV 1197
Cdd:cd03263 79 YCPQFDALFDElTVREHLRfYArlKGL--PKSEIKEEVELL-LRVL--GLTDKANKRAR----TLSGGMKRKLSLAIALI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1198 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKN-ADVIAVVKNG 1255
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDG 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
398-612 |
1.06e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 113.31 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAG-----DVLIDG---INLKEFQLKWIRSKIGLVSQEP 469
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTarsLSQQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 470 VLFT-ASIKDNIAYGKEdATTEEIKAAAElANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:PRK11264 95 NLFPhRTVLENIIEGPV-IVKGEPKEEAT-ARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 549 ATSALDAEserVVQEALDRIMV----NRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK11264 171 PTSALDPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1042-1261 |
1.97e-27 |
|
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: 111.13 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTvALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwLRQQTG 1121
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILF-NETIRANIAYGkggdASESEIVSSAELSNAHGFIS--GLQQGYDTMVGergiQLSGGQKQRVAIARAIVK 1198
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYI----AWLKGIPSKEVKARVDEVLElvNLGDRAKKKIG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
404-611 |
2.82e-27 |
|
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: 114.82 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSL---FISSGTTV-ALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KEFQLKWIRSKIGLVSQEPVLFT-A 474
Cdd:TIGR02142 11 DFSLdadFTLPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPhL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 SIKDNIAYGKEDATTEEIKAAAElanasKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALD 554
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERRISFE-----RVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 555 AESERVVQEALDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:TIGR02142 164 DPRKYEILPYLERLHaeFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1042-1259 |
6.02e-27 |
|
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: 110.60 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYP-ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL----RLKWL 1116
Cdd:COG4181 9 IELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedaRARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1117 RQQTGLVSQ-EPILFNETIRANIAY-----GKGGDASESEivssAELSNAhgfisGLqqgydtmvGERG----IQLSGGQ 1186
Cdd:COG4181 89 ARHVGFVFQsFQLLPTLTALENVMLplelaGRRDARARAR----ALLERV-----GL--------GHRLdhypAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1187 KQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR---TTIV-VAHRLSTIKNADVIAVVKNGVIVE 1259
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE--LNRergTTLVlVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1042-1214 |
7.07e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.11 E-value: 7.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPA-RPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIK---SLRlkwlr 1117
Cdd:COG4525 4 LTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 qqtGLVSQEPILFN-ETIRANIAYG---KGGDASESEIVSSAELSnahgfISGLQQgydtmVGERGI-QLSGGQKQRVAI 1192
Cdd:COG4525 79 ---GVVFQKDALLPwLNVLDNVAFGlrlRGVPKAERRARAEELLA-----LVGLAD-----FARRRIwQLSGGMRQRVGI 145
|
170 180
....*....|....*....|..
gi 15226477 1193 ARAIVKDPKVLLLDEATSALDA 1214
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDA 167
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
406-611 |
1.14e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.89 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIGLVSQEPVLFT-ASIKDNIAYG- 483
Cdd:PRK11432 26 NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPhMSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 484 ------KEDaTTEEIKAAAELANASKFVDKLpqgLDtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 557
Cdd:PRK11432 104 kmlgvpKEE-RKQRVKEALELVDLAGFEDRY---VD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 558 ERVVQEALDRIM--VNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK11432 172 RRSMREKIRELQqqFNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-612 |
1.43e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.00 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVS----LIERFYDPQ-AGDVLIDGINLKEFQLKWI 458
Cdd:PRK14247 4 IEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 459 RSKIGLVSQEP-VLFTASIKDNIAYG-------KEDATTEE-IKAAAELAnasKFVDKLPQGLDTMVGehgtQLSGGQKQ 529
Cdd:PRK14247 81 RRRVQMVFQIPnPIPNLSIFENVALGlklnrlvKSKKELQErVRWALEKA---QLWDEVKDRLDAPAG----KLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 530 RIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
....
gi 15226477 609 KDPE 612
Cdd:PRK14247 234 TNPR 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
406-615 |
1.73e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.59 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF---QLKWIR-SKIGLVSQEPVLFT-ASIKDNI 480
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRrKKIAMVFQSFALMPhMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 481 AYGKEDATTeeikAAAElaNASKFVDKLPQ-GLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 559
Cdd:PRK10070 128 AFGMELAGI----NAEE--RREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 560 VVQEALDRIMV--NRTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:PRK10070 202 EMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1065-1266 |
1.81e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.84 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR--------LKWLRQQTGLVSQEPILF-NETIR 1135
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkglIRQLRQHVGFVFQNFNLFpHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1136 ANIAYGK---GGDASESEIVSSAELSNAHGfISGLQQGYDTmvgergiQLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1212
Cdd:PRK11264 104 ENIIEGPvivKGEPKEEATARARELLAKVG-LAGKETSYPR-------RLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1213 DAEserVVQDALDRVMV----NRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTL 1266
Cdd:PRK11264 176 DPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
384-610 |
1.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.64 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTY-PARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KEFQLKW 457
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEhQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 458 IRSKIGLVSQ--EPVLFTASIKDNIAYGKED--ATTEEIKAAA-----ELANASKFVDKLPqgldtmvgehgTQLSGGQK 528
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKNYAhrllmDLGFSRDVMSQSP-----------FQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 529 QRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMV--NRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHT 605
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPK 231
|
....*
gi 15226477 606 ELLKD 610
Cdd:PRK13646 232 ELFKD 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
384-611 |
2.57e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.35 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKefQLKWIRSKIG 463
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFT-ASIKDNIAYGKEDATTEEIKAAAELANASKFVDklpqgLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQ-----LEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 543 ILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAH----RLSTvrnADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
60-310 |
3.17e-26 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 110.22 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIGnGLGFPLMTllfGDLIDAFGENQTNTTdkvskvalkFVWLGIGTF-AAAFLQ-LSGWMIS--GERQA 135
Cdd:cd18551 2 ILALLLSLLGTAA-SLAQPLLV---KNLIDALSAGGSSGG---------LLALLVALFlLQAVLSaLSSYLLGrtGERVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 136 ARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIP 215
Cdd:cd18551 69 LDLRRRLWRRLLRLPVSFFD-RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 216 LLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLF 295
Cdd:cd18551 148 LAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMG 227
|
250
....*....|....*
gi 15226477 296 LVVFCSYALAVWYGG 310
Cdd:cd18551 228 LAVQLALLVVLGVGG 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1041-1261 |
3.28e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1041 DIELRHVSFKYPAR-PdvqiFQ-----DLCLSIRAGKTVALVGESGSGKSTVI----ALLQrfydPDSGEITLDGVEI-- 1108
Cdd:PRK13634 2 DITFQKVEHRYQYKtP----FErralyDVNVSIPSGSYVAIIGHTGSGKSTLLqhlnGLLQ----PTSGTVTIGERVIta 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1109 --KSLRLKWLRQQTGLVSQ--EPILFNETIRANIAYG-KGGDASESEIVSSAelsnahgfisglqqgyDTMVGERGI--- 1180
Cdd:PRK13634 74 gkKNKKLKPLRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQKA----------------REMIELVGLpee 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1181 -------QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLSTIKN-ADVIA 1250
Cdd:PRK13634 138 llarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIV 217
|
250
....*....|.
gi 15226477 1251 VVKNGVIVEKG 1261
Cdd:PRK13634 218 VMHKGTVFLQG 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
402-612 |
3.74e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 111.73 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 402 FRGFSL-----FISSGTTvALVGQSGSGKSTVVSLI---ERfydPQAGDVLIDG---------INLK-EfqlkwiRSKIG 463
Cdd:COG4148 11 RGGFTLdvdftLPGRGVT-ALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGevlqdsargIFLPpH------RRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLF-TASIKDNIAYGkedatteeIKAAAELANASKF---VDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:COG4148 81 YVFQEARLFpHLSVRGNLLYG--------RKRAPRAERRISFdevVELL--GIGHLLDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 540 DPRILLLDEATSALDAES--------ERVVQEAldRIMVnrttVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:COG4148 151 SPRLLLMDEPLAALDLARkaeilpylERLRDEL--DIPI----LYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSR 224
|
..
gi 15226477 611 PE 612
Cdd:COG4148 225 PD 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
60-341 |
4.06e-26 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 109.88 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIGNGLGFplmtllfgdLIDA-FGENQTNTTDKvSKVALKFVWLGIGTFAAAFLQLSGWMisGERQAARI 138
Cdd:cd18575 4 ALLIAAAATLALGQGLRL---------LIDQgFAAGNTALLNR-AFLLLLAVALVLALASALRFYLVSWL--GERVVADL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 139 RSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLV 218
Cdd:cd18575 72 RKAVFAHLLRLSPSFFE-TTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 219 MAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVV 298
Cdd:cd18575 151 LPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15226477 299 FCSYALAVWYGGKLILDKGYTGGQVLNIII-AVLTGSmSLGQTS 341
Cdd:cd18575 231 FGAIVFVLWLGAHDVLAGRMSAGELSQFVFyAVLAAG-SVGALS 273
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
395-592 |
8.16e-26 |
|
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: 106.41 E-value: 8.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWiRSKIGLVSQEPVLFTA 474
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 -SIKDNIAY----GKEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEA 549
Cdd:COG4133 90 lTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15226477 550 TSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRNADMIAV 592
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1026-1261 |
9.02e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 113.24 E-value: 9.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1026 DPSVESGRVLdnvkgdIELRHVSFKYPAR--------PDVQIFQDLCLSIRAGKTVALVGESGSGKSTV-IALLQrfYDP 1096
Cdd:COG4172 266 RPVPPDAPPL------LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLR--LIP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1097 DSGEITLDGVEIKSLR---LKWLRQQTGLVSQEPilFNE-----TIRANIA-----YGKGGDASE-SEIVSSAelsnahg 1162
Cdd:COG4172 338 SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAeglrvHGPGLSAAErRARVAEA------- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1163 fisgLQQ-GYDTMVGERGI-QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDaeseRVVQ----DALDRVMVNR--TTI 1234
Cdd:COG4172 409 ----LEEvGLDPAARHRYPhEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqilDLLRDLQREHglAYL 480
|
250 260
....*....|....*....|....*...
gi 15226477 1235 VVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:COG4172 481 FISHDLAVVRAlAHRVMVMKDGKVVEQG 508
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1042-1259 |
1.89e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDG--VEIKSLRLkwlRQQ 1119
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRD---AQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TG--LVSQEPILFNE-TIRANIAYG----KGGDASESEIVSSA-ELSNAHGF-ISGlqqgyDTMVGErgiqLSGGQKQRV 1190
Cdd:COG1129 79 AGiaIIHQELNLVPNlSVAENIFLGreprRGGLIDWRAMRRRArELLARLGLdIDP-----DTPVGD----LSVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1191 AIARAIVKDPKVLLLDEATSAL-DAESER---VVQDALDRvmvNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVE 1259
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLtEREVERlfrIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
398-623 |
1.99e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.98 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN----------LKEF---QLKWIRSKIGL 464
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVAdknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 VSQEPVLFT-ASIKDNIAYGKEDATTEEIKAAAElaNASKFVDKLpqGLDTMV-GEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:PRK10619 97 VFQHFNLWShMTVLENVMEAPIQVLGLSKQEARE--RAVKYLAKV--GIDERAqGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 543 ILLLDEATSALDAEserVVQEALdRIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAys 616
Cdd:PRK10619 173 VLLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQSP-- 246
|
....*..
gi 15226477 617 qliRLQE 623
Cdd:PRK10619 247 ---RLQQ 250
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1042-1255 |
2.27e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.51 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEP--ILFNETIRANIAYG---KGGDASE--SEIVSSAELSNAHGFISglqqgydtmvgERGIQLSGGQKQRVAIAR 1194
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGlenKGIPHEEmkERVNEALELVGMQDFKE-----------REPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESE----RVVQDALDRvmVNRTTIVVAHRLSTIKNADVIAVVKNG 1255
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1268 |
2.28e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.13 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYpaRPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEP--ILFNETIRANIAYG---KGGDASESEIVSSAELSnahgfISGLQQGYDtmvgERGIQLSGGQKQRVAIARAI 1196
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnMGLDKDEVERRVEEALK-----AVRMWDFRD----KPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1197 VKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLS-TIKNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
382-610 |
2.69e-25 |
|
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: 107.25 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFTYpARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQaGDVLIDGINLKEFQLKWIRSK 461
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTASIKDNI-AYGKEdaTTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 541 PRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1042-1262 |
2.76e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.14 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQ---IFqDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI----KSLRLK 1114
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgraLF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WLRQQTGLVSQ--EPILFNETIRANIAYG-KGGDASESEIVSSAELSNAHGFISglqqgyDTMVGERGIQLSGGQKQRVA 1191
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGpQNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIV-VAHRLSTIKN-ADVIAVVKNGVIVEKGK 1262
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
406-616 |
2.81e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.54 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKefQLKWIRSKIGLVSQEPVLFT-ASIKDNIAYG- 483
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPhMTVEQNIAFGl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 484 KEDATTE-EIKAAAE----LANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE-S 557
Cdd:PRK11607 117 KQDKLPKaEIASRVNemlgLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 558 ERVVQEALDRI-MVNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYS 616
Cdd:PRK11607 186 DRMQLEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
379-624 |
3.12e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.40 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 379 DIKGDIELKDVYFTYPAR-PDEqiFRGF---SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG----INL 450
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKtPFE--FKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 451 KEF-QLKWIRSKIGLVSQEP--VLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVdKLPQgldTMVGEHGTQLSGGQ 527
Cdd:PRK13645 80 KKIkEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPE---DYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 528 KQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVN--RTTVVVAHRLSTV-RNADMIAVIHQGKIVEKG-- 602
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGsp 235
|
250 260 270
....*....|....*....|....*....|
gi 15226477 603 ----SHTELLK----DPEGAYSQLIRLQEE 624
Cdd:PRK13645 236 feifSNQELLTkieiDPPKLYQLMYKLKNK 265
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1042-1261 |
3.37e-25 |
|
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: 104.88 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqifQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwlRQQTG 1121
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANIAYGKggdaSESEIVSSAELSNAHGFISglQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDP 1200
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGL----SPGLKLTAEDRQAIEVALA--RVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1201 KVLLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-617 |
3.47e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.28 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF---YDPQA---GDVLIDGINLKEFQLKWIRSKIGLVSQEPVL 471
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKIkvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 472 FT-ASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEAT 550
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 551 SALDAESERVVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQ 617
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1043-1258 |
4.20e-25 |
|
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: 104.26 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYPARPDvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSlrlKWLRQQTGL 1122
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1123 VSQEP--ILFNETIRANIAYGKGGDASESEIVSS-------AELSNAHGFIsglqqgydtmvgergiqLSGGQKQRVAIA 1193
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKELDAGNEQAETvlkdldlYALKERHPLS-----------------LSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1194 RAIVKDPKVLLLDEATSALDAESERVVQDALDRVM-VNRTTIVVAHRLSTIKN-ADVIAVVKNGVIV 1258
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
404-617 |
4.86e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 111.31 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGTTVALVGQSGSGKST----VVSLIerfydPQAGDVLIDGIN---LKEFQLKWIRSKIGLVSQEPvlFTA-- 474
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDldgLSRRALRPLRRRMQVVFQDP--FGSls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 ---SIKDNIAYG------KEDATTEEIKAAAELANAskfvdklpqGLD-TMVGEHGTQLSGGQKQRIAVARAILKDPRIL 544
Cdd:COG4172 377 prmTVGQIIAEGlrvhgpGLSAAERRARVAEALEEV---------GLDpAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 545 LLDEATSALDaeseRVVQ----EALDRIMVNR--TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAYSQ 617
Cdd:COG4172 448 VLDEPTSALD----VSVQaqilDLLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTR 523
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
725-995 |
8.92e-25 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 106.03 E-value: 8.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 725 ISAAANGVIlpifGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFAsiIAYPAQTFFFAIAGCKLVQRIRSMCFEKVV 804
Cdd:cd18575 7 IAAAATLAL----GQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLA--LASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 805 HMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMK 884
Cdd:cd18575 81 RLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 885 FMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASF 964
Cdd:cd18575 159 RVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVL 238
|
250 260 270
....*....|....*....|....*....|...
gi 15226477 965 YVGARLVDDGKTTFD--SVFrVFFALtMAAMAI 995
Cdd:cd18575 239 WLGAHDVLAGRMSAGelSQF-VFYAV-LAAGSV 269
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
384-613 |
8.97e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.22 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYpaRPDEQI-FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKI 462
Cdd:PRK13648 8 IVFKNVSFQY--QSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEPV-LFTASI-KDNIAYGKE------DATTEEIKAAAELANASKFVDKLPQGLdtmvgehgtqlSGGQKQRIAVA 534
Cdd:PRK13648 86 GIVFQNPDnQFVGSIvKYDVAFGLEnhavpyDEMHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
.
gi 15226477 613 G 613
Cdd:PRK13648 235 E 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
384-612 |
1.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.16 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLKWIRSK 461
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAV 533
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
.
gi 15226477 612 E 612
Cdd:PRK13639 229 E 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1042-1268 |
1.05e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.33 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDG--------VEIKSLRL 1113
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1114 kwLRQQTGLVSQE----PILfneTIRANI--AYGKGGDASESEIVSSAElsnahGFISGLQQgydTMVGER-GIQLSGGQ 1186
Cdd:PRK11124 80 --LRRNVGMVFQQynlwPHL---TVQQNLieAPCRVLGLSKDQALARAE-----KLLERLRL---KPYADRfPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1187 KQRVAIARAIVKDPKVLLLDEATSALDAE-SERVVQDALDRVMVNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGKHD 1264
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDAS 226
|
....
gi 15226477 1265 TLIN 1268
Cdd:PRK11124 227 CFTQ 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
384-599 |
1.18e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.78 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFT-YPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQlkwi 458
Cdd:COG1101 2 LELKNLSKTfNPGTVNEkRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 459 RSK-IGLVSQEPVLFTA---SIKDN--IAYGKEDA-------TTEEIKAAAELanaskfVDKLPQGL----DTMVGehgt 521
Cdd:COG1101 78 RAKyIGRVFQDPMMGTApsmTIEENlaLAYRRGKRrglrrglTKKRRELFREL------LATLGLGLenrlDTKVG---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 522 QLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRImVNR---TTVVVAHRLS-TVRNADMIAVIHQGK 597
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMEqALDYGNRLIMMHEGR 226
|
..
gi 15226477 598 IV 599
Cdd:COG1101 227 II 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1042-1266 |
1.19e-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: 104.40 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSG-EITLDGVEIKSLRLKWLRQQT 1120
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVS---QEPILFNETIRaniaygkggdasesEIVssaeLSNAHGFIsGLQQGYDTMVGER--------GI--------- 1180
Cdd:COG1119 81 GLVSpalQLRFPRDETVL--------------DVV----LSGFFDSI-GLYREPTDEQRERarellellGLahladrpfg 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1181 QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES-ERVVQdALDRVMVNR-TTIV-VAHRLStiknaDVIAVV----- 1252
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArELLLA-LLDKLAAEGaPTLVlVTHHVE-----EIPPGIthvll 215
|
250
....*....|....*.
gi 15226477 1253 -KNGVIVEKG-KHDTL 1266
Cdd:COG1119 216 lKDGRVVAAGpKEEVL 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1042-1262 |
1.46e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGE---ITLDGVEIKSLRLKWLRQ 1118
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEP--ILFNETIRANIAYGkggdaSESEIVSSAE-LSNAHGFISglQQGYDTMVGERGIQLSGGQKQRVAIARA 1195
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFG-----LENRAVPRPEmIKIVRDVLA--DVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1196 IVKDPKVLLLDEATSALDAESERVVQDALDRVMV--NRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGK 1262
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1027-1262 |
1.50e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1027 PSVESGRVLDNVkgdIELRHVSFKYPARPDVQifqDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGV 1106
Cdd:PRK11607 8 PQAKTRKALTPL---LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1107 EIkSLRLKWLRQqTGLVSQEPILF-NETIRANIAYG-KGGDASESEIVSSAE--LSNAHgfisgLQQgydtMVGERGIQL 1182
Cdd:PRK11607 82 DL-SHVPPYQRP-INMMFQSYALFpHMTVEQNIAFGlKQDKLPKAEIASRVNemLGLVH-----MQE----FAKRKPHQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1183 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAE-SERV---VQDALDRVMVnrTTIVVAH-RLSTIKNADVIAVVKNGVI 1257
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMqleVVDILERVGV--TCVMVTHdQEEAMTMAGRIAIMNRGKF 228
|
....*
gi 15226477 1258 VEKGK 1262
Cdd:PRK11607 229 VQIGE 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1273 |
2.19e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.06 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQIfQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEP--ILFNETIRANIAYGKggdasESEIVSSAELsnaHGFISGLQQGYDtMVGERGIQ---LSGGQKQRVAIARAI 1196
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGL-----ENHAVPYDEM---HRRVSEALKQVD-MLERADYEpnaLSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1197 VKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKDGV 1273
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
384-596 |
2.33e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. 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: 213257 [Multi-domain] Cd Length: 218 Bit Score: 102.79 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK-- 461
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 --IGLVSQEPVLFTASIKDNIAYGKEdATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:cd03290 79 ysVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 540 DPRILLLDEATSALDAE-SERVVQEALDRIMVN--RTTVVVAHRLSTVRNADMIAVIHQG 596
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
384-602 |
2.56e-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: 102.19 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYparpDEQIFRgFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIG 463
Cdd:cd03298 1 VRLDKIRFSY----GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFT-ASIKDNIAYGKEDAT--TEEIKAAAELANASkfvdklpQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGLklTAEDRQAIEVALAR-------VGLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 541 PRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
404-617 |
3.22e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.05 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGTTVALVGQSGSGKSTV---VSLIERfydPQAGDVLIDGINLKEF---QLKWIRSKIGLVSQEPvlftasik 477
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNP-------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 478 dniaYG------KEDATTEE-------IKAAAELANASKFVDKLpqGLDTmvgEHGTQ----LSGGQKQRIAVARAILKD 540
Cdd:PRK11308 102 ----YGslnprkKVGQILEEpllintsLSAAERREKALAMMAKV--GLRP---EHYDRyphmFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 541 PRILLLDEATSALDAEservVQ-EALDRIM-----VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEG 613
Cdd:PRK11308 173 PDVVVADEPVSALDVS----VQaQVLNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
....
gi 15226477 614 AYSQ 617
Cdd:PRK11308 249 PYTQ 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
403-603 |
4.19e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.32 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYD--PQA---GDVLIDGINL--KEFQLKWIRSKIGLVSQEPVLFTAS 475
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYGKE--------DATTEEIKAAAELANASKfvDKLPQGldtmvgehGTQLSGGQKQRIAVARAILKDPRILLLD 547
Cdd:PRK14243 107 IYDNIAYGARingykgdmDELVERSLRQAALWDEVK--DKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 548 EATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQgKIVEKGS 603
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFNV-ELTEGGG 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1046-1261 |
4.26e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 108.23 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1046 HVSFKYPARpDVQIFQDLCLSIRAGKTVALVGESGSGKS----TVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQ--- 1118
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 -QTGLVSQEPI-----LFneTIRANIA------YGKGGDASESEIVssaELsnahgfisgLQQgydtmVG----ERGI-- 1180
Cdd:COG4172 92 nRIAMIFQEPMtslnpLH--TIGKQIAevlrlhRGLSGAAARARAL---EL---------LER-----VGipdpERRLda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1181 ---QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAeserVVQ----DALDRvMVNRTTIVVA---HRLSTIKN-ADVI 1249
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKD-LQRELGMALLlitHDLGVVRRfADRV 227
|
250
....*....|..
gi 15226477 1250 AVVKNGVIVEKG 1261
Cdd:COG4172 228 AVMRQGEIVEQG 239
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
384-607 |
4.57e-24 |
|
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: 101.81 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTA-SIKDNIAY-----GKEDatTEEIKAAAELANASKFVDKLpqglDTMVGehgtQLSGGQKQRIAVARAI 537
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPK--SEIKEEVELLLRVLGLTDKA----NKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
382-580 |
6.00e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.97 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 382 GDIELKDVYFtypARPDEQ-IFRGFSLFISSGTTVALVGQSGSGKSTVV-SL----------IERfydPQAGDVLidgin 449
Cdd:COG4178 361 GALALEDLTL---RTPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTLLrAIaglwpygsgrIAR---PAGARVL----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 450 lkefqlkwirskigLVSQEPVLFTASIKDNIAY--GKEDATTEEIKAAAELANASKFVDKLPQGLDTmvgehGTQLSGGQ 527
Cdd:COG4178 430 --------------FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15226477 528 KQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHR 580
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1042-1268 |
6.07e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 6.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDG--------VEIKSLRL 1113
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1114 kwLRQQTGLVSQE----PILfneTIRANI--AYGKGGDASESEIVSSAElsnahGFISGLQqgYDTMVGERGIQLSGGQK 1187
Cdd:COG4161 80 --LRQKVGMVFQQynlwPHL---TVMENLieAPCKVLGLSKEQAREKAM-----KLLARLR--LTDKADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1188 QRVAIARAIVKDPKVLLLDEATSALDAE-SERVVQDALDRVMVNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGKHDT 1265
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDASH 227
|
...
gi 15226477 1266 LIN 1268
Cdd:COG4161 228 FTQ 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
400-612 |
7.21e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.78 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIGLVSQEPVLFT-ASIKD 478
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 479 NIAYG------KEDATTEEIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKVtqllEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 549 ATSALDAEservVQEALDRIM------VNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK10851 163 PFGALDAQ----VRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
399-602 |
7.51e-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: 100.32 E-value: 7.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 399 EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI--ERFYDPQAGDVLIDGINLKefqLKWIRSKIGLVSQEPVLF-TAS 475
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHpTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYgkedatteeikaAAELanaskfvdklpQGldtmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDA 555
Cdd:cd03213 99 VRETLMF------------AAKL-----------RG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15226477 556 ESERVVQEALdRIMV--NRTTVVVAHRLST--VRNADMIAVIHQGKIVEKG 602
Cdd:cd03213 145 SSALQVMSLL-RRLAdtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
384-610 |
8.14e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPA-RPdeqiFRGFSLF-----ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KEF 453
Cdd:PRK13649 3 INLQNVSYTYQAgTP----FEGRALFdvnltIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 454 QLKWIRSKIGLVSQ--EPVLFTASIKDNIAYG-------KEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLS 524
Cdd:PRK13649 79 DIKQIRKKVGLVFQfpESQLFEETVLKDVAFGpqnfgvsQEEAEALAREKLALVGISESLFEKNP-----------FELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 525 GGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
....*...
gi 15226477 603 SHTELLKD 610
Cdd:PRK13649 228 KPKDIFQD 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
384-624 |
8.74e-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: 102.08 E-value: 8.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAG-DVLIDGINLKEFQLKWIRSKI 462
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVS---QEPVLFTASIKDNIAYGKED-------ATTEEIKAAAELANASkfvdklpqGLDTMVGEHGTQLSGGQKQRIA 532
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyrePTDEQRERARELLELL--------GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMVN--RTTVVVAHRLStvrnaDMIAVIH------QGKIVEKGSH 604
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVE-----EIPPGIThvlllkDGRVVAAGPK 227
|
250 260
....*....|....*....|..
gi 15226477 605 TELLKDP--EGAYSQLIRLQEE 624
Cdd:COG1119 228 EEVLTSEnlSEAFGLPVEVERR 249
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
763-977 |
1.05e-23 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 102.77 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 763 AIIFM-VLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLA 841
Cdd:cd18784 38 AIIIMgLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDT--VKTGDITSRLTSDTTTMSDTVSLNLN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 842 QTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18784 116 IFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANED 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 922 KVMNMYSKKCEGPMKNGIRQGIVSGiGFGFSFFVLFSSYAAS-FYVGARLVDDGKTT 977
Cdd:cd18784 196 GEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELALTVStLYYGGHLVITGQIS 251
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
384-608 |
1.09e-23 |
|
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: 102.19 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYP------ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF---Q 454
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 455 LKWIRSKIGLVSQE-PVLFTA--SIKDNIA-----YGKEDATTEEIKAAAELANA---SKFVDKLPQgldtmvgehgtQL 523
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNPrmTVRQIIGeplrhLTSLDESEQKARIAELLDMVglrSEDADKLPR-----------QL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 524 SGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTT--VVVAHRLSTV-RNADMIAVIHQGKIVE 600
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
....*...
gi 15226477 601 KGSHTELL 608
Cdd:TIGR02769 232 ECDVAQLL 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
416-612 |
1.82e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.01 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 416 ALVGQSGSGKSTVVSLIERFYD--PQ---AGDVLIDGINLKEFQLKW--IRSKIGLVSQEPVLFTASIKDNIAYG----- 483
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPMSIYENVVYGlrlkg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 484 ---KE--DATTEEIKAAAELANASKfvDKLPqglDTMVGehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:PRK14239 115 ikdKQvlDEAVEKSLKGASIWDEVK--DRLH---DSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 559 RVVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK14239 185 GKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
400-617 |
2.01e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.92 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKS----TVVSLIERFYDPQAGDVLIDGINL---KEFQLKWIR-SKIGLVSQEPV- 470
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRgNRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 ----LFTasIKDNIA--------YGKEDATTEEIKAAAE--LANASKFVDKLPqgldtmvgeHgtQLSGGQKQRIAVARA 536
Cdd:COG4172 104 slnpLHT--IGKQIAevlrlhrgLSGAAARARALELLERvgIPDPERRLDAYP---------H--QLSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 537 ILKDPRILLLDEATSALDAeserVVQ----EALDRIMVNRTTVVV--AHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG4172 171 LANEPDLLIADEPTTALDV----TVQaqilDLLKDLQRELGMALLliTHDLGVVRRfADRVAVMRQGEIVEQGPTAELFA 246
|
....*...
gi 15226477 610 DPEGAYSQ 617
Cdd:COG4172 247 APQHPYTR 254
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
63-322 |
2.41e-23 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 101.86 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTNTTdkvskvalkFVWLGIGTFAAAFLQ-----LSGWMIS--GERQA 135
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL---------LLWIALLLLLLALLRallsyLRRYLAArlGQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 136 ARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIP 215
Cdd:cd07346 72 FDLRRDLFRHLQRLSLSFFD-RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 216 LLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLF 295
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
250 260
....*....|....*....|....*..
gi 15226477 296 LVVFCSYALAVWYGGKLILDKGYTGGQ 322
Cdd:cd07346 231 LLTALGTALVLLYGGYLVLQGSLTIGE 257
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1058-1261 |
2.67e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 98.78 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1058 QIFQDLCLSIRAGKTVALVGESGSGKSTVIALL--QRFYDPDSGEITLDGveiKSLRLKWLRQQTGLVSQEPILF-NETI 1134
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDILHpTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1135 RANIAYgkggdaseseivsSAELsnahgfisglqqgydtmvgeRGIqlSGGQKQRVAIARAIVKDPKVLLLDEATSALDA 1214
Cdd:cd03213 100 RETLMF-------------AAKL--------------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 1215 ESERVVQDALDR-VMVNRTTIVVAHRLST--IKNADVIAVVKNGVIVEKG 1261
Cdd:cd03213 145 SSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1043-1215 |
2.68e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.48 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPD---SGEITLDGVEIksLRLKWLRQQ 1119
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL--TALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILF-NETIRANIAYG---KGGDASESEIVSSAeLSNAhgfisGLQqGYdtmvGERGI-QLSGGQKQRVAIAR 1194
Cdd:COG4136 78 IGILFQDDLLFpHLSVGENLAFAlppTIGRAQRRARVEQA-LEEA-----GLA-GF----ADRDPaTLSGGQRARVALLR 146
|
170 180
....*....|....*....|.
gi 15226477 1195 AIVKDPKVLLLDEATSALDAE 1215
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAA 167
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1042-1269 |
2.81e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKY-PARP-DVQIFQDLCLSIRAGKTVALVGESGSGKSTviaLLQRF---YDPDSGEITLDGVEIK----SLR 1112
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKST---LMQHFnalLKPSSGTITIAGYHITpetgNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1113 LKWLRQQTGLVSQ--EPILFNETIRANIAYG-KGGDASESEIVSSAelsnahgfISGLQQ-GYDTMVGERG-IQLSGGQK 1187
Cdd:PRK13641 80 LKKLRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDEAKEKA--------LKWLKKvGLSEDLISKSpFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1188 QRVAIARAIVKDPKVLLLDEATSALDAES-ERVVQDALDRVMVNRTTIVVAHRLSTI-KNADVIAVVKNGVIVekgKHDT 1265
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLI---KHAS 228
|
....
gi 15226477 1266 LINI 1269
Cdd:PRK13641 229 PKEI 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
384-605 |
3.45e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPArpdEQIFRGFSLFISSGTTVALVGQSGSGKST---VVSLIERfydPQAGDVLIDGINL------KEFQ 454
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGNHFdfsktpSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 455 LKWIRSKIGLVSQE----PVLftaSIKDNI--------AYGKEDATTEEIKAAAELaNASKFVDKLPQgldtmvgehgtQ 522
Cdd:PRK11124 77 IRELRRNVGMVFQQynlwPHL---TVQQNLieapcrvlGLSKDQALARAEKLLERL-RLKPYADRFPL-----------H 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 523 LSGGQKQRIAVARAILKDPRILLLDEATSALDAE-SERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVE 600
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
....*
gi 15226477 601 KGSHT 605
Cdd:PRK11124 222 QGDAS 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1040-1239 |
3.48e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.66 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFkypARPDVQ-IFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRFYdpdSGEITL-DGVEIkslrlk 1114
Cdd:COG4178 361 GALALEDLTL---RTPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTllrAIAGLWPYG---SGRIARpAGARV------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 wLrqqtgLVSQEPILFNETIRANIAYGKGGDA-SESEIVSSAELSNAHGFISGLQQGYDtmvgeRGIQLSGGQKQRVAIA 1193
Cdd:COG4178 429 -L-----FLPQRPYLPLGTLREALLYPATAEAfSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15226477 1194 RAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHR 1239
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
400-610 |
3.66e-23 |
|
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: 99.43 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQLkwIRSKIGLVSQEPVLF-TAS 475
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrdiTGLPPHER--ARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYGKEDATTEEIKAAAElanasKFVDKLPQgLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALda 555
Cdd:cd03224 92 VEENLLLGAYARRRAKRKARLE-----RVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL-- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 556 eSERVVQEALDRIM-VNR---TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:cd03224 164 -APKIVEEIFEAIReLRDegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
384-612 |
5.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTY-PARPDEQI-FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG----INLKEFQLKW 457
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 458 IRSKIGLVSQ--EPVLFTASIKDNIAYGKED--ATTEEIKAAAelanaSKFVDKLpqGLDTMVGEHGT-QLSGGQKQRIA 532
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKA-----LKWLKKV--GLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAES-ERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
..
gi 15226477 611 PE 612
Cdd:PRK13641 236 KE 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
403-612 |
5.83e-23 |
|
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: 99.05 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQlkwiRSKIGLVS--QEPVLFTA-SI 476
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGediTGLPPHE----IARLGIGRtfQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 477 KDNIAYG---------KEDATTEEIKAAAELANAS-KFVdKLPQGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLL 546
Cdd:cd03219 93 LENVMVAaqartgsglLLARARREEREARERAEELlERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 547 DEATSAL-DAESERVVqEALDRIMV-NRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:cd03219 168 DEPAAGLnPEETEELA-ELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
720-991 |
5.94e-23 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 100.57 E-value: 5.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 720 LILGSISAAANGVILPIFGILISSVIKAffqppkklKEDTSFWAIIFMVLGFASI--IAYPAQTFFFAIAGCKLVQRIRS 797
Cdd:cd18552 5 ILGMILVAATTAALAWLLKPLLDDIFVE--------KDLEALLLVPLAIIGLFLLrgLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 798 MCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIAL 877
Cdd:cd18552 77 DLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 878 NGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLF 957
Cdd:cd18552 155 PIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGA 234
|
250 260 270
....*....|....*....|....*....|....
gi 15226477 958 SSYAASFYVGARLVDDGKTTFDSVFRVFFALTMA 991
Cdd:cd18552 235 IAIALVLWYGGYQVISGELTPGEFISFITALLLL 268
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
395-608 |
7.18e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.76 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF---QLKWIRSKIGLVSQEPvl 471
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 472 FTA-----SIKDNIAY----------GKEDATTEEIKAAAELANAskFVDKLPQgldtmvgehgtQLSGGQKQRIAVARA 536
Cdd:PRK10419 99 ISAvnprkTVREIIREplrhllsldkAERLARASEMLRAVDLDDS--VLDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 537 ILKDPRILLLDEATSALDaeseRVVQ----EALDRIMVNRTT--VVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQagviRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKL 240
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1058-1282 |
9.03e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.85 E-value: 9.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1058 QIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI----KSLRLKWLRQQTGLVSQ--EPILFN 1131
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1132 ETIRANIAYGKGGDASESEIVSSaelsNAHGFIsgLQQGYDTMVGERG-IQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1210
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDEVKN----YAHRLL--MDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1211 ALDAESERVVQDALDRVMV--NRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGKHDTLINIKDgvyaSLVQLHL 1282
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDKK----KLADWHI 245
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-612 |
9.06e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.15 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYD--PQA---GDVLIDGINLKEFQLKWI--RSKIGLVSQEPV 470
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDPIevRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 LFT-ASIKDNIAYGKEdaTTEEIKAAAELANASKFVDK---LPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLL 546
Cdd:PRK14267 96 PFPhLTIYDNVAIGVK--LNGLVKSKKELDERVEWALKkaaLWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 547 DEATSALDAESERVVQEALDRIMVNRTTVVVAHR-LSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
384-612 |
1.12e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.39 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYpARPDEQIFR----GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKW-I 458
Cdd:PRK13633 5 IKCKNVSYKY-ESNEESTEKlaldDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 459 RSKIGLVSQEP--VLFTASIKDNIAYGKED--ATTEEIKAAAELA----NASKFVDKLPQgldtmvgehgtQLSGGQKQR 530
Cdd:PRK13633 84 RNKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 531 IAVARAILKDPRILLLDEATSALDAESERvvqEALDRIM-VNR----TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHT 605
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRR---EVVNTIKeLNKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*..
gi 15226477 606 ELLKDPE 612
Cdd:PRK13633 230 EIFKEVE 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
385-556 |
1.15e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.55 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA---GDVLIDGINLKEFQLKwiRSK 461
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFT-ASIKDNIAYG-KEDATTEEIKAAAE--LANAskfvdklpqGLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFAlPPTIGRAQRRARVEqaLEEA---------GLAGFADRDPATLSGGQRARVALLRAL 148
|
170
....*....|....*....
gi 15226477 538 LKDPRILLLDEATSALDAE 556
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAA 167
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
384-602 |
1.32e-22 |
|
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: 97.44 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTY-PARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwIRSKI 462
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEPVLFT-ASIKDNIAY-----G-KEDATTEEIKAAAELANASKFVDKLPQGLDTmvgehgtqlsgGQKQRIAVAR 535
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYfaglyGlKGDELTARLEELADRLGMEELLDRRVGGFST-----------GMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKG 602
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1042-1261 |
1.45e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.69 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL-------RLK 1114
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWspaelarRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WLRQQTGLVSqePILFNETIRANIAYGKGGDASESEIVSSA-ELSNAHGFisglqqgydtmvGERGI-QLSGGQKQRVAI 1192
Cdd:PRK13548 80 VLPQHSSLSF--PFTVEEVVAMGRAPHGLSRAEDDALVAAAlAQVDLAHL------------AGRDYpQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1193 ARAIV------KDPKVLLLDEATSALD-AESERVVQDALDRVMVNRTT-IVVAHRLstikN-----ADVIAVVKNGVIVE 1259
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAvIVVLHDL----NlaaryADRIVLLHQGRLVA 221
|
..
gi 15226477 1260 KG 1261
Cdd:PRK13548 222 DG 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
384-594 |
1.49e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLFTASIKDNIA--YGKEDATTEEIKAAAELAnasKFvdKLPqglDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLE---RF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVV--VAHRLSTVRNADmiAVIH 594
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHAD--KVIT 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1042-1266 |
1.72e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDG--VEIKSLrlkwlrQQ 1119
Cdd:PRK11432 7 VVLKNITKRFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHRSI------QQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TG--LVSQEPILF-NETIRANIAYG-KGGDASESEI---VSSA-ELSNAHGFisglqqgydtmvGERGI-QLSGGQKQRV 1190
Cdd:PRK11432 78 RDicMVFQSYALFpHMSLGENVGYGlKMLGVPKEERkqrVKEAlELVDLAGF------------EDRYVdQISGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKGKHDTL 1266
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQqqFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
384-608 |
1.77e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTY---PARpdeqifrgFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRS 460
Cdd:PRK10771 2 LKLTDITWLYhhlPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFT-ASIKDNIAYGKE------DATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAV 533
Cdd:PRK10771 72 PVSMLFQENNLFShLTVAQNIGLGLNpglklnAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1014-1268 |
1.77e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.29 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1014 SIFAIMDRESKIDPSVEsgrvldnvkgdIELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRF 1093
Cdd:PRK13536 25 GISEAKASIPGSMSTVA-----------IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1094 YDPDSGEITLDGVEIKSlRLKWLRQQTGLVSQEPILFNE-TIRAN-IAYGK--GGDASESEIVSSAELSNAHgfisgLQQ 1169
Cdd:PRK13536 91 TSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEfTVRENlLVFGRyfGMSTREIEAVIPSLLEFAR-----LES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1170 GYDTMVGErgiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVV-------AHRLst 1242
Cdd:PRK13536 165 KADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-- 238
|
250 260
....*....|....*....|....*.
gi 15226477 1243 iknADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK13536 239 ---CDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-611 |
1.94e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPArpdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQaGDVLIDG--------INLKEFQL 455
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 456 KWIRSKIGLVSQEPVLFTASIKDNIAYGKE----------DATTEEIKAAAELANASKfvdklpqgldTMVGEHGTQLSG 525
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpkleiDDIVESALKDADLWDEIK----------HKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALD--RIMVNRTTVVVAHRLSTV-RNADMIAVIHQ-----GK 597
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQ 233
|
250
....*....|....
gi 15226477 598 IVEKGSHTELLKDP 611
Cdd:PRK14258 234 LVEFGLTKKIFNSP 247
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1042-1268 |
2.04e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL-------RLK 1114
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpsrelakRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WLRQQTGLVSQepiLfneTIRANIAYG-----KG-GDASESEIVSSA----ELSN-AHGFISglqqgydtmvgergiQLS 1183
Cdd:COG4604 79 ILRQENHINSR---L---TVRELVAFGrfpysKGrLTAEDREIIDEAiaylDLEDlADRYLD---------------ELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1184 GGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvMV---NRTTIVVAHRLstikN-----ADVIAVVKNG 1255
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRR-LAdelGKTVVIVLHDI----NfascyADHIVAMKDG 212
|
250
....*....|...
gi 15226477 1256 VIVEKGKHDTLIN 1268
Cdd:COG4604 213 RVVAQGTPEEIIT 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1042-1261 |
2.15e-22 |
|
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: 97.05 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKY-PARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwLRQQT 1120
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFNE-TIRANIAY-----GKGGDASESEIVSSAELSNAHGFISglqqgydtmvgERGIQLSGGQKQRVAIAR 1194
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfaglyGLKGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1045-1259 |
2.20e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.22 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1045 RHVSFKYP------ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKW 1115
Cdd:PRK10419 7 SGLSHHYAhgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 LRQQTGLVSQEPI-LFN--ETIRANIA----YGKGGDASESEiVSSAELSNAHGFISGLQQgydtmvgERGIQLSGGQKQ 1188
Cdd:PRK10419 87 FRRDIQMVFQDSIsAVNprKTVREIIReplrHLLSLDKAERL-ARASEMLRAVDLDDSVLD-------KRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1189 RVAIARAIVKDPKVLLLDEATSALDaeseRVVQ----DALDRVMVNRTT--IVVAHRLSTIKN-ADVIAVVKNGVIVE 1259
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLD----LVLQagviRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
100-328 |
2.24e-22 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 98.92 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 100 DKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMG 179
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD-TVKTGDITSRLTSDTTTMSDTVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 180 EKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASF 259
Cdd:cd18784 112 LNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSF 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 260 TGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVLNIII 328
Cdd:cd18784 192 ANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFIL 260
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
386-598 |
2.26e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.21 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 386 LKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlkwIRSKIGLV 465
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 466 SQEPVLFT-ASIKDNIAYG-KEDATTEEIKAAAELanaskfvdklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGlKGQWRDAALQALAAV------------GLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKI 598
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1044-1216 |
2.99e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1044 LRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDgveiKSLRLKWLRQQTGLV 1123
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1124 SQEPIL------FNETIRA----NIAYGKGGDASEsEIVSSAEL-------------SNAHGFISGL---QQGYDTMVGE 1177
Cdd:COG0488 74 DDLTVLdtvldgDAELRALeaelEELEAKLAEPDE-DLERLAELqeefealggweaeARAEEILSGLgfpEEDLDRPVSE 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 15226477 1178 rgiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES 1216
Cdd:COG0488 153 ----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1059-1261 |
3.44e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1059 IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPiLFNE--TIRA 1136
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHH-LTPEgiTVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1137 NIAYGKG------GDASES--EIVSSAelsnahgfisgLQQ-GYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDE 1207
Cdd:PRK11231 96 LVAYGRSpwlslwGRLSAEdnARVNQA-----------MEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1208 ATSALDAeSERVVQDALDRVMVN--RTTIVVAHRLS-TIKNADVIAVVKNGVIVEKG 1261
Cdd:PRK11231 165 PTTYLDI-NHQVELMRLMRELNTqgKTVVTVLHDLNqASRYCDHLVVLANGHVMAQG 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1060-1235 |
3.62e-22 |
|
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: 96.73 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1060 FQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLD----GVEIKSL---RLKWLRQQT-GLVSQ------ 1125
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQAsprEILALRRRTiGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1126 ---------EPILfnetiraniayGKGGDASESEIVSSAELS--NahgfisglqqgydtmVGERGIQL-----SGGQKQR 1189
Cdd:COG4778 107 rvsaldvvaEPLL-----------ERGVDREEARARARELLArlN---------------LPERLWDLppatfSGGEQQR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIV 1235
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1042-1261 |
3.62e-22 |
|
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: 96.13 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWlrQQTG 1121
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANI-AYGKGGDASESEIVSSAElsnahgfISGLQQGYDTMVGergiQLSGGQKQRVAIARAIVKD 1199
Cdd:cd03268 76 ALIEAPGFYPNlTARENLrLLARLLGIRKKRIDEVLD-------VVGLKDSAKKKVK----GFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1200 PKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KNADVIAVVKNGVIVEKG 1261
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1055-1255 |
3.74e-22 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. 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: 213257 [Multi-domain] Cd Length: 218 Bit Score: 96.25 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1055 PDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEI----TLDGVEIKSLRLKWLRQQTGLVSQEPILF 1130
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1131 NETIRANIAYGKGGDASESEIVSSAelSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1210
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDA--CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226477 1211 ALDAE-SERVVQDALDRVMVN--RTTIVVAHRLSTIKNADVIAVVKNG 1255
Cdd:cd03290 170 ALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
384-599 |
4.21e-22 |
|
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: 94.42 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPArpdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwirskig 463
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 lvsqEPVLFtASIKDNIAYGKEdatteeikaaaelanaskfvdklpqgldtMVgehgTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03216 62 ----KEVSF-ASPRDARRAGIA-----------------------------MV----YQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 544 LLLDEATSAL-DAESERVVqEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIV 599
Cdd:cd03216 104 LILDEPTAALtPAEVERLF-KVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1042-1227 |
4.43e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRlkwlrQQTG 1121
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQ-EPILFNETIRANIAYG---KGGDASESEIVSSAELSNAhgfisGLQqGYdtmvGERGI-QLSGGQKQRVAIARAI 1196
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGlqlAGVEKMQRLEIAHQMLKKV-----GLE-GA----EKRYIwQLSGGQRQRVGIARAL 143
|
170 180 190
....*....|....*....|....*....|.
gi 15226477 1197 VKDPKVLLLDEATSALDAESERVVQDALDRV 1227
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1074-1216 |
4.56e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 99.40 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1074 ALVGESGSGKSTV---IALLQRfydPDSGEITLDG-VEIKSLRLKWL---RQQTGLVSQEPILFNE-TIRANIAYG-KGG 1144
Cdd:COG4148 29 ALFGPSGSGKTTLlraIAGLER---PDSGRIRLGGeVLQDSARGIFLpphRRRIGYVFQEARLFPHlSVRGNLLYGrKRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1145 DASES-----EIVssaelsnahgfisglqqgydTMVG-----ERGI-QLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1213
Cdd:COG4148 106 PRAERrisfdEVV--------------------ELLGighllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
...
gi 15226477 1214 AES 1216
Cdd:COG4148 166 LAR 168
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1062-1276 |
7.44e-22 |
|
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: 98.65 E-value: 7.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1062 DLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWL----RQQTGLVSQEPILFNE-TIRA 1136
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1137 NIAYGKGGDASESEIVSSAELsnahgfISGLqqGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES 1216
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERV------IELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1217 ERVVQDALDRVM--VNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTLINIKDGVYAS 1276
Cdd:TIGR02142 167 KYEILPYLERLHaeFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1042-1268 |
8.78e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.42 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKY---PARPDvqifqdlcLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEikslrlkwlrQ 1118
Cdd:PRK10771 2 LKLTDITWLYhhlPMRFD--------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----------H 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEP--ILFNE-------TIRANIAYG-----KGGDASESEIVSSAElsnahgfisglQQGYDTMVGERGIQLSG 1184
Cdd:PRK10771 64 TTTPPSRRPvsMLFQEnnlfshlTVAQNIGLGlnpglKLNAAQREKLHAIAR-----------QMGIEDLLARLPGQLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1185 GQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLStikNADVIA----VVKNGVIV 1258
Cdd:PRK10771 133 GQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLE---DAARIAprslVVADGRIA 209
|
250
....*....|
gi 15226477 1259 EKGKHDTLIN 1268
Cdd:PRK10771 210 WDGPTDELLS 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
386-643 |
9.08e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 386 LKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwiRSKIGLV 465
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 466 SQEPVLF-TASIKDNI----------------AYGKEDATTEEIKAAAEL-------------ANASKFVDKL---PQGL 512
Cdd:COG0488 67 PQEPPLDdDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELqeefealggweaeARAEEILSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 513 DTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAEServvQEALDRIMVNR--TTVVVAH-R--LSTVrnA 587
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYpgTVLVVSHdRyfLDRV--A 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 588 DMIAVIHQGKivekgshtelLKDPEGAYS------QLIRLQEEKksdENAAEEQKMSSIESF 643
Cdd:COG0488 217 TRILELDRGK----------LTLYPGNYSayleqrAERLEQEAA---AYAKQQKKIAKEEEF 265
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1061-1268 |
1.48e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.57 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQ----QTGLVSQE-PILFNETIR 1135
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSfALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1136 ANIAYGKggdasesEIVSSAELSNAHGFISGLQQ-GYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDA 1214
Cdd:PRK10070 125 DNTAFGM-------ELAGINAEERREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1215 ESERVVQDALDRVMV--NRTTIVVAHRL-STIKNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK10070 198 LIRTEMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
384-600 |
1.57e-21 |
|
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: 94.81 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI---ERfydPQAGDVLIDGINLkeFQL---- 455
Cdd:COG4181 9 IELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDL--FALdeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 456 --KWIRSKIGLVSQE----PVLfTAsiKDNIAY-----GKEDATTeeiKAAAELANAskfvdklpqGLDTMVGEHGTQLS 524
Cdd:COG4181 84 raRLRARHVGFVFQSfqllPTL-TA--LENVMLplelaGRRDARA---RARALLERV---------GLGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 525 GGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRimVNR---TT-VVVAHRLSTVRNADMIAVIHQGKIVE 600
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE--LNRergTTlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1040-1261 |
1.74e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.23 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYPARP--DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI-----KSLR 1112
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1113 LKWLRQQTGLVSQEP--ILFNETIRANIAYGK---GGDASES-----EIVSSAELSNAHgfisglqqgydtmVGERGIQL 1182
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPvnlGENKQEAykkvpELLKLVQLPEDY-------------VKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1183 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN--RTTIVVAHRLSTI-KNADVIAVVKNGVIVE 1259
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
|
..
gi 15226477 1260 KG 1261
Cdd:PRK13645 232 IG 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1042-1261 |
1.82e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.57 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLkW------ 1115
Cdd:COG4559 2 LEAENLSVRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSP-Welarrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 --LRQQTGLVsqepilFNETIRANIAYGK----GGDASESEIVSSA-ELSNAHGFisglqqgydtmvGERGIQ-LSGGQK 1187
Cdd:COG4559 78 avLPQHSSLA------FPFTVEEVVALGRaphgSSAAQDRQIVREAlALVGLAHL------------AGRSYQtLSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1188 QRVAIARAIV-------KDPKVLLLDEATSALD-AESERVVQdaLDRVMVNRTTIVVA--HRLstikN-----ADVIAVV 1252
Cdd:COG4559 140 QRVQLARVLAqlwepvdGGPRWLFLDEPTSALDlAHQHAVLR--LARQLARRGGGVVAvlHDL----NlaaqyADRILLL 213
|
....*....
gi 15226477 1253 KNGVIVEKG 1261
Cdd:COG4559 214 HQGRLVAQG 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1042-1268 |
1.91e-21 |
|
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: 94.42 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRL-KWLRQQT 1120
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFNE-TIRANI---AYGKGGDASESEIvssAELsnahgfisglqqgYD------TMVGERGIQLSGGQKQRV 1190
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLllgAYARRRAKRKARL---ERV-------------YElfprlkERRKQLAGTLSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALdaeSERVVQDALDRVM-VNR--TTIVV----AHRLSTIknADVIAVVKNGVIVEKGKH 1263
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGL---APKIVEEIFEAIReLRDegVTILLveqnARFALEI--ADRAYVLERGRVVLEGTA 216
|
....*
gi 15226477 1264 DTLIN 1268
Cdd:cd03224 217 AELLA 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1040-1243 |
2.07e-21 |
|
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: 95.69 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYPARPDVqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDsGEITLDGVEIKSLRLKWLRQQ 1119
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILFNETIRANI-AYGKGGDaseSEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVK 1198
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTI 1243
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAM 200
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
384-612 |
2.93e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVN--RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1061-1259 |
3.43e-21 |
|
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: 94.04 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwLRQQTGLVS--QEPILFNE-TIRAN 1137
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1138 I-----AYGKGGDASESEIVSSAELSN-AHGFIS--GLQQGYDTMVGErgiqLSGGQKQRVAIARAIVKDPKVLLLDEAT 1209
Cdd:cd03219 96 VmvaaqARTGSGLLLARARREEREARErAEELLErvGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1210 SAL-DAESERVVqDALDRVMV-NRTTIVVAHRLSTIKN-ADVIAVVKNG-VIVE 1259
Cdd:cd03219 172 AGLnPEETEELA-ELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGrVIAE 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
63-331 |
4.01e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 95.18 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQtnttdkvSKVALKFVWLGI-GTFA----AAFLQ--LSGWMisGERQA 135
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEK-------DLEALLLVPLAIiGLFLlrglASYLQtyLMAYV--GQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 136 ARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIP 215
Cdd:cd18552 72 RDLRNDLFDKLLRLPLSFFD-RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 216 LLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGV-IEGGSTGLGLGTL 294
Cdd:cd18552 151 LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMkIARARALSSPLME 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 15226477 295 FLVVFCSyALAVWYGGKLILDKGYTGGQVLNIIIAVL 331
Cdd:cd18552 231 LLGAIAI-ALVLWYGGYQVISGELTPGEFISFITALL 266
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-610 |
4.93e-21 |
|
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: 100.37 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQaGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNI 480
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 481 AyGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERV 560
Cdd:TIGR01271 1313 D-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQI 1391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 561 VQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:TIGR01271 1392 IRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1042-1259 |
5.29e-21 |
|
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: 94.10 E-value: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYP------ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR--- 1112
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1113 LKWLRQQTGLVSQE-PILFN--ETIRANIA----YGKGGDASESEiVSSAELSNAHGFISGLQQGYDTmvgergiQLSGG 1185
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNprMTVRQIIGeplrHLTSLDESEQK-ARIAELLDMVGLRSEDADKLPR-------QLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1186 QKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTT--IVVAHRLSTIKN-ADVIAVVKNGVIVE 1259
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
384-610 |
5.57e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQlKWIRSKI- 462
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELARRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEPVL-FTASIKDNIAYGKEDATTEEIKAAAELANASKFVDklpqgLDTMVGEHGTQLSGGQKQRIAVARAIL--- 538
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVD-----LAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 539 ---KDPRILLLDEATSALD-AESERVVQEALDRIMVNRTTV-VVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAViVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
401-607 |
5.81e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 94.54 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwirsKIGLVSQEPVLFTASIKDNI 480
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 481 AYG---KEDATTEEIKAAAELANASKFVDKLpqglDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 557
Cdd:cd03291 119 IFGvsyDEYRYKSVVKACQLEEDITKFPEKD----NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15226477 558 ERVVQEA-LDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1042-1261 |
6.36e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.92 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSfKYPARpdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwlRQQTG 1121
Cdd:PRK10851 3 IEIANIK-KSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANIAYGkggdaseSEIVSSAELSNAHGFISGLQQGYDtMV-----GER-GIQLSGGQKQRVAIAR 1194
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFG-------LTVLPRRERPNAAAIKAKVTQLLE-MVqlahlADRyPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1195 AIVKDPKVLLLDEATSALDAEservVQDALDRVM------VNRTTIVVAH-RLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQ----VRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1051-1247 |
8.41e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1051 YPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveikSLRLKWLRQQTGLVSQEPIlf 1130
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1131 neTIRANIAYGKGG--------DASESEIVSSA-ELSNAHGFiSGLQqgydtmVGErgiqLSGGQKQRVAIARAIVKDPK 1201
Cdd:NF040873 73 --TVRDLVAMGRWArrglwrrlTRDDRAAVDDAlERVGLADL-AGRQ------LGE----LSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDR-VMVNRTTIVVAHRLSTIKNAD 1247
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRAD 186
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1061-1255 |
8.70e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 92.53 E-value: 8.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIkslrlkwlrQQTG----LVSQEPILFN-ETIR 1135
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---------TEPGpdrmVVFQNYSLLPwLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1136 ANIAYGKGG---DASESEivsSAELSNAHGFISGLQQGYDtmvgERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1212
Cdd:TIGR01184 73 ENIALAVDRvlpDLSKSE---RRAIVEEHIALVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15226477 1213 DAESERVVQDALDRVMVNR--TTIVVAHRL-STIKNADVIAVVKNG 1255
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
402-576 |
9.75e-21 |
|
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: 92.50 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLID----GINL---KEFQLKWIRSK-IGLVSQ------ 467
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLaqaSPREILALRRRtIGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 468 ---------EPVLftasikdniAYGKEDATTEEiKAAAELA--NaskfvdkLPQGLdtmvgehgTQL-----SGGQKQRI 531
Cdd:COG4778 107 rvsaldvvaEPLL---------ERGVDREEARA-RARELLArlN-------LPERL--------WDLppatfSGGEQQRV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226477 532 AVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV 576
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1024-1259 |
1.08e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1024 KIDPSVESGRVLdnvkgdIELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITL 1103
Cdd:COG0488 304 RFPPPERLGKKV------LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1104 -DGVEIkslrlkwlrqqtGLVSQEPILFNE--TIRANIAYGkGGDASESEIVSSAElsnAHGFiSGLQQgyDTMVGErgi 1180
Cdd:COG0488 375 gETVKI------------GYFDQHQEELDPdkTVLDELRDG-APGGTEQEVRGYLG---RFLF-SGDDA--FKPVGV--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1181 qLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDR----VmvnrttIVVAH-R--LSTIknADVIAVVK 1253
Cdd:COG0488 433 -LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV--ATRILEFE 503
|
....*.
gi 15226477 1254 NGVIVE 1259
Cdd:COG0488 504 DGGVRE 509
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
403-621 |
1.10e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKWIR----SKIGLVSQEPVLF-TASIK 477
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRdaqaAGIAIIHQELNLVpNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 478 DNIAYGKEDATTEEIKAAAELANASKFVDKLpqGLD----TMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:COG1129 98 ENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 554 -DAESER---VVQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDpegaysQLIRL 621
Cdd:COG1129 172 tEREVERlfrIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTED------ELVRL 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1042-1268 |
1.31e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.98 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVS--FKYPA----RPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIK----SL 1111
Cdd:COG4167 5 LEVRNLSktFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygdyKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1112 RLKWLR-------------QQTGLVSQEPILFNETIRANiaygkggdASESEIVSSAE---LSNAHGFIsglqqgYDTMv 1175
Cdd:COG4167 85 RCKHIRmifqdpntslnprLNIGQILEEPLRLNTDLTAE--------EREERIFATLRlvgLLPEHANF------YPHM- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1176 gergiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAeSERvVQdaldrvMVNR----------TTIVVAHRLSTIKN 1245
Cdd:COG4167 150 ------LSSGQKQRVALARALILQPKIIIADEALAALDM-SVR-SQ------IINLmlelqeklgiSYIYVSQHLGIVKH 215
|
250 260
....*....|....*....|....
gi 15226477 1246 -ADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:COG4167 216 iSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1074-1262 |
1.50e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1074 ALVGESGSGKSTVIALLQRFYD--PD---SGEITLDGVEIKSLRLKW--LRQQTGLVSQEPILFNETIRANIAYG---KG 1143
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPMSIYENVVYGlrlKG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1144 -GDASESEIVSSAELSNAHGFISGLQQGYDTMVGergiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQD 1222
Cdd:PRK14239 115 iKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15226477 1223 ALDRVMVNRTTIVVAHRL---STIknADVIAVVKNGVIVEKGK 1262
Cdd:PRK14239 190 TLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYND 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-614 |
1.63e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 399 EQIFRGFSlfisSGTTVALVGQSGSGKSTVVSLIERFYDP-----QAGDVLIDGINLKEFQ-LKWIRSKIGLVSQEPVLF 472
Cdd:PRK14271 38 DQVSMGFP----ARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 473 TASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 553 LDAESERVVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDPEGA 614
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1042-1261 |
1.79e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEP--ILFNETIRANIAYG--KGGDASESEIVSSAELSNAHGFISglqqgYDTMVGERgiqLSGGQKQRVAIARAIV 1197
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGmeNQGIPREEMIKRVDEALLAVNMLD-----FKTREPAR---LSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1198 KDPKVLLLDEATSALD----AESERVVQDALDRVMVnrTTIVVAHRLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
393-588 |
2.10e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 393 YPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwiRSKIGLVSQ---EP 469
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 470 VLFTASIKDNIAYG------------KED-ATTEEIKAA---AELANASkfvdklpqgLDTmvgehgtqLSGGQKQRIAV 533
Cdd:NF040873 68 DSLPLTVRDLVAMGrwarrglwrrltRDDrAAVDDALERvglADLAGRQ---------LGE--------LSGGQRQRALL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVVVAHRLSTVRNAD 588
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRAD 186
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
384-568 |
2.12e-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: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPA-RPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlKWIR--- 459
Cdd:COG4525 4 LTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG--------VPVTgpg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 460 SKIGLVSQEPVLFT-ASIKDNIAYGKEDATteeIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:COG4525 76 ADRGVVFQKDALLPwLNVLDNVAFGLRLRG---VPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190
....*....|....*....|....*....|
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRI 568
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1042-1240 |
2.52e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVS--FkYPARPD-VQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL----RLK 1114
Cdd:COG1101 2 LELKNLSktF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeykRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WLrqqtGLVSQEPIL---FNETIRAN--IAYGKGGDASESEIVSSAELSNAHGFISGLQQGY----DTMVGergiQLSGG 1185
Cdd:COG1101 81 YI----GRVFQDPMMgtaPSMTIEENlaLAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLenrlDTKVG----LLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1186 QKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVmVNR---TTIVVAHRL 1240
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNM 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
400-617 |
2.88e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKS-TVVSLIERFYDPQA----GDVLIDGINL---KEFQLKWIR-SKIGLVSQEPV 470
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 LFTA---SIKDNIA--------YGKEDATTEEIKAAAELA--NASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAI 537
Cdd:PRK15134 103 VSLNplhTLEKQLYevlslhrgMRREAARGEILNCLDRVGirQAAKRLTDYPH-----------QLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 538 LKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGA 614
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQqeLNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHP 251
|
...
gi 15226477 615 YSQ 617
Cdd:PRK15134 252 YTQ 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
398-608 |
3.88e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTA-SI 476
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 477 KDNIAYGKE----------DATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLL 546
Cdd:PRK11231 94 RELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLADRRL-----------TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 547 DEATSALDAeSERVVQEALDRIMVN--RTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK11231 163 DEPTTYLDI-NHQVELMRLMRELNTqgKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
384-610 |
4.22e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.10 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTY-PARPdeqiFRGFSLF-----ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KEF 453
Cdd:PRK13643 2 IKFEKVNYTYqPNSP----FASRALFdidleVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 454 QLKWIRSKIGLVSQEP--VLFTASIKDNIAYGKED---ATTEEIKAAAE----LANASKFVDKLPqgldtmvgehgTQLS 524
Cdd:PRK13643 78 EIKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgiPKEKAEKIAAEklemVGLADEFWEKSP-----------FELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 525 GGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
....*...
gi 15226477 603 SHTELLKD 610
Cdd:PRK13643 227 TPSDVFQE 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
375-612 |
4.87e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.61 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 375 KVLDDIKGDI--ELKDVYFTYPARPDEQI--FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGI-- 448
Cdd:PRK13631 11 KVPNPLSDDIilRVKNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 449 ----------------NLKEFqlKWIRSKIGLVSQEP--VLFTASIKDNIAYGKEDATTEEIKAAAElanASKFVDKLpq 510
Cdd:PRK13631 91 gdkknnhelitnpyskKIKNF--KELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKL---AKFYLNKM-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 511 GLD-TMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER-VVQEALDRIMVNRTTVVVAHRLSTVRN-A 587
Cdd:PRK13631 164 GLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvA 243
|
250 260
....*....|....*....|....*
gi 15226477 588 DMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
405-624 |
6.19e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.05 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 405 FSLfiSSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLkwiRSK-IGLVSQEPvlfTASIKDNIA 481
Cdd:COG4167 34 FTL--EAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkLEYGDYKY---RCKhIRMIFQDP---NTSLNPRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 482 YGKedaTTEE-IKAAAELaNASKFVDKLPQGLdTMVG---EHGT----QLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:COG4167 106 IGQ---ILEEpLRLNTDL-TAEEREERIFATL-RLVGllpEHANfyphMLSSGQKQRVALARALILQPKIIIADEALAAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 554 DAeSERV--------VQEALdrimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAYSQliRLQEE 624
Cdd:COG4167 181 DM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANPQHEVTK--RLIES 252
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
403-612 |
6.34e-20 |
|
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: 90.87 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKE--------------FQLkwIRS-------- 460
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphriarlgiartFQN--PRLfpeltvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 --KIGLVSQEPVLFTASIKDNIAYGKEDATTEEikAAAELAnasKFVdklpqGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:COG0411 99 nvLVAAHARLGRGLLAALLRLPRARREEREARE--RAEELL---ERV-----GLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 539 KDPRILLLDEATSAL-DAESERVVqEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:COG0411 169 TEPKLLLLDEPAAGLnPEETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1056-1261 |
8.03e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1056 DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPIL-FNETI 1134
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1135 RANIAYGK--------GGDASESEIVSSAelsnahgfisgLQQGYDTMVGERGI-QLSGGQKQRVAIARAIVKDPKVLLL 1205
Cdd:PRK09536 95 RQVVEMGRtphrsrfdTWTETDRAAVERA-----------MERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1206 DEATSALDAESE-RVVQDALDRVMVNRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKG 1261
Cdd:PRK09536 164 DEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1053-1261 |
8.17e-20 |
|
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: 89.64 E-value: 8.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1053 ARPDVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRFYDPDSGEITLDGVEIKslRLKWlRQQTGLVSQEPIL 1129
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRK--PDQF-QKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1130 FNE-TIRANIAYGK----GGDASESEIVSSAElsnahgfISGLQQGYDTMVGERGIQ-LSGGQKQRVAIARAIVKDPKVL 1203
Cdd:cd03234 93 LPGlTVRETLTYTAilrlPRKSSDAIRKKRVE-------DVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1204 LLDEATSALDAEServvqdALDRVMV-------NRTTIVVAH--RLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03234 166 ILDEPTSGLDSFT------ALNLVSTlsqlarrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
721-977 |
1.05e-19 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 90.95 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 721 ILGSISAAANGVILP-IFGILISSVIKAFFQppkklkedTSFWAIIFMVLGFA---SIIAYpAQTFFFAIAGCKLVQRIR 796
Cdd:cd18542 5 ILALLLATALNLLIPlLIRRIIDSVIGGGLR--------ELLWLLALLILGVAllrGVFRY-LQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 797 SMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIA 876
Cdd:cd18542 76 NDLYDHLQRLSFSFHDK--ARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 877 LNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVL 956
Cdd:cd18542 154 LFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLS 233
|
250 260
....*....|....*....|.
gi 15226477 957 FSSYAASFYVGARLVDDGKTT 977
Cdd:cd18542 234 GLQIVLVLWVGGYLVINGEIT 254
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1042-1268 |
1.52e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL-RLKWLRQQT 1120
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEP--ILFNETIRANIAYGkggdaSESEIVSSAELsnahgfisglQQGYDTMVGERGIQ---------LSGGQKQR 1189
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFG-----PENLCLPPIEI----------RKRVDRALAEIGLEkyrhrspktLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIV-VAHRLSTIKNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1056-1266 |
1.57e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.72 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1056 DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGV------EIKSLRLKWLRQQTGLVSQEPIL 1129
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1130 FNE-TIRANIAY--GKGGDASESEIVSSAELSNAHgfiSGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLD 1206
Cdd:PRK14246 102 FPHlSIYDNIAYplKSHGIKEKREIKKIVEECLRK---VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 1207 EATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGKHDTL 1266
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1044-1262 |
2.07e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1044 LRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEItLDGveikSLRLKWLRQQTGLV 1123
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1124 SQEPILFN-ETIRANIAYGKGGD----ASES-EIVSSAELSNahgfisglqqgydtmvgERGIQLSGGQKQRVAIARAIV 1197
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKGQwrdaALQAlAAVGLADRAN-----------------EWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1198 KDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRLStiknaDVIAVVKNGVIVEKGK 1262
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVS-----EAVAMADRVLLIEEGK 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1040-1256 |
2.12e-19 |
|
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: 94.98 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveikslrlkwlrqQ 1119
Cdd:TIGR01271 425 GDDGLFFSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------R 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILFNETIRANIAYGKGGDASE-SEIVSSAELSNAhgfISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVK 1198
Cdd:TIGR01271 489 ISFSPQTSWIMPGTIKDNIIFGLSYDEYRyTSVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISLARAVYK 565
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1199 DPKVLLLDEATSALDAESER-VVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGV 1256
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1061-1240 |
2.39e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYD-----PDSGEITLDGVEIKSLRLK--WLRQQTGLVSQEPILFNET 1133
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1134 IRANIAYG---KGGDASESEIVSSAelsnahgfisgLQQG--YDTM---VGERGIQLSGGQKQRVAIARAIVKDPKVLLL 1205
Cdd:PRK14243 107 IYDNIAYGariNGYKGDMDELVERS-----------LRQAalWDEVkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190
....*....|....*....|....*....|....*
gi 15226477 1206 DEATSALDAESERVVQDALDRVMVNRTTIVVAHRL 1240
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1270 |
2.40e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARP--DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEI------------------ 1101
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1102 TLDGVEIKSLR------LKWLRQQTGLVSQ--EPILFNETIRANIAYGkggdaSESEIVSSAE-LSNAHGFIS--GLQQG 1170
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG-----PVSMGVSKEEaKKRAAKYIElvGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1171 YdtmVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN-RTTIVVAHRL-STIKNADV 1248
Cdd:PRK13651 158 Y---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKR 234
|
250 260
....*....|....*....|...
gi 15226477 1249 IAVVKNGVIVEKGK-HDTLINIK 1270
Cdd:PRK13651 235 TIFFKDGKIIKDGDtYDILSDNK 257
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1059-1255 |
2.51e-19 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 89.92 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1059 IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveikslrlkwlrqQTGLVSQEPILFNETIRANI 1138
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1139 AYGKGGDASE-SEIVSSAELSNAhgfISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE 1217
Cdd:cd03291 119 IFGVSYDEYRyKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 15226477 1218 R-VVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNG 1255
Cdd:cd03291 196 KeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
388-612 |
2.61e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 388 DVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLKWIRSKIGLV 465
Cdd:PRK13638 6 DLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 466 SQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQGLdtmvgehgtqlSGGQKQRIAVARAI 537
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSlrnlgvPEAEITRRVDEALTLVDAQHFRHQPIQCL-----------SHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVV-AHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1042-1268 |
2.78e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.33 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDsGEITLDG-VEI-------KSLRL 1113
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrVEFfnqniyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1114 KWLRQQTGLVSQEPILFNETIRANIAYGKG--GDASESE---IVSSAeLSNAHgfisgLQQGYDTMVGERGIQLSGGQKQ 1188
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivGWRPKLEiddIVESA-LKDAD-----LWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1189 RVAIARAIVKDPKVLLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKN-ADVIAVVKN-----GVIVEK 1260
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEF 237
|
....*...
gi 15226477 1261 GKHDTLIN 1268
Cdd:PRK14258 238 GLTKKIFN 245
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
717-974 |
3.13e-19 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 89.41 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 717 IPVLILGSISAAAnGVILPIFgilISSVIKAFFqppkklKEDTSFWAIIFMVLGF-ASIIAYPAQTFFFAIAGCKLVQRI 795
Cdd:cd18551 2 ILALLLSLLGTAA-SLAQPLL---VKNLIDALS------AGGSSGGLLALLVALFlLQAVLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 796 RSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLI 875
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 876 ALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFV 955
Cdd:cd18551 150 FLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLA 229
|
250
....*....|....*....
gi 15226477 956 LFSSYAASFYVGARLVDDG 974
Cdd:cd18551 230 VQLALLVVLGVGGARVASG 248
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1056-1261 |
3.36e-19 |
|
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: 87.34 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1056 DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL---RLKWLRQQTGLVSqepilfNE 1132
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAarnRIGYLPEERGLYP------KM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1133 TIRANIAY-GKGGDASESEIVSSAE--LSNAHgfISGLQQgydtmvgERGIQLSGGQKQRVAIARAIVKDPKVLLLDEAT 1209
Cdd:cd03269 86 KVIDQLVYlAQLKGLKKEEARRRIDewLERLE--LSEYAN-------KRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1210 SALDAESERVVQDALDRVMVNRTTIV-VAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1061-1259 |
3.52e-19 |
|
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: 88.56 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLkWLRQQTGLVS--QEPILFNE-TIRAN 1137
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1138 IA----------------YGKGGDASESEIVSSAE--LSnahgfISGLQQGYDTMVGErgiqLSGGQKQRVAIARAIVKD 1199
Cdd:COG0411 100 VLvaaharlgrgllaallRLPRARREEREARERAEelLE-----RVGLADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1200 PKVLLLDEATSAL-DAESERVVqDALDRV--MVNRTTIVVAHRLSTIKN-ADVIAVVKNG-VIVE 1259
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
384-568 |
3.63e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGInlkefQLKWIRSKIG 463
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQ-EPVLFTASIKDNIAYGKEDATTEEikaAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQLAGVEK---MQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180
....*....|....*....|....*.
gi 15226477 543 ILLLDEATSALDAESERVVQEALDRI 568
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
719-1207 |
3.67e-19 |
|
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: 92.94 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 719 VLILGSISAAANGVILPifgiLISSVIKAFFQPPkklkeDTSFW-----AIIFMVLGFAS--IIAYPAQTFFFAIaGCKL 791
Cdd:COG4615 18 ALLLGLLSGLANAGLIA----LINQALNATGAAL-----ARLLLlfaglLVLLLLSRLASqlLLTRLGQHAVARL-RLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 792 VQRIRSMCFEKVvhMEVGwfdepensSGTIGARLSADAATIRGLVGdSLAQTVQNLSSILAGLI-IAFLAcWQLAFVVLA 870
Cdd:COG4615 88 SRRILAAPLERL--ERIG--------AARLLAALTEDVRTISQAFV-RLPELLQSVALVLGCLAyLAWLS-PPLFLLTLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 871 MLPL-IALNGFLYMKFMKGFsadakkmyGEASQVANDAVGSIRTVASFCAEDKvmnMYSKKCE-------GPMKNGIRQG 942
Cdd:COG4615 156 LLGLgVAGYRLLVRRARRHL--------RRAREAEDRLFKHFRALLEGFKELK---LNRRRRRaffdedlQPTAERYRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 943 IVSG-----IGFGFSFFVLFSSYAASFYVGARLVDDGKTTfdsVFRVFFALTMAAMAISQSSSLSPDSSKADVAAASIFA 1017
Cdd:COG4615 225 RIRAdtifaLANNWGNLLFFALIGLILFLLPALGWADPAV---LSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1018 IMDRESKIDPSVESGRVLDNVKG--DIELRHVSFKYPARPDVQIFQ----DLclSIRAGKTVALVGESGSGKSTVIALLQ 1091
Cdd:COG4615 302 LELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEGFTlgpiDL--TIRRGELVFIVGGNGSGKSTLAKLLT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1092 RFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETiraniaYGKGGDASESEIvssAELsnahgfisgLQQ-G 1170
Cdd:COG4615 380 GLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPARA---REL---------LERlE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15226477 1171 YDTMVGERG-----IQLSGGQKQRVAIARAIVKDPKVLLLDE 1207
Cdd:COG4615 442 LDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1058-1268 |
3.71e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1058 QIFQDLCLSIRAGKTVALVGESGSGKS-TVIALLQRFYDPD----SGEITLDGveiKSL------RLKWLR-QQTGLVSQ 1125
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHG---ESLlhaseqTLRGVRgNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1126 EPIL-FN--ETIRANIA------YGKGGDASESEIVSSAE---LSNAHGFISGLQQgydtmvgergiQLSGGQKQRVAIA 1193
Cdd:PRK15134 100 EPMVsLNplHTLEKQLYevlslhRGMRREAARGEILNCLDrvgIRQAAKRLTDYPH-----------QLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1194 RAIVKDPKVLLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
386-611 |
4.04e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 386 LKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLV 465
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 466 SQE-PVLFTASIKDNIA------------YGKEDatTEEIKAAAELANASKFVDKLpqgLDTmvgehgtqLSGGQKQRIA 532
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAigrypwhgalgrFGAAD--REKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
..
gi 15226477 610 DP 611
Cdd:PRK10575 238 GE 239
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
402-618 |
4.10e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.44 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDV--------LIDGINLKEFQLKWI-RSKIGLVSQEP--- 469
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAERRRLlRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 470 VLFTASIKDNIA----------YGKEDATTEEIKAAAELANASkfVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILK 539
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYGDIRATAGDWLERVEIDAAR--IDDLP-----------TTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 540 DPRILLLDEATSALDAEservVQ-EALD--RIMVNR---TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVS----VQaRLLDllRGLVRElglAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
....*.
gi 15226477 613 GAYSQL 618
Cdd:PRK11701 245 HPYTQL 250
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1049-1268 |
4.80e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1049 FKYPARpdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKS---LRLKWLRQQTGLVSQ 1125
Cdd:PRK11308 22 FKPERL--VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1126 EPilfnetiraniaYG------KGGDASESEIVSSAELSNAhgfiSGLQQGYDTM--VGERGIQ-------LSGGQKQRV 1190
Cdd:PRK11308 100 NP------------YGslnprkKVGQILEEPLLINTSLSAA----ERREKALAMMakVGLRPEHydryphmFSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALDAESERVVqdaLDRVM-----VNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHD 1264
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQV---LNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKE 240
|
....
gi 15226477 1265 TLIN 1268
Cdd:PRK11308 241 QIFN 244
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1056-1261 |
5.34e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.05 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1056 DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYD--PD---SGEITLDGVEIKSLRLKWLRQQTGLVSQEP-IL 1129
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1130 FNETIRANIAYGkggdASESEIVSS-AELSNAHGFISGLQQGYDTM---VGERGIQLSGGQKQRVAIARAIVKDPKVLLL 1205
Cdd:PRK14247 95 PNLSIFENVALG----LKLNRLVKSkKELQERVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1206 DEATSALDAESERVVQDALDRVMVNRTTIVVAH------RLStiknaDVIAVVKNGVIVEKG 1261
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
385-612 |
5.74e-19 |
|
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: 87.34 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQLkwIRSK 461
Cdd:COG0410 5 EVENLHAGYGGI---HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGediTGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTA-SIKDNI---AYGKEDAttEEIKAAAELAnaskfVDKLPQgLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLllgAYARRDR--AEVRADLERV-----YELFPR-LKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 538 LKDPRILLLDEATSALdaeSERVVQEALDRIM-VNR--TTVVV----AHRLSTVrnADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEEIFEIIRrLNRegVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLAD 226
|
..
gi 15226477 611 PE 612
Cdd:COG0410 227 PE 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
384-621 |
5.77e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLKWIRSK 461
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQGLdtmvgehgtqlSGGQKQRIAV 533
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDNALKRTGIEHLKDKPTHCL-----------SFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 534 ARAILKDPRILLLDEATSALD----AESERVVQEALDRIMVnrTTVVVAHRLSTVR-NADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGL--TIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
250
....*....|...
gi 15226477 609 KDPEGAYSQLIRL 621
Cdd:PRK13636 231 AEKEMLRKVNLRL 243
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1042-1267 |
5.89e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.09 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQifqDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSlRLKWLRQQTG 1121
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQ----EPilfNETIRANI-AYGK--GGDASESEIVSSAELSNAHgfisgLQQGYDTMVGErgiqLSGGQKQRVAIAR 1194
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLlVFGRyfGLSAAAARALVPPLLEFAK-----LENKADAKVGE----LSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVV-------AHRLstiknADVIAVVKNGVIVEKGKHDTLI 1267
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
406-602 |
6.19e-19 |
|
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: 86.50 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqLKWIRSKIGLVSQEPVLFTA-SIKDNI---- 480
Cdd:cd03268 20 SLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALIEAPGFYPNlTARENLrlla 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 481 -AYGKEDATTEEIKAAAELANASKfvDKlpqgldtmVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 559
Cdd:cd03268 98 rLLGIRKKRIDEVLDVVGLKDSAK--KK--------VK----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226477 560 VVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:cd03268 164 ELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1042-1261 |
6.36e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.64 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKY-PARP-DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL----RLKW 1115
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 LRQQTGLVSQEP--ILFNETIRANIAYGK---GGDASESEIVSSAELSnahgfISGLQQGYdtmVGERGIQLSGGQKQRV 1190
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPqnfGIPKEKAEKIAAEKLE-----MVGLADEF---WEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
384-604 |
6.61e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 6.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVL---FTasIKDN-IAYGKE-DATTEEIKAAaeLANASKFVdKLPQGLDTMVGEhgtqLSGGQKQRIAVARAIL 538
Cdd:PRK13536 118 VVPQFDNLdleFT--VRENlLVFGRYfGMSTREIEAV--IPSLLEFA-RLESKADARVSD----LSGGMKRRLTLARALI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVVVAHRLSTV-RNADMIAVIHQG-KIVEKGSH 604
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPH 257
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
383-607 |
7.61e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 383 DIELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKI 462
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEPVLFT-ASIKDNIAYGKEDATTE--EIK----AAAELANASKFVDKLPQGLdtmvgehgtqlSGGQKQRIAVAR 535
Cdd:PRK11000 78 GMVFQSYALYPhLSVAENMSFGLKLAGAKkeEINqrvnQVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 536 AILKDPRILLLDEATSALDAeSERVVQealdRIMV-------NRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDA-ALRVQM----RIEIsrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1044-1252 |
8.35e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.92 E-value: 8.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1044 LRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLK-WLRQQTGL 1122
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1123 VSQEPILFNETIRANIAYGK----GG----DASESEIVSSAelsnahgfIS--GLQQGYDTMVGergiQLSGGQKQRVAI 1192
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRypwhGAlgrfGAADREKVEEA--------ISlvGLKPLAHRLVD----SLSGGERQRAWI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1193 ARAIVKDPKVLLLDEATSALDAESERVVqdaldrvmvnrttIVVAHRLSTIKNADVIAVV 1252
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDV-------------LALVHRLSQERGLTVIAVL 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
384-602 |
1.21e-18 |
|
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: 85.80 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKwIRSKIG 463
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIA-ARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLF-TASIKDNIAY-------GKEDATTEeikaAAELANASKFVDKLPQGLDtmvgehgtQLSGGQKQRIAVAR 535
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlaqlkglKKEEARRR----IDEWLERLELSEYANKRVE--------ELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV-VAHRLSTV-RNADMIAVIHQGKIVEKG 602
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
410-627 |
1.28e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.16 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 410 SSGTTvALVGQSGSGKSTVVSLIERFYDPQAG------DVLID---GINLKEFQlkwirSKIGLVSQEPVLFTA-SIKDN 479
Cdd:PRK11144 23 AQGIT-AIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDaekGICLPPEK-----RRIGYVFQDARLFPHyKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 480 IAYGKEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 559
Cdd:PRK11144 97 LRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 560 VVQEALDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLkdpegaYSQLIR--LQEEKKS 627
Cdd:PRK11144 166 ELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVW------ASSAMRpwLPKEEQS 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1058-1268 |
1.82e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.56 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1058 QIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR-------------LKWLRQQTGLVS 1124
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvadknqLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1125 QEPILFNE-TIRANI--AYGKGGDASESEIVSSAELSNAHGFISGLQQGydtmvgERGIQLSGGQKQRVAIARAIVKDPK 1201
Cdd:PRK10619 99 QHFNLWSHmTVLENVmeAPIQVLGLSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1202 VLLLDEATSALDAEserVVQDALdRVMVN-----RTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK10619 173 VLLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
403-579 |
1.95e-18 |
|
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: 85.98 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKE--------FQ----LKWIrskiglvsqepv 470
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrmvvFQnyslLPWL------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 lftaSIKDNIAYG----KEDATTEEIKAAAE----LANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPR 542
Cdd:TIGR01184 70 ----TVRENIALAvdrvLPDLSKSERRAIVEehiaLVGLTEAADKRP-----------GQLSGGMKQRVAIARALSIRPK 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 15226477 543 ILLLDEATSALDAESERVVQEALDRIMV-NRTTVV-VAH 579
Cdd:TIGR01184 135 VLLLDEPFGALDALTRGNLQEELMQIWEeHRVTVLmVTH 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1042-1258 |
2.27e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPA-RPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGE--------ITLDGVEIKSLR 1112
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1113 lkwlRQQTGLVSQE-PILFNETIRANIAYgkggDASESEIVSSAELSNAHGFISGLqqGYDTMVGERGIQLSGGQKQRVA 1191
Cdd:PRK10535 85 ----REHFGFIFQRyHLLSHLTAAQNVEV----PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN-RTTIVVAHRLSTIKNADVIAVVKNGVIV 1258
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
371-617 |
2.38e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.84 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 371 STNGKVLDDIKG-----DIELKDVYFTYPARPDEQIfRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLI 445
Cdd:PRK15079 2 TEGKKVLLEVADlkvhfDIKDGKQWFWQPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 446 DGINL---KEFQLKWIRSKIGLVSQEPVlftAS------IKDNIA-----YgKEDATTEEIKAaaELANASKFVDKLPQg 511
Cdd:PRK15079 81 LGKDLlgmKDDEWRAVRSDIQMIFQDPL---ASlnprmtIGEIIAeplrtY-HPKLSRQEVKD--RVKAMMLKVGLLPN- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 512 ldtMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE-RVVQ--EALDRIMvNRTTVVVAHRLSTVRN-A 587
Cdd:PRK15079 154 ---LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaQVVNllQQLQREM-GLSLIFIAHDLAVVKHiS 229
|
250 260 270
....*....|....*....|....*....|
gi 15226477 588 DMIAVIHQGKIVEKGSHTELLKDPEGAYSQ 617
Cdd:PRK15079 230 DRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
384-619 |
2.41e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTypaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRS 460
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipaMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFT-ASIKDNIAYgkedATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAY----PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 540 DPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAYS 616
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPDPRVR 240
|
...
gi 15226477 617 QLI 619
Cdd:PRK11831 241 QFL 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
406-599 |
2.75e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLK----WIRSKIGLVSQEPVLF-TASIKDNI 480
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRsprdAIALGIGMVHQHFMLVpNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 481 AYGKEDA------TTEEIKAAAELANASKF-VDklpqgLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:COG3845 102 VLGLEPTkggrldRKAARARIRELSERYGLdVD-----PDAKVE----DLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15226477 554 -DAESERVVqEALDRIMVNRTTVV-VAHRLSTVR-NADMIAVIHQGKIV 599
Cdd:COG3845 173 tPQEADELF-EILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1042-1258 |
3.46e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDG--VEIKS----LRLKw 1115
Cdd:COG3845 6 LELRGITKRFG---GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaIALG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 lrqqTGLVSQEPILFNE-TIRANIAYG----KGG----DASESEIvssAELSNAHGFISGLqqgyDTMVGergiQLSGGQ 1186
Cdd:COG3845 82 ----IGMVHQHFMLVPNlTVAENIVLGleptKGGrldrKAARARI---RELSERYGLDVDP----DAKVE----DLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1187 KQRVAIARAIVKDPKVLLLDEATSAL-DAESERVVqDALdRVMVNR-TTIV-VAHRLSTIK-NADVIAVVKNGVIV 1258
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLtPQEADELF-EIL-RRLAAEgKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1029-1268 |
3.55e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1029 VESGRVLDNVKGDIELRHVSFKYparpdvqIFQDLCLSIRAGKTVALVGESGSGKSTV-IALLQRFydPDSGEITLDGVE 1107
Cdd:PRK15134 278 VEQLQVAFPIRKGILKRTVDHNV-------VVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1108 IKSLRLKWL---RQQTGLVSQEPilfNETI--RANIAYgkggDASESEIVSSAELSNAH---GFISGLQQ-GYDTMVGER 1178
Cdd:PRK15134 349 LHNLNRRQLlpvRHRIQVVFQDP---NSSLnpRLNVLQ----IIEEGLRVHQPTLSAAQreqQVIAVMEEvGLDPETRHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1179 -GIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDaeseRVVQD---ALDRVMVNR---TTIVVAHRLSTIKNA--DVI 1249
Cdd:PRK15134 422 yPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRALchQVI 497
|
250
....*....|....*....
gi 15226477 1250 aVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK15134 498 -VLRQGEVVEQGDCERVFA 515
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1043-1268 |
3.77e-18 |
|
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: 85.03 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRL-KWLRQQTG 1121
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANI---AYGKGGDASESEIvssaelsnahgfisgLQQGYDT------MVGERGIQLSGGQKQRVA 1191
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLllgAYARRDRAEVRAD---------------LERVYELfprlkeRRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1192 IARAIVKDPKVLLLDEATSALdaeSERVVQDALDRVM-VNR--TTIVV----AHRLSTIknADVIAVVKNGVIVEKGKHD 1264
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRrLNRegVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAA 221
|
....
gi 15226477 1265 TLIN 1268
Cdd:COG0410 222 ELLA 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1058-1266 |
3.97e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 84.88 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1058 QIFQDLCLSIRAGKTVALVGESGSGKST----VIALLQrfydPDSGEITLDGVEIKSLRLKWlRQQTGL--VSQEPILFN 1131
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLLP----VKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1132 E-TIRANIAYGKGG-DASESEIVSSA-ELSNAhgfisgLQQgydtMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEA 1208
Cdd:TIGR03410 89 RlTVEENLLTGLAAlPRRSRKIPDEIyELFPV------LKE----MLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1209 TSALD----AESERVVQDALDRvmVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTL 1266
Cdd:TIGR03410 159 TEGIQpsiiKDIGRVIRRLRAE--GGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
396-617 |
5.37e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.53 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 396 RPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG----------INLKEF---QLKWIR-SK 461
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQsaaQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPV-----LFTA------SIKDNIAYGKEDAtteeikaaaeLANASKFVD--KLPQGlDTMVGEHGTQLSGGQK 528
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeqiaeSIRLHQGASREEA----------MVEAKRMLDqvRIPEA-QTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 529 QRIAVARAILKDPRILLLDEATSALDAESE-------RVVQEALDrimvnRTTVVVAHRLSTVRN-ADMIAVIHQGKIVE 600
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMS-----MGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
250
....*....|....*..
gi 15226477 601 KGSHTELLKDPEGAYSQ 617
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTR 266
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1261 |
5.64e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.44 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1037 NVKGDIELR--HVSFKYPARPDVQI--FQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI---- 1108
Cdd:PRK13631 15 PLSDDIILRvkNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1109 ------------KSLRLKWLRQQTGLVSQEP--ILFNETIRANIAYGK---GGDASESeivssAELSNAHgfISGLQQGY 1171
Cdd:PRK13631 95 nnhelitnpyskKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPvalGVKKSEA-----KKLAKFY--LNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1172 DTMvgERG-IQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESER-VVQDALDRVMVNRTTIVVAHRLSTI-KNADV 1248
Cdd:PRK13631 168 SYL--ERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADE 245
|
250
....*....|...
gi 15226477 1249 IAVVKNGVIVEKG 1261
Cdd:PRK13631 246 VIVMDKGKILKTG 258
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
82-341 |
7.32e-18 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 85.67 E-value: 7.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 82 LLFGDLIDAFGENQTNTT----DKVSKVALKFVWL----GIGTFAAAFLqLSgwmISGERQAARIRSLYLKTILRQDIAF 153
Cdd:cd18574 17 LLLGDLVNVISRSLKETNgdfiEDLKKPALKLLGLyllqSLLTFAYISL-LS---VVGERVAARLRNDLFSSLLRQDIAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 154 FDIdTNTGEVVGRMSGDtvlIQD---AMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAK 230
Cdd:cd18574 93 FDT-HRTGELVNRLTAD---VQEfksSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 231 TASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHL--------VTAYKAGVIEGGSTglglgtlfLVVFCSY 302
Cdd:cd18574 169 LSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVekaaklneKLGLGIGIFQGLSN--------LALNGIV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 15226477 303 ALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTS 341
Cdd:cd18574 241 LGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLS 279
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
403-607 |
7.49e-18 |
|
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: 83.96 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN-LKEfqLKWIRSKIGLVSQEPVL---FTAsiKD 478
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVRE--PREVRRRIGIVFQDLSVddeLTG--WE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 479 NIA-----YG-KEDATTEEIKAAAELANASKFVDKLpqgldtmVGEHgtqlSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:cd03265 93 NLYiharlYGvPGAERRERIDELLDFVGLLEAADRL-------VKTY----SGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 553 LDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
60-339 |
7.75e-18 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 85.56 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIGNGLGFPLmtlLFGDLID-AFGENQTNttdkvskvalKFVWLGIGTFAAAFLQ-----LSGWM--ISG 131
Cdd:cd18542 1 YLLAILALLLATALNLLIPL---LIRRIIDsVIGGGLRE----------LLWLLALLILGVALLRgvfryLQGYLaeKAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 132 ERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVML 211
Cdd:cd18542 68 QKVAYDLRNDLYDHLQRLSFSFHD-KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 212 SSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGL 291
Cdd:cd18542 147 AIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYW 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15226477 292 GTLFLVVFCSYALAVWYGGklildkgytggqvlniiIAVLTGSMSLGQ 339
Cdd:cd18542 227 PLMDFLSGLQIVLVLWVGG-----------------YLVINGEITLGE 257
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1261 |
8.22e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 8.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR--LKWLRQQ 1119
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkgLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEP--ILFNETIRANIAYGKGG-DASESEIVSSAELSNAHGFISGLQQgydtmvgERGIQLSGGQKQRVAIARAI 1196
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNlKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1197 VKDPKVLLLDEATSALD----AESERVVQDALDRVMVnrTTIVVAHRLSTIK-NADVIAVVKNGVIVEKG 1261
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGL--TIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1042-1243 |
9.61e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.77 E-value: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLRQ 1118
Cdd:PRK10908 2 IRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQE-PILFNETIRANIAYgkggdaseSEIVSSAELSNAHGFISGLQQGYDTMVGERG--IQLSGGQKQRVAIARA 1195
Cdd:PRK10908 80 QIGMIFQDhHLLMDRTVYDNVAI--------PLIIAGASGDDIRRRVSAALDKVGLLDKAKNfpIQLSGGEQQRVGIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15226477 1196 IVKDPKVLLLDEATSALD-AESERVVQ--DALDRVMVnrTTIVVAHRLSTI 1243
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDdALSEGILRlfEEFNRVGV--TVLMATHDIGLI 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1042-1266 |
1.06e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRlKWLRQQTG 1121
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 --LVSQEPILF-NETIRANIAYG--KGGDASESEIVSSAELsnahgfisGLQQGYDTMVGergiQLSGGQKQRVAIARAI 1196
Cdd:PRK15439 88 iyLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAAL--------GCQLDLDSSAG----SLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1197 VKDPKVLLLDEATSALD-AESERVVQDaLDRVMVNRTTIV-VAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTL 1266
Cdd:PRK15439 156 MRDSRILILDEPTASLTpAETERLFSR-IRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1261 |
1.07e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYpaRPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTG 1121
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEP--ILFNETIRANIAYGKGGDASESEIVssaelsnAHGFISGLQQ-GYDTMVGERGIQLSGGQKQRVAIARAIVK 1198
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETV-------AHRVSSALHMlGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDALDRVMVN--RTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYG 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
404-621 |
1.22e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLfiSSGTTVALVGQSGSGKSTVVSLIERFYDPQaGDVLIDGINLKEF---QLKWIRSKIGLVSQEPV------LFTA 474
Cdd:PRK15134 306 SFTL--RPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDPNsslnprLNVL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 SIkdnIAYGKE------DATTEE---IKAAAELanaskfvdklpqGLD-TMVGEHGTQLSGGQKQRIAVARAILKDPRIL 544
Cdd:PRK15134 383 QI---IEEGLRvhqptlSAAQREqqvIAVMEEV------------GLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 545 LLDEATSALDaeseRVVQE---ALDRIMVNR---TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAYS- 616
Cdd:PRK15134 448 ILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEYTr 523
|
....*
gi 15226477 617 QLIRL 621
Cdd:PRK15134 524 QLLAL 528
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1261 |
1.31e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.36 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI----KSLrLKwLR 1117
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSL-LE-VR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 QQTGLVSQEP--ILFNETIRANIAYGK---GGDASESEIVSSAELSNAhgfisGLqQGYDTMVGErgiQLSGGQKQRVAI 1192
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEEDVAFGPlnlGLSKEEVEKRVKEALKAV-----GM-EGFENKPPH---HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 1193 ARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KNADVIAVVKNGVIVEKG 1261
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1042-1266 |
1.47e-17 |
|
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: 83.19 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSlRLKWLRQQTG 1121
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNE-TIRANIA-----YGKGGDASESEIvssAELSNAhgfiSGLQQGYDTMVGergiQLSGGQKQRVAIARA 1195
Cdd:cd03265 77 IVFQDLSVDDElTGWENLYiharlYGVPGAERRERI---DELLDF----VGLLEAADRLVK----TYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1196 IVKDPKVLLLDEATSALDAESE----RVVQDALDRvmVNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGKHDTL 1266
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRahvwEYIEKLKEE--FGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
384-611 |
1.66e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.43 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTypaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK09536 4 IDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVL-FTASIKDNIAYGK----------EDATTEEIKAAAELANASKFVDKlpqgldtmvgeHGTQLSGGQKQRIA 532
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFADR-----------PVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 533 VARAILKDPRILLLDEATSALDAESE-RVVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTA 229
|
.
gi 15226477 611 P 611
Cdd:PRK09536 230 D 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
384-610 |
1.77e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.59 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVlFTA--SIKDNIAYG----------KEDAttEEIKAA------AELANasKFVDklpqgldtmvgehgtQLSG 525
Cdd:COG4604 79 ILRQENH-INSrlTVRELVAFGrfpyskgrltAEDR--EIIDEAiayldlEDLAD--RYLD---------------ELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALdRIMV---NRTTVVVAHRLstvrN-----ADMIAVIHQGK 597
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLL-RRLAdelGKTVVIVLHDI----NfascyADHIVAMKDGR 213
|
250
....*....|....*...
gi 15226477 598 IVEKGS-----HTELLKD 610
Cdd:COG4604 214 VVAQGTpeeiiTPEVLSD 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1041-1262 |
3.03e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.08 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1041 DIELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwlRQQT 1120
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILF-NETIRANIAYG-KGGDASESEIVS----SAELsnahgfisgLQQGYdtMVGERGIQLSGGQKQRVAIAR 1194
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFGlKLAGAKKEEINQrvnqVAEV---------LQLAH--LLDRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1195 AIVKDPKVLLLDEATSALDAeSERV---VQDALDRVMVNRTTIVVAH-RLSTIKNADVIAVVKNGVIVEKGK 1262
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
384-600 |
4.47e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIdGINLKefqlkwirskIG 463
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVLF--TASIKDNIAYGKEDATTEEIKAAAElanasKF------VDKLpqgldtmVGEhgtqLSGGQKQRIAVAR 535
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLG-----RFlfsgddAFKP-------VGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRImvNRTTVVVAH-R--LSTVrnADMIAVIHQGKIVE 600
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
400-612 |
4.57e-17 |
|
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: 81.82 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQL-KWIRSKIGLVSQEPVLFtasikd 478
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 479 niaygkEDATTEE-IKAAAELANASKfvDKLPQGLDTMVGE---------HGTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:cd03218 88 ------RKLTVEEnILAVLEIRGLSK--KEREEKLEELLEEfhithlrksKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 549 ATSALD----AESERVVQEALDR---IMVN----RTTVVVAHRlstvrnadmIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:cd03218 160 PFAGVDpiavQDIQKIIKILKDRgigVLITdhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
384-599 |
4.99e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.32 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPArPDEQI--FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF------QL 455
Cdd:PRK10535 5 LELKDIRRSYPS-GEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalaQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 456 KwiRSKIGLVSQEPVLFT-ASIKDNIAYGKEDATTEEikaAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVA 534
Cdd:PRK10535 84 R--REHFGFIFQRYHLLShLTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTVRNADMIAVIHQGKIV 599
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1042-1238 |
5.00e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSfKYPARPDVQ--IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL----RLKW 1115
Cdd:PRK10584 7 VEVHHLK-KSVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeaRAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 LRQQTGLVSQEPILFnETIRA--NI---AYGKGGDASESEIVSSAELSNAhgfisGLQQGYDTMVGergiQLSGGQKQRV 1190
Cdd:PRK10584 86 RAKHVGFVFQSFMLI-PTLNAleNVelpALLRGESSRQSRNGAKALLEQL-----GLGKRLDHLPA----QLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALDAESERVVQDALdrVMVNR----TTIVVAH 1238
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL--FSLNRehgtTLILVTH 205
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
393-617 |
5.08e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 393 YPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDP----QAGDVLIDGINLKEFQLKWIrsKIGLVSQE 468
Cdd:PRK10418 13 QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGR--KIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 469 P--------VLFTASIKDNIAYGKE--DATTEEIKAAAELANAskfvdklpqglDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PRK10418 88 PrsafnplhTMHTHARETCLALGKPadDATLTAALEAVGLENA-----------ARVLKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIMVNRT--TVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKHAV 236
|
..
gi 15226477 616 SQ 617
Cdd:PRK10418 237 TR 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
384-597 |
5.93e-17 |
|
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: 79.03 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwiRSKIG 463
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQepvlftasikdniaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 544 LLLDEATSALDAESERVVQEALDRImvNRTTVVVAH-R--LSTVrnADMIAVIHQGK 597
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
400-606 |
6.33e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 6.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRSKIGLVSQEP-VLFTAS 475
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYGK--EDATTEEIKAAAELAnaskfVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:PRK10908 96 VYDNVAIPLiiAGASGDDIRRRVSAA-----LDKV--GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 554 D-AESERVVQ--EALDRIMVnrTTVVVAHRLSTV-RNADMIAVIHQGKIVEkGSHTE 606
Cdd:PRK10908 169 DdALSEGILRlfEEFNRVGV--TVLMATHDIGLIsRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1065-1277 |
6.58e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLQRFYDPDS---GEITLDGVEIK-----SLRLKWLRQQTGLVSQEPILFNE-TIR 1135
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQregrlARDIRKSRANTGYIFQQFNLVNRlSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1136 ANIAYGKGGDASESEIVSS--AELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1213
Cdd:PRK09984 105 ENVLIGALGSTPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1214 AESERVVQDALDRVMVNR--TTIVVAHRLS-TIKNADVIAVVKNGVIVEKGKHDTLINIK-DGVYASL 1277
Cdd:PRK09984 185 PESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHLYRSI 252
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1043-1267 |
6.98e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYPArpdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIK--SLRlKWLRQQT 1120
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTT-AALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFNE-TIRANIAYG----KGGDASESEIVSSAELSNAHgfiSGLQQGYDTMVGErgiqLSGGQKQRVAIARA 1195
Cdd:PRK11288 82 AIIYQELHLVPEmTVAENLYLGqlphKGGIVNRRLLNYEAREQLEH---LGVDIDPDTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1196 IVKDPKVLLLDEATSALDA-ESE---RVVQDALDRvmvNRTTIVVAHRLSTI-KNADVIAVVKNGVIVE------KGKHD 1264
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRD 231
|
...
gi 15226477 1265 TLI 1267
Cdd:PRK11288 232 QLV 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1040-1268 |
7.93e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 7.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDIELRHVSFKYPARpdvqifqdlclsiragKTVALVGESGSGKSTVIALLQRFYDP-----DSGEITLDGVEIKSLR-L 1113
Cdd:PRK14271 33 GKTVLDQVSMGFPAR----------------AVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1114 KWLRQQTGLVSQEPILFNETIRANIAYG----KGGDASESEIVSSAELSNAhgfisGLQQGYDTMVGERGIQLSGGQKQR 1189
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPFPMSIMDNVLAGvrahKLVPRKEFRGVAQARLTEV-----GLWDAVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
721-978 |
8.36e-17 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 82.44 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 721 ILGSISAAANGVILPIfgiLISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCF 800
Cdd:cd18544 5 LLLLLLATALELLGPL---LIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 801 EKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGF 880
Cdd:cd18544 82 SHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 881 LYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSY 960
Cdd:cd18544 160 LFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLAL 239
|
250
....*....|....*...
gi 15226477 961 AASFYVGARLVDDGKTTF 978
Cdd:cd18544 240 ALVLWYGGGQVLSGAVTL 257
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
409-608 |
1.13e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 409 ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVL-FTASIKDNIAYG---- 483
Cdd:PRK10253 30 IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQELVARGryph 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 484 --------KEDAtteeiKAAAELANASKFVDKLPQGLDTmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDA 555
Cdd:PRK10253 110 qplftrwrKEDE-----EAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 556 ESERVVQEALDRImvNR----TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK10253 177 SHQIDLLELLSEL--NRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1042-1213 |
1.14e-16 |
|
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: 80.66 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKwLRQQTG 1121
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 L--VSQEPILFNE-TIRANIAYgkggdASESEIVSSAELSN-AHGFISGLQqgYDTMVGERGIQLSGGQKQRVAIARAIV 1197
Cdd:cd03218 77 IgyLPQEASIFRKlTVEENILA-----VLEIRGLSKKEREEkLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALA 149
|
170
....*....|....*.
gi 15226477 1198 KDPKVLLLDEATSALD 1213
Cdd:cd03218 150 TNPKFLLLDEPFAGVD 165
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
384-555 |
1.32e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.97 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPArpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INlkefQLKWIRSK 461
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVN----ELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVA 534
Cdd:PRK11650 78 IAMVFQNYALYPhMSVRENMAYGlkirgmPKAEIEERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMG 146
|
170 180
....*....|....*....|.
gi 15226477 535 RAILKDPRILLLDEATSALDA 555
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1049-1279 |
1.33e-16 |
|
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: 86.22 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1049 FKYPARPDVQifqDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSlRLKWLRQQTGLVSQEPI 1128
Cdd:TIGR01257 938 FEPSGRPAVD---RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1129 LFNE-TIRANI---AYGKGGDASESEIVSSAELSNahgfiSGLQQGYDtmvgERGIQLSGGQKQRVAIARAIVKDPKVLL 1204
Cdd:TIGR01257 1014 LFHHlTVAEHIlfyAQLKGRSWEEAQLEMEAMLED-----TGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1205 LDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTLIN-IKDGVYASLVQ 1279
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNcFGTGFYLTLVR 1161
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1042-1239 |
1.41e-16 |
|
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: 78.73 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFkypARPDVQIF-QDLCLSIRAGKTVALVGESGSGKST---VIALLQRFYdpdSGEITLDGVEikslrlkwlr 1117
Cdd:cd03223 1 IELENLSL---ATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSlfrALAGLWPWG---SGRIGMPEGE---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 qQTGLVSQEPILFNETIRANIAYgkggdaseseivssaelsnahgfisglqqgydtmvgERGIQLSGGQKQRVAIARAIV 1197
Cdd:cd03223 65 -DLLFLPQRPYLPLGTLREQLIY------------------------------------PWDDVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15226477 1198 KDPKVLLLDEATSALDAESERVVQDALDRVMVnrTTIVVAHR 1239
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
398-610 |
1.78e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.50 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI---ERfYDPQAGDVLIDGINLkefqLKW---IRSK--IGLVSQEP 469
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDI----LELspdERARagIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 470 V--------LFTASIKDNIAYGKEDATT--EEIKAAAELAN-ASKFVDKlpqGLDtmVGehgtqLSGGQKQRIAVARAIL 538
Cdd:COG0396 87 VeipgvsvsNFLRTALNARRGEELSAREflKLLKEKMKELGlDEDFLDR---YVN--EG-----FSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGSHtELLKD 610
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELALE 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1042-1255 |
2.50e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 77.10 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveikslrlkwlrqqtg 1121
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 lvsqepilfnetiRANIAYgkggdaseseivssaelsnahgfisglqqgYDtmvgergiQLSGGQKQRVAIARAIVKDPK 1201
Cdd:cd03221 62 -------------TVKIGY------------------------------FE--------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRvmVNRTTIVVAHRLSTIKN-ADVIAVVKNG 1255
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
721-977 |
2.58e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 81.05 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 721 ILGSISAAANGVILP-IFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMC 799
Cdd:cd18574 2 VLSALAAALVNIQIPlLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 800 FEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNG 879
Cdd:cd18574 82 FSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 880 FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIvsGIGF--GFSFFVLF 957
Cdd:cd18574 160 TLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGL--GIGIfqGLSNLALN 237
|
250 260
....*....|....*....|
gi 15226477 958 SSYAASFYVGARLVDDGKTT 977
Cdd:cd18574 238 GIVLGVLYYGGSLVSRGELT 257
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1042-1261 |
2.79e-16 |
|
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: 79.50 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYP-------------------ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEIT 1102
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1103 LDGvEIKSLrlkwLRQQTGLvsqEPILfneTIRANIAY--------GKGGDASESEIVSSAELSNAhgfisglqqgYDTM 1174
Cdd:cd03220 81 VRG-RVSSL----LGLGGGF---NPEL---TGRENIYLngrllglsRKEIDEKIDEIIEFSELGDF----------IDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1175 VGErgiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDAL-DRVMVNRTTIVVAHRLSTIKN-ADVIAVV 1252
Cdd:cd03220 140 VKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVL 215
|
....*....
gi 15226477 1253 KNGVIVEKG 1261
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1056-1261 |
2.85e-16 |
|
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: 78.72 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1056 DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRF--YDPDSGEITLDGVEIKSLRLKwLRQQTG--LVSQEPIlfn 1131
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGifLAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1132 etiraniaygkggdasesEIvssAELSNAHgFISGLQQGydtmvgergiqLSGGQKQRVAIARAIVKDPKVLLLDEATSA 1211
Cdd:cd03217 88 ------------------EI---PGVKNAD-FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1212 LDAESERVVQDALDRVM-VNRTTIVVAH--RLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:cd03217 135 LDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1042-1282 |
2.99e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFkYPARPDVQifqDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPD----SGEITLDGVEI--KSLRLKw 1115
Cdd:PRK10418 5 IELRNIAL-QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVapCALRGR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 lrqQTGLVSQEP-ILFN--ETIRAN-----IAYGK-GGDASESEIVSSAELSNAHgfisglqqgydTMVGERGIQLSGGQ 1186
Cdd:PRK10418 80 ---KIATIMQNPrSAFNplHTMHTHaretcLALGKpADDATLTAALEAVGLENAA-----------RVLKLYPFEMSGGM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1187 KQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRT--TIVVAHRLSTI-KNADVIAVVKNGVIVEKGKH 1263
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDV 225
|
250 260
....*....|....*....|
gi 15226477 1264 DTLINI-KDGVYASLVQLHL 1282
Cdd:PRK10418 226 ETLFNApKHAVTRSLVSAHL 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
384-610 |
3.09e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.90 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPAR-PDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDV------------------ 443
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 444 LIDGINLKEF------QLKWIRSKIGLVSQ--EPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVdklpqGLDTM 515
Cdd:PRK13651 83 VLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELV-----GLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 516 VGEHGT-QLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTV-RNADMIAV 592
Cdd:PRK13651 158 YLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKRTIF 237
|
250
....*....|....*...
gi 15226477 593 IHQGKIVEKGSHTELLKD 610
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1059-1241 |
3.15e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.47 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1059 IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL----RLKWLRQQTGLVSQ-EPILFNET 1133
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1134 IRANIAY----GKGGDASESEivssaelsNAHGFISGLqqGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEAT 1209
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINS--------RALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....
gi 15226477 1210 SALDAESERVVQDALDRVMVNRTT--IVVAHRLS 1241
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
761-981 |
3.22e-16 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 80.85 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 761 FWAIIFMVL-GFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAAtirgLVGDS 839
Cdd:cd18590 36 TSAIGLMCLfSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTT----LMSRS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 840 LAQtvqNLSSILAGLIIAFLAC-------WQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIR 912
Cdd:cd18590 110 VAL---NANVLLRSLVKTLGMLgfmlslsWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIR 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 913 TVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSV 981
Cdd:cd18590 187 TVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSL 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
404-610 |
3.26e-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: 83.31 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLI----DGINLKE--FQLKWiRSK--IGLVSQEPVLFT-A 474
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKpgPDGRG-RAKryIGILHQEYDLYPhR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 SIKDNIA----------YGKEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRIL 544
Cdd:TIGR03269 381 TVLDNLTeaiglelpdeLARMKAVITLKMVGFDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 545 LLDEATSALDAESERVVQEAL--DRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
60-339 |
3.58e-16 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 80.60 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIGNGLGFPLMTllfGDLIDafGENQTNTTDKVSKVALKFVWLGIGTFAAAFL--QLSGWMISG-ErqaA 136
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLT---RRAID--GPIAHGDRSALWPLVLLLLALGVAEAVLSFLrrYLAGRLSLGvE---H 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 137 RIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGeKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18543 73 DLRTDLFAHLQRLDGAFHD-RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 217 LVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFL 296
Cdd:cd18543 151 LVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEA 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15226477 297 VVFCSYALAVWYGGklildkgytggqvlniiIAVLTGSMSLGQ 339
Cdd:cd18543 231 LPELGLAAVLALGG-----------------WLVANGSLTLGT 256
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1042-1268 |
3.64e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYP-------------------ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEIT 1102
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1103 LDGveikslRLKWL--------RQQTGLvsqEPILFNETI----RANIaygkggDASESEIVSSAELSNahgFIsglqqg 1170
Cdd:COG1134 85 VNG------RVSALlelgagfhPELTGR---ENIYLNGRLlglsRKEI------DEKFDEIVEFAELGD---FI------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1171 yDTMVGergiQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAE----SERVVQDALDRvmvNRTTIVVAHRLSTIKN- 1245
Cdd:COG1134 141 -DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRl 212
|
250 260
....*....|....*....|...
gi 15226477 1246 ADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
398-610 |
3.84e-16 |
|
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: 78.34 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF--YDPQAGDVLIDGINLKEFQLKwIRSK--IGLVSQEPVLFt 473
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPPEI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 474 asikdniaygkedattEEIKaaaeLANASKFVDklpqgldtmVGehgtqLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:cd03217 90 ----------------PGVK----NADFLRYVN---------EG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 554 DAESERVVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGShTELLKD 610
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
395-565 |
4.30e-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: 78.30 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTA 474
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 SIKDNIAYGKEDATTEEIKAAAELANASKFVDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 554
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGFED-RPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|.
gi 15226477 555 AESERVVQEAL 565
Cdd:cd03231 158 KAGVARFAEAM 168
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1042-1266 |
4.53e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.81 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFkypARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL---RLKWLRQ 1118
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNE-TIRANIAYG-KGGDASESEIVSSAELSNAHGFisGLQQGYDTMVGErgiqLSGGQKQRVAIARAI 1196
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPlREHTQLPAPLLHSTVMMKLEAV--GLRGAAKLMPSE----LSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1197 VKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTL 1266
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1042-1262 |
5.06e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.15 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKslrlKWLRQQTG 1121
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILF-NETIRANIAY-G--KGGDASESEIvSSAELSNAHGfisgLQQGYDTMVGErgiqLSGGQKQRVAIARAIV 1197
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlArlKGLSKAEAKR-RADEWLERLG----LGDRANKKVEE----LSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1198 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTI-KNADVIAVVKNGVIVEKGK 1262
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1042-1261 |
6.54e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpdVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQ-T 1120
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFNE-TIRANIAYGKGG----------DASESEIVSSAELsnahgFISGLQQGYDTMVGErgiqLSGGQKQR 1189
Cdd:PRK09700 83 GIIYQELSVIDElTVLENLYIGRHLtkkvcgvniiDWREMRVRAAMML-----LRVGLKVDLDEKVAN----LSISHKQM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1190 VAIARAIVKDPKVLLLDEATSAL-DAESERVVQdALDRVMVNRTTIV-VAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1042-1261 |
7.22e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQ---IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKW-LR 1117
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 QQTGLVSQEPilfNETIRANI-----AYGK---GGDASE-----SEIVSSAELSNAHGFISGLqqgydtmvgergiqLSG 1184
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATIveedvAFGPenlGIPPEEirervDESLKKVGMYEYRRHAPHL--------------LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1185 GQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR----TTIVVAHRLSTIKNADVIAVVKNGVIVEK 1260
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKE--LNKkygiTIILITHYMEEAVEADRIIVMDSGKVVME 225
|
.
gi 15226477 1261 G 1261
Cdd:PRK13633 226 G 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
402-598 |
9.17e-16 |
|
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: 76.70 E-value: 9.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQ-LKWIRSKIGLVSQEP----VLFTASI 476
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 477 KDNIAygkedatteeikaaaelanaskfvdkLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE 556
Cdd:cd03215 96 AENIA--------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15226477 557 SERVVQEALDRIMVNRTTVVVahrLST-----VRNADMIAVIHQGKI 598
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1062-1262 |
9.30e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.30 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1062 DLCLSIRA-----GKTvALVGESGSGKSTVIALLQRFYDPDSGEITLDG-VEIKSLRLKWL---RQQTGLVSQEPILF-N 1131
Cdd:PRK11144 12 DLCLTVNLtlpaqGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLppeKRRIGYVFQDARLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1132 ETIRANIAYG-KGGDASEseivssaelsnahgfisglqqgYDTMVGERGIQ---------LSGGQKQRVAIARAIVKDPK 1201
Cdd:PRK11144 91 YKVRGNLRYGmAKSMVAQ----------------------FDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1202 VLLLDEATSALDAESERVVQDALDRVM--VNRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGK 1262
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
396-609 |
9.71e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 396 RPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIErFYDPQ----AGDVLIDG--INLKEFQLkwiRSK-------- 461
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGmpIDAKEMRA---ISAyvqqddlf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IG-LVSQEPVLFTASIK--DNIAYGKEDATTEEIKAAAELANASkfvdklpqglDTMVGEHGTQ--LSGGQKQRIAVARA 536
Cdd:TIGR00955 111 IPtLTVREHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCA----------NTRIGVPGRVkgLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLST--VRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
401-582 |
1.29e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.55 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF----QLKWIRSKIGLVSQEPVL---FT 473
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLlpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 474 ASikDNIAY-----GKEDATTEEiKAAAELANAskfvdklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:PRK11629 104 AL--ENVAMplligKKKPAEINS-RALEMLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 15226477 549 ATSALDAESERVVQEALDRIMVNRTT--VVVAHRLS 582
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
412-617 |
1.59e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 412 GTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGI---NLKEFQLKWIRSKIGLVSQEPVlftASIKDNIAYGkeDAT 488
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPY---ASLDPRQTVG--DSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 489 TEEIK---------AAAELANASKFVDKLPqgldtmvgEHG----TQLSGGQKQRIAVARAILKDPRILLLDEATSALDA 555
Cdd:PRK10261 425 MEPLRvhgllpgkaAAARVAWLLERVGLLP--------EHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 556 E-SERVVQEALD--RIMvNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQ 617
Cdd:PRK10261 497 SiRGQIINLLLDlqRDF-GIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQHPYTR 561
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
416-633 |
1.67e-15 |
|
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: 82.37 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 416 ALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLkEFQLKWIRSKIGLVSQEPVLFT-ASIKDNIA-YGKEDATTEEik 493
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILfYAQLKGRSWE-- 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 494 aAAELANASKFVDKlpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRT 573
Cdd:TIGR01257 1037 -EAQLEMEAMLEDT---GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 574 TVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTeLLKD--PEGAYSQLIRLQEEKKSDENAAE 633
Cdd:TIGR01257 1113 IIMSTHHMDEADLlGDRIAIISQGRLYCSGTPL-FLKNcfGTGFYLTLVRKMKNIQSQRGGCE 1174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1042-1261 |
1.93e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVS--FKYPA----RPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI------- 1108
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1109 KSLRLKWL----------RQQTGLVSQEPILFNETIraniaygkggDASESEIVSSAELSNAhGFISGLQQGYDTMvger 1178
Cdd:PRK15112 85 RSQRIRMIfqdpstslnpRQRISQILDFPLRLNTDL----------EPEQREKQIIETLRQV-GLLPDHASYYPHM---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1179 giqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAEservVQDALDRVMVNR------TTIVVAHRLSTIKN-ADVIAV 1251
Cdd:PRK15112 150 ---LAPGQKQRLGLARALILRPKVIIADEALASLDMS----MRSQLINLMLELqekqgiSYIYVTQHLGMMKHiSDQVLV 222
|
250
....*....|
gi 15226477 1252 VKNGVIVEKG 1261
Cdd:PRK15112 223 MHQGEVVERG 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1049-1262 |
1.96e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1049 FKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIK-SLR-LKWLRQQTGLVSQE 1126
Cdd:PRK13638 9 FRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRgLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1127 P--ILFNETIRANIAYG-KGGDASESEIVSSAE----LSNAHGFisglqqgydtmvGERGIQ-LSGGQKQRVAIARAIVK 1198
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSlRNLGVPEAEITRRVDealtLVDAQHF------------RHQPIQcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDALDRVMVN-RTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGK 1262
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGA 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1060-1255 |
2.15e-15 |
|
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: 75.55 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1060 FQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWL-----------RQQTGLVSQEPI 1128
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragiayvpedRKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1129 LFNETIraniaygkggdaseseivssaelsnahgfisglqqgydtmvgerGIQLSGGQKQRVAIARAIVKDPKVLLLDEA 1208
Cdd:cd03215 96 AENIAL--------------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1209 TSALDAESERVVQDALDRVMVNRTTIVVahrLST-----IKNADVIAVVKNG 1255
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEG 180
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1042-1207 |
3.08e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQifqDLCLSIRAGKTVALVGESGSGKSTViallqrFY------DPDSGEITLDGVEIKSLRLkW 1115
Cdd:COG1137 4 LEAENLVKSYGKRTVVK---DVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-H 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 LRQQTGL--VSQEPILFN-----ETIRAnIAYGKGGDASE-SEIVSS--AELSnahgfISGLQqgyDTmvgeRGIQLSGG 1185
Cdd:COG1137 74 KRARLGIgyLPQEASIFRkltveDNILA-VLELRKLSKKErEERLEEllEEFG-----ITHLR---KS----KAYSLSGG 140
|
170 180
....*....|....*....|..
gi 15226477 1186 QKQRVAIARAIVKDPKVLLLDE 1207
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDE 162
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
405-611 |
3.08e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 405 FSLFISSGTTVALVGQSGSGKSTVVSLIERFYdPQAGDVLIDGINLKEFQL-KWIRSKIGLVSQEPVLFTASIKDNIAYG 483
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 484 KEDATTEEIKAAA--ELANASKFVDKLPQGLdtmvgehgTQLSGGQKQRIAVARAILK-DPRI------LLLDEATSALD 554
Cdd:PRK03695 94 QPDKTRTEAVASAlnEVAEALGLDDKLGRSV--------NQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 555 aeserVVQE-ALDRIMV-----NRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK03695 166 -----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
403-610 |
3.33e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.84 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKwIRSKIGLVSQEPVLFTA-SIKDNIA 481
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPE-DRRRIGYLPEERGLYPKmKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 482 Y-----GkedatteeIKAAAELANASKFVDKLpqGLdtmvGEHGT----QLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:COG4152 94 YlarlkG--------LSKAEAKRRADEWLERL--GL----GDRANkkveELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 553 LDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:COG4152 160 LDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1053-1216 |
3.65e-15 |
|
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: 75.47 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1053 ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRqqtglvsqepilfne 1132
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1133 tiraNIAYGKGGDASESEIVSSAELSNAHGFISGLQQGYD---TMVGERGI------QLSGGQKQRVAIARAIVKDPKVL 1203
Cdd:TIGR01189 74 ----NILYLGHLPGLKPELSALENLHFWAAIHGGAQRTIEdalAAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLW 149
|
170
....*....|...
gi 15226477 1204 LLDEATSALDAES 1216
Cdd:TIGR01189 150 ILDEPTTALDKAG 162
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1063-1262 |
4.20e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.42 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1063 LCLSIRAGKTVALVGESGSGKSTVIALLQRFYdPDSGEITLDGVEIKSLRLK-------WLRQQTGLVSQEPI-----LF 1130
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFAMPVfqylaLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1131 netiraniaYGKGGDASESEIVSsAELSNAhgfiSGLQQGYDTMVGergiQLSGGQKQRVAIARAIVK-------DPKVL 1203
Cdd:COG4138 94 ---------QPAGASSEAVEQLL-AQLAEA----LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptinpEGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1204 LLDEATSALDaeserVVQD-ALDRVMVN-----RTTIVVAHRLS-TIKNADVIAVVKNGVIVEKGK 1262
Cdd:COG4138 156 LLDEPMNSLD-----VAQQaALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1022-1260 |
4.47e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1022 ESKIDPSVESGRVLDNVkgDIELRHVSFKyparpdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFY--DPDSG 1099
Cdd:COG2401 18 SSVLDLSERVAIVLEAF--GVELRVVERY--------VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1100 EITLDGVEIKSlrlkwlrqqtglvsqepilfNETIRANIayGKGGDASES-EIVSSAELSNAHGFISglqqgydtmvgeR 1178
Cdd:COG2401 88 CVDVPDNQFGR--------------------EASLIDAI--GRKGDFKDAvELLNAVGLSDAVLWLR------------R 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1179 GIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVV----QDALDRvmVNRTTIVVAHRlSTIKNA---DVIAV 1251
Cdd:COG2401 134 FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVarnlQKLARR--AGITLVVATHH-YDVIDDlqpDLLIF 210
|
250
....*....|
gi 15226477 1252 V-KNGVIVEK 1260
Cdd:COG2401 211 VgYGGVPEEK 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1042-1214 |
4.88e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 78.35 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpDVQIFQDLCLSIRAGKTVALVGESGSGKSTV---IALLQRFydpDSGEITLDGVEIKSLrlkwlrq 1118
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRVVNEL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 qtglvsqEP------ILFNE-------TIRANIAYG-KGGDASESEI---VSSA----ELsnahgfisglqqgyDTMVGE 1177
Cdd:PRK11650 72 -------EPadrdiaMVFQNyalyphmSVRENMAYGlKIRGMPKAEIeerVAEAarilEL--------------EPLLDR 130
|
170 180 190
....*....|....*....|....*....|....*..
gi 15226477 1178 RGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDA 1214
Cdd:PRK11650 131 KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
719-978 |
5.49e-15 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 77.06 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 719 VLILGSISAAANgVILPIF-GILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRS 797
Cdd:cd18547 4 VIILAIISTLLS-VLGPYLlGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 798 MCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIal 877
Cdd:cd18547 83 DLFEKLQRLPLSYFDT--HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 878 ngFLYMKFM-----KGFSADAKKMyGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFS 952
Cdd:cd18547 159 --LLVTKFIakrsqKYFRKQQKAL-GELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIM 235
|
250 260
....*....|....*....|....*.
gi 15226477 953 FFVLFSSYAASFYVGARLVDDGKTTF 978
Cdd:cd18547 236 NFINNLGYVLVAVVGGLLVINGALTV 261
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
400-607 |
6.20e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 75.64 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLkwIRSKIGLVSQEPVLFTA-S 475
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHER--ARAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYGkedatteeikaAAELANASKFVDK----LPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATS 551
Cdd:TIGR03410 92 VEENLLTG-----------LAALPRRSRKIPDeiyeLFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 552 ALD----AESERVVQEALDRImvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:TIGR03410 161 GIQpsiiKDIGRVIRRLRAEG--GMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
384-610 |
6.89e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL------KEFQLkw 457
Cdd:PRK15439 12 LCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpaKAHQL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 458 irsKIGLVSQEPVLF-TASIKDNIAYG--KEDATTEeiKAAAELANASKFVDklpqgLDTMVGehgtQLSGGQKQRIAVA 534
Cdd:PRK15439 87 ---GIYLVPQEPLLFpNLSVKENILFGlpKRQASMQ--KMKQLLAALGCQLD-----LDSSAG----SLEVADRQIVEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 535 RAILKDPRILLLDEATSALD-AESERV---VQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLST 229
|
.
gi 15226477 610 D 610
Cdd:PRK15439 230 D 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1042-1255 |
6.96e-15 |
|
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: 79.10 E-value: 6.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDS--GEITLDGVEIKSLRLKWL-RQ 1118
Cdd:TIGR02633 2 LEMKGIVKTFG---GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPILFNE-TIRANIAYG-----KGGDASESEIVssaelSNAHGFISGLQqgYDTMVGERGI-QLSGGQKQRVA 1191
Cdd:TIGR02633 79 GIVIIHQELTLVPElSVAENIFLGneitlPGGRMAYNAMY-----LRAKNLLRELQ--LDADNVTRPVgDYGGGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAESERVVQDAL-DRVMVNRTTIVVAHRLSTIKN-ADVIAVVKNG 1255
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIrDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1056-1261 |
7.53e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.49 E-value: 7.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1056 DVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRfYDPDSGEITLDG-----------------------VEIK 1109
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGedilelspderaragiflafqypVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1110 SLRLK-WLRQQTGLVSQEPI---LFNETIRANIAygkggdaseseivssaELSNAHGFIsglqqgydtmvgERGIQ--LS 1183
Cdd:COG0396 91 GVSVSnFLRTALNARRGEELsarEFLKLLKEKMK----------------ELGLDEDFL------------DRYVNegFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1184 GGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMV-NRTTIVVAH--RLSTIKNADVIAVVKNGVIVEK 1260
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKS 222
|
.
gi 15226477 1261 G 1261
Cdd:COG0396 223 G 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
401-561 |
9.38e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL---KEFQLKWIRSK-IGLVSQEPVLF-TAS 475
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRAKhVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAY-----GKEDATTEEiKAAAELANA--SKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:PRK10584 105 ALENVELpallrGESSRQSRN-GAKALLEQLglGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170
....*....|....
gi 15226477 549 ATSALDAES-ERVV 561
Cdd:PRK10584 173 PTGNLDRQTgDKIA 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
395-566 |
9.75e-15 |
|
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: 74.32 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTA 474
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 SIKDNIAYGKEDATTEE--IKAAAELANASKFVDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQrtIEDALAAVGLTGFED-LPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170
....*....|....
gi 15226477 553 LDAESERVVQEALD 566
Cdd:TIGR01189 158 LDKAGVALLAGLLR 171
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1055-1267 |
1.13e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1055 PDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveiKSLRLKWLR--QQTGL--VSQEPILF 1130
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKssQEAGIgiIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1131 NE-TIRANIAYGKggdaseseivssaELSNAHGFIS---------------GLQQGYDTMVGErgiqLSGGQKQRVAIAR 1194
Cdd:PRK10762 92 PQlTIAENIFLGR-------------EFVNRFGRIDwkkmyaeadkllarlNLRFSSDKLVGE----LSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1195 AIVKDPKVLLLDEATSAL-DAESE---RVVQDALDRvmvNRTTIVVAHRLSTI-KNADVIAVVKNG-VIVEKG----KHD 1264
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRLKEIfEICDDVTVFRDGqFIAEREvadlTED 231
|
...
gi 15226477 1265 TLI 1267
Cdd:PRK10762 232 SLI 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1019-1213 |
1.21e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1019 MDRESKIDPSVESGRVLDNvKGDIELRHVSFKYPARP--------DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALL 1090
Cdd:PRK10261 292 LEHPAKQEPPIEQDTVVDG-EPILQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1091 QRFYDPDSGEITLDGVEIKSL---RLKWLRQQTGLVSQEPILFNETiRANIAYgkggdaseseivSSAELSNAHGFISG- 1166
Cdd:PRK10261 371 LRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDP-RQTVGD------------SIMEPLRVHGLLPGk 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 1167 -LQQGYDTMVGERGIQ----------LSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1213
Cdd:PRK10261 438 aAAARVAWLLERVGLLpehawrypheFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1058-1262 |
1.26e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1058 QIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPD-----SGEITLDGVEIKSLRLKWL--RQQTGLVSQEPILF 1130
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1131 -NETIRANIAYG---KGGDASESEIVSSAELSNAHgfiSGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLD 1206
Cdd:PRK14267 98 pHLTIYDNVAIGvklNGLVKSKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1207 EATSALDAESERVVQDALDRVMVNRTTIVVAHR-LSTIKNADVIAVVKNGVIVEKGK 1262
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1042-1268 |
1.55e-14 |
|
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: 77.92 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRF--YDPDSGEI------------------ 1101
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1102 ----------TLDGVEI------KSLRLKWLRQQTGLVSQEPILF-NETIRANI--AYGKGGDASESEIVSSAELsnahg 1162
Cdd:TIGR03269 78 vgepcpvcggTLEPEEVdfwnlsDKLRRRIRKRIAIMLQRTFALYgDDTVLDNVleALEEIGYEGKEAVGRAVDL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1163 fISGLQQGYDTMVGERgiQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTIVVAHRL 1240
Cdd:TIGR03269 153 -IEMVQLSHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWP 229
|
250 260
....*....|....*....|....*....
gi 15226477 1241 STIKN-ADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:TIGR03269 230 EVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1055-1255 |
2.03e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1055 PDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYdPD---SGEITLDGveiKSLRLKWLR--QQTGLV--SQEP 1127
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG---EELQASNIRdtERAGIAiiHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1128 ILFNE-TIRANIAYGkggdaseSEIVSsaelsnaHGFISglqqgYDTM----------------VGERGIQLSGGQKQRV 1190
Cdd:PRK13549 92 ALVKElSVLENIFLG-------NEITP-------GGIMD-----YDAMylraqkllaqlkldinPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 1191 AIARAIVKDPKVLLLDEATSALdAESE-----RVVQDALDRvmvNRTTIVVAHRLSTIKN-ADVIAVVKNG 1255
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASL-TESEtavllDIIRDLKAH---GIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
400-627 |
2.09e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVV----SLIERFYDPQAGDVLIDGINLKEFQL----KWIRSKIGLVSQEPVL 471
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRTVQREGRLardiRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 472 FTA-SIKDNIAYGKEDATTEEIKAAAELANASKfvDKLPQGLdTMVG------EHGTQLSGGQKQRIAVARAILKDPRIL 544
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRTCFSWFTREQK--QRALQAL-TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 545 LLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDP-EGAYSQLIR 620
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHLYRSINR 254
|
....*..
gi 15226477 621 LQEEKKS 627
Cdd:PRK09984 255 VEENAKA 261
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
60-324 |
2.63e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 75.24 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIgnglgfpLMTLLFGDLIDAFGENQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMIS--GERQAAR 137
Cdd:cd18563 5 FLLMLLGTALGL-------VPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLArlGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 138 IRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLL 217
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFD-KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 218 VMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGV-IEGGSTGLGLGTLFL 296
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIrAEKLWATFFPLLTFL 236
|
250 260
....*....|....*....|....*....
gi 15226477 297 VVFCsyALAVWY-GGKLILDKGYTGGQVL 324
Cdd:cd18563 237 TSLG--TLIVWYfGGRQVLSGTMTLGTLV 263
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
395-602 |
2.99e-14 |
|
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: 73.46 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA---GDVLIDGINLKEFQLKwirSKIGLVSQ---- 467
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQ---KCVAYVRQddil 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 468 -------EPVLFTASIK-DNIAYGKEDATTEEIKAAAELAnaskfvdklpqglDTMVG-EHGTQLSGGQKQRIAVARAIL 538
Cdd:cd03234 93 lpgltvrETLTYTAILRlPRKSSDAIRKKRVEDVLLRDLA-------------LTRIGgNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKG 602
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
406-611 |
5.18e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPvlfTASIKDNIAYGK- 484
Cdd:PRK15112 33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQRISQi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 485 --------EDATTEEIKAAaeLANASKFVDKLPqgldtmvgEHGT----QLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:PRK15112 110 ldfplrlnTDLEPEQREKQ--IIETLRQVGLLP--------DHASyyphMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 553 LDAEservVQEALDRIMVNR------TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK15112 180 LDMS----MRSQLINLMLELqekqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
118-324 |
5.67e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 74.47 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 118 AAAFLQLSGWMISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMgekVGKAIQLLA---TFVG 194
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD-RRRTGDLLSRLTGDVGAIQDLL---VSGVLPLLTnllTLVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 195 GFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLV 274
Cdd:cd18564 145 MLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENR 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 275 TAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVL 324
Cdd:cd18564 225 KSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLL 274
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
406-612 |
1.01e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKST----VVSLIERfydpQAGDVLIDGINLKEFQL-KWIRSKIGLVSQEPVLFTA-SIKDN 479
Cdd:PRK10895 23 SLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 480 IAYG---KEDATTEEIKAAAELANASKFVDKLPQGLdtmvgehGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE 556
Cdd:PRK10895 99 LMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 557 S----ERVVQEALDRIMvnrTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK10895 172 SvidiKRIIEHLRDSGL---GVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
384-580 |
1.12e-13 |
|
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: 70.26 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFtypARPDEQIF-RGFSLFISSGTTVALVGQSGSGKSTVVSLI--------ERFYDPQAGDVLidginlkefq 454
Cdd:cd03223 1 IELENLSL---ATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgsGRIGMPEGEDLL---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 455 lkwirskigLVSQEPVLFTASIKDNIAYGKEDAtteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVA 534
Cdd:cd03223 68 ---------FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFA 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15226477 535 RAILKDPRILLLDEATSALDAESE----RVVQEALdrimvnrTTVV-VAHR 580
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEdrlyQLLKELG-------ITVIsVGHR 147
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
398-612 |
1.12e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.37 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF--YDPQAGDVLIDGINLKEFQLKwIRSKIGL----------- 464
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 -VSQEPVLFTASIKDNIAYGKEDAttEEIKAAAELANASKFVDKLPQGLDTMVGEhgtQLSGGQKQRIAVARAILKDPRI 543
Cdd:CHL00131 98 gVSNADFLRLAYNSKRKFQGLPEL--DPLEFLEIINEKLKLVGMDPSFLSRNVNE---GFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGShTELLKDPE 612
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AELAKELE 243
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
384-608 |
1.21e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.30 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPVL---FTasIKDNIA-----YGKEDATTEE-IKAAAELAnaskfvdKLPQGLDTMVGEhgtqLSGGQKQRIAVA 534
Cdd:PRK13537 84 VVPQFDNLdpdFT--VRENLLvfgryFGLSAAAARAlVPPLLEFA-------KLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1042-1207 |
1.22e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.39 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPArpdvQIFQ--DLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQ 1119
Cdd:PRK10522 323 LELRNVTFAYQD----NGFSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGLVSQEPILFNETIraniayGKGGDASESEIVSS--AELSNAHGFisglqqgydTMVGER--GIQLSGGQKQRVAIARA 1195
Cdd:PRK10522 399 FSAVFTDFHLFDQLL------GPEGKPANPALVEKwlERLKMAHKL---------ELEDGRisNLKLSKGQKKRLALLLA 463
|
170
....*....|..
gi 15226477 1196 IVKDPKVLLLDE 1207
Cdd:PRK10522 464 LAEERDILLLDE 475
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
128-278 |
1.36e-13 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 72.76 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 128 MISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLiqdaMGEKVGKAIQ-LLATFVGGF-VIAFVRG-- 203
Cdd:cd18590 61 MCTLSRLNLRLRHQLFSSLVQQDIGFFE-KTKTGDLTSRLSTDTTL----MSRSVALNANvLLRSLVKTLgMLGFMLSls 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 204 WLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYK 278
Cdd:cd18590 136 WQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYN 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1059-1261 |
1.37e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1059 IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNE-TIRAN 1137
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1138 IAYGKGGD--------ASESEIVSSAelSNAHGFISGLQQGYDTmvgergiqLSGGQKQRVAIARAIVKDPKVLLLDEAT 1209
Cdd:PRK10253 102 VARGRYPHqplftrwrKEDEEAVTKA--MQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1210 SALDAESERVVQDALDRvmVNR----TTIVVAHRLS-TIKNADVIAVVKNGVIVEKG 1261
Cdd:PRK10253 172 TWLDISHQIDLLELLSE--LNRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
384-612 |
1.40e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.98 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKST----VVSLIErfydPQAGDVLIDGINLKEFQLkWIR 459
Cdd:COG1137 4 LEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPM-HKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 460 SK--IGLVSQEPVLFTA-SIKDNIaygkedatteeiKAAAELANASKfvDKLPQGLDTMVGE----H-----GTQLSGGQ 527
Cdd:COG1137 76 ARlgIGYLPQEASIFRKlTVEDNI------------LAVLELRKLSK--KEREERLEELLEEfgitHlrkskAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 528 KQRIAVARAILKDPRILLLDEATSALD----AESERVVQEALDR-IMV-----N-RTTvvvahrLSTVRNAdmiAVIHQG 596
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKERgIGVlitdhNvRET------LGICDRA---YIISEG 212
|
250
....*....|....*.
gi 15226477 597 KIVEKGSHTELLKDPE 612
Cdd:COG1137 213 KVLAEGTPEEILNNPL 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1042-1262 |
1.53e-13 |
|
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: 71.59 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKY------------------PARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITL 1103
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1104 DGVEIKSLRLKWLRQQTGLVSQEPILF-----NETIRANIA-YGKGGDASESEIVSSAELSNahgfisgLQQGYDTMVge 1177
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQKTQLWwdlpvIDSFYLLAAiYDLPPARFKKRLDELSELLD-------LEELLDTPV-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1178 RgiQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVahrLSTIKNADVIAVVKNGVI 1257
Cdd:cd03267 152 R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVL---LTSHYMKDIEALARRVLV 226
|
....*
gi 15226477 1258 VEKGK 1262
Cdd:cd03267 227 IDKGR 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
384-603 |
1.54e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYP------------------ARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVL 444
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrTRREEfWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 445 IDGInlkefqlkwIRSKIGL---VSQEpvlFTAsiKDNI-----AYG---KE-DATTEEIKAAAELANAskfvdklpqgL 512
Cdd:COG1134 85 VNGR---------VSALLELgagFHPE---LTG--RENIylngrLLGlsrKEiDEKFDEIVEFAELGDF----------I 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 513 DTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE----SERVVQEALDRimvNRTTVVVAHRLSTVRN-A 587
Cdd:COG1134 141 DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlC 213
|
250
....*....|....*.
gi 15226477 588 DMIAVIHQGKIVEKGS 603
Cdd:COG1134 214 DRAIWLEKGRLVMDGD 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1053-1261 |
1.65e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1053 ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVI-ALLQRFYDPD-------SGEITLDG---VEIKSLRLKWLRQQTG 1121
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGeplAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFneTIRANIAYGK-------GGDASESEIVSSAELSNAhgfisglqqGYDTMVGERGIQLSGGQKQRVAIAR 1194
Cdd:PRK13547 90 QAAQPAFAF--SAREIVLLGRypharraGALTHRDGEIAWQALALA---------GATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1195 AIVK---------DPKVLLLDEATSALDAESERVVQDALDRVM----VNRTTIVVAHRLSTiKNADVIAVVKNGVIVEKG 1261
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHG 237
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1053-1222 |
1.82e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1053 ARPDVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRfydPDSGEITLDGVEIKSLRLK----WLRQQTGLvsq 1125
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTllrLIAGLLP---PAAGTIKLDGGDIDDPDVAeachYLGHRNAM--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1126 EPILfneTIRANIA-----YGkggdASESEIVSSAELSNAHGfISGLQQGYdtmvgergiqLSGGQKQRVAIARAIVKDP 1200
Cdd:PRK13539 85 KPAL---TVAENLEfwaafLG----GEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNR 146
|
170 180
....*....|....*....|..
gi 15226477 1201 KVLLLDEATSALDAESERVVQD 1222
Cdd:PRK13539 147 PIWILDEPTAALDAAAVALFAE 168
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
369-602 |
1.93e-13 |
|
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: 71.02 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 369 SYSTNGKVLDDIKGDIELKDVyftyPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGi 448
Cdd:cd03220 9 SYPTYKGGSSSLKKLGILGRK----GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 449 nlkefQLKWIrskIGL-VSQEPVLftaSIKDNIAY--------GKE-DATTEEIKAAAELANAskfvdklpqgLDTMVGE 518
Cdd:cd03220 84 -----RVSSL---LGLgGGFNPEL---TGRENIYLngrllglsRKEiDEKIDEIIEFSELGDF----------IDLPVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 519 hgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAE-SERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQG 596
Cdd:cd03220 143 ----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKG 218
|
....*.
gi 15226477 597 KIVEKG 602
Cdd:cd03220 219 KIRFDG 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
392-563 |
2.42e-13 |
|
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: 74.20 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 392 TYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIerfydpqAGdvlIDginlKEFQLKWIRS---KIGLVSQE 468
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD----KDFNGEARPQpgiKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 469 PVL-FTASIKDNI-------------------AYGKEDA----------TTEEIKAAAELANASKFVD------KLPQGl 512
Cdd:TIGR03719 77 PQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDAdfdklaaeqaELQEIIDAADAWDLDSQLEiamdalRCPPW- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 513 DTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES----ERVVQE 563
Cdd:TIGR03719 156 DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
385-599 |
2.46e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARPDEQI-----------FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEF 453
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVleveglsvggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 454 QLK----WIRSKIGLVS----QEPVLFTASIKDNIAYGKEDATTEE--IKAAAELANASKFVDKL---PQGLDTMVGehg 520
Cdd:COG1129 317 RIRsprdAIRAGIAYVPedrkGEGLVLDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLrikTPSPEQPVG--- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 521 tQLSGGQKQRIAVARAILKDPRILLLDEATSALD--AESE--RVVQEALDR----IMVnrttvvvahrlST-----VRNA 587
Cdd:COG1129 394 -NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRELAAEgkavIVI-----------SSelpelLGLS 461
|
250
....*....|..
gi 15226477 588 DMIAVIHQGKIV 599
Cdd:COG1129 462 DRILVMREGRIV 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1042-1240 |
4.82e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveikSLRLKWLRQQTG 1121
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 LVSQEPILFNETIRANIAYGKGGDASESEIVSSAELSNAhgfisGLQQgydtmvgergiqLSGGQKQRVAIARAIVKDPK 1201
Cdd:PRK09544 78 LDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDA-----PMQK------------LSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15226477 1202 VLLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRL 1240
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDL 181
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
403-602 |
4.87e-13 |
|
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: 70.05 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRsKIGLV--SQEPVLFTASIKDNI 480
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 481 AYGKEdatTEEIKAAAELANASKFVDKLPQG--LDTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:cd03267 117 YLLAA---IYDLPPARFKKRLDELSELLDLEelLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15226477 559 RVVQEALDRIMVNRTTVVV--AHRLSTV-RNADMIAVIHQGKIVEKG 602
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
404-597 |
4.93e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYdPQA---GDVLIDGinlKEFQLKWIR----SKIGLVSQEPVLFTA-S 475
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEG---EELQASNIRdterAGIAIIHQELALVKElS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYGKEDATTEEIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALdA 555
Cdd:PRK13549 99 VLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-T 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226477 556 ESERVVQEALDRIMVNR--TTVVVAHRLSTVRN-ADMIAVIHQGK 597
Cdd:PRK13549 176 ESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1059-1226 |
5.92e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1059 IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR------LKWLRQQTG----LVSQEPI 1128
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyhqdLLYLGHQPGikteLTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1129 LFNETIRaniaygkgGDASESEIVSSAELSNAHGFisglqqgYDTMVGergiQLSGGQKQRVAIARAIVKDPKVLLLDEA 1208
Cdd:PRK13538 96 RFYQRLH--------GPGDDEALWEALAQVGLAGF-------EDVPVR----QLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170
....*....|....*...
gi 15226477 1209 TSALDAESERVVQDALDR 1226
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQ 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1045-1258 |
7.06e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1045 RHVSFKYPARPDVQ--------------IFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDG--VEI 1108
Cdd:COG1129 239 RELEDLFPKRAAAPgevvleveglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1109 KS----LRLKwL------RQQTGLVSQEPILFNETIrANIA-YGKGGdaseseIVS-SAELSNAHGFISGLQ---QGYDT 1173
Cdd:COG1129 319 RSprdaIRAG-IayvpedRKGEGLVLDLSIRENITL-ASLDrLSRGG------LLDrRRERALAEEYIKRLRiktPSPEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1174 MVGergiQLSGGQKQRVAIARAIVKDPKVLLLDEATSALD--AESE--RVVQDALDRVMvnrtTIVVAhrlST-----IK 1244
Cdd:COG1129 391 PVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRELAAEGK----AVIVI---SSelpelLG 459
|
250
....*....|....
gi 15226477 1245 NADVIAVVKNGVIV 1258
Cdd:COG1129 460 LSDRILVMREGRIV 473
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
60-272 |
7.20e-13 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 70.90 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIgnglgfpLMTLLFGDLIDAFGENQTNTT----DKVSKVALKFVWLGIGTFAAAFLQlsGWMIS--GER 133
Cdd:cd18547 5 IILAIISTLLSV-------LGPYLLGKAIDLIIEGLGGGGgvdfSGLLRILLLLLGLYLLSALFSYLQ--NRLMArvSQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 134 QAARIRS-LYLKtILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLS 212
Cdd:cd18547 76 TVYDLRKdLFEK-LQRLPLSYFD-THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 213 SIPLLVmagaLLAIVIAKTASRG----QTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKH 272
Cdd:cd18547 154 TVPLSL----LVTKFIAKRSQKYfrkqQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEI 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
404-579 |
1.02e-12 |
|
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: 69.36 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGT-----TVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKeFQLKWIRSKiglvsqepvlFTASIKD 478
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD----------YEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 479 nIAYGKEDATTEEIKAAAELANaskfvdklPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:cd03237 81 -LLSSITKDFYTHPYFKTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180
....*....|....*....|...
gi 15226477 559 RVVQEALDRIMVN--RTTVVVAH 579
Cdd:cd03237 152 LMASKVIRRFAENneKTAFVVEH 174
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1054-1241 |
1.02e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.39 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1054 RPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQrFYDPD----SGEITLDGVEIKSlrlKWLRQQTGLVSQEPIL 1129
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDA---KEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1130 FNE-TIR------ANIAYGKGGDASES-EIVSsaELSNAhgfiSGLQQGYDTMVGERGIQ--LSGGQKQRVAIARAIVKD 1199
Cdd:TIGR00955 111 IPTlTVRehlmfqAHLRMPRRVTKKEKrERVD--EVLQA----LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15226477 1200 PKVLLLDEATSALDAES-ERVVQDALDRVMVNRTTIVVAHRLS 1241
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPS 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1027-1262 |
1.27e-12 |
|
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: 72.14 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1027 PSVESGRVLDNVKGDIELRHVSFKYPA--RPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITL- 1103
Cdd:TIGR03269 265 SEVEKECEVEVGEPIIKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVr 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1104 ---DGVEIKSLRLKW---LRQQTGLVSQEPILF-NETIRANIAYGKGGDASEseivssaELSNAHGFISGLQQGYDTMVG 1176
Cdd:TIGR03269 345 vgdEWVDMTKPGPDGrgrAKRYIGILHQEYDLYpHRTVLDNLTEAIGLELPD-------ELARMKAVITLKMVGFDEEKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1177 ERGI-----QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDAL--DRVMVNRTTIVVAHRLSTIKN-ADV 1248
Cdd:TIGR03269 418 EEILdkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDR 497
|
250
....*....|....
gi 15226477 1249 IAVVKNGVIVEKGK 1262
Cdd:TIGR03269 498 AALMRDGKIVKIGD 511
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
406-628 |
1.29e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKS----TVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG----LVSQEPVlftASIk 477
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPM---TSL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 478 dNIAYGKEDATTEEIKA---AAELANASKFVDKLpqgldTMVG-----------EHgtQLSGGQKQRIAVARAILKDPRI 543
Cdd:PRK11022 103 -NPCYTVGFQIMEAIKVhqgGNKKTRRQRAIDLL-----NQVGipdpasrldvyPH--QLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMV--NRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQ-LI 619
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQaLL 254
|
....*....
gi 15226477 620 RLQEEKKSD 628
Cdd:PRK11022 255 RALPEFAQD 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1054-1261 |
1.32e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1054 RPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVeikslrlkWLRQQtglvSQEPILFNET 1133
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKM--------LLRRR----SRQVIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1134 IRANIAYGKGGDASE----------------SEIVSSAELSNAHGFISGLQQG-----------YDTMVGERGIQLSGGQ 1186
Cdd:PRK10261 94 SAAQMRHVRGADMAMifqepmtslnpvftvgEQIAESIRLHQGASREEAMVEAkrmldqvripeAQTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1187 KQRVAIARAIVKDPKVLLLDEATSALDAESE-------RVVQDALDrvmvnRTTIVVAHRLSTIKN-ADVIAVVKNGVIV 1258
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMS-----MGVIFITHDMGVVAEiADRVLVMYQGEAV 248
|
...
gi 15226477 1259 EKG 1261
Cdd:PRK10261 249 ETG 251
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
405-617 |
1.37e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.52 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 405 FSLfiSSGTTVALVGQSGSGKS-TVVSLIERFydpqAGDVLIDG---------INLKEFQLKWIRS-KIGLVSQEPVlfT 473
Cdd:PRK09473 37 FSL--RAGETLGIVGESGSGKSqTAFALMGLL----AANGRIGGsatfngreiLNLPEKELNKLRAeQISMIFQDPM--T 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 474 A-----SIKDNIA--------YGKEDATTEEIKA--AAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAIL 538
Cdd:PRK09473 109 SlnpymRVGEQLMevlmlhkgMSKAEAFEESVRMldAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKreFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
..
gi 15226477 616 SQ 617
Cdd:PRK09473 258 SI 259
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1063-1264 |
1.53e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1063 LCLSIRAGKTVALVGESGSGKSTVIA----LLqrfydPDSGEITLDGVEIKSLRLKWL-RQQTGLVSQEPILFN----ET 1133
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAmpvfQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1134 IRANIAYGKGGDASESEIVSSAELSnahgfisGLQQGYDTMVGergiQLSGGQKQRVAIA-------RAIVKDPKVLLLD 1206
Cdd:PRK03695 90 LTLHQPDKTRTEAVASALNEVAEAL-------GLDDKLGRSVN----QLSGGEWQRVRLAavvlqvwPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1207 EATSALDaeserVVQD-ALDRVMV-----NRTTIVVAHRLS-TIKNADVIAVVKNGVIVEKGKHD 1264
Cdd:PRK03695 159 EPMNSLD-----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRD 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1058-1255 |
2.77e-12 |
|
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: 66.88 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1058 QIFQDLCLSIRAGKTVALVGESGSGKSTVIALL-QRFYDPD-SGEITLDGVEIKslrlKWLRQQTGLVSQEPILF-NETI 1134
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLD----KNFQRSTGYVEQQDVHSpNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1135 RANIAYgkggdaseseivsSAELsnahgfisglqqgydtmvgeRGiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDA 1214
Cdd:cd03232 97 REALRF-------------SALL--------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15226477 1215 ESERVVQDALDRV-MVNRTTIVVAHRLS--TIKNADVIAVVKNG 1255
Cdd:cd03232 142 QAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1055-1259 |
3.11e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.59 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1055 PDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDS--GEITLDG--VEIKSLRLKwlrQQTGLV--SQE-- 1126
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevCRFKDIRDS---EALGIViiHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1127 --PILfneTIRANIAYG----KGG--DASESEIVSSAELSNAhgfisGLQQGYDTMVGERGIqlsgGQKQRVAIARAIVK 1198
Cdd:NF040905 89 liPYL---SIAENIFLGneraKRGviDWNETNRRARELLAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1199 DPKVLLLDEATSAL-DAESERVvqdaLDRVMVNR----TTIVVAHRLSTI-KNADVIAVVKNGVIVE 1259
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
405-620 |
3.28e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.16 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 405 FSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQ----AGDVLIDGINL-----KEfQLKWIRSKIGLVSQEPVLF--- 472
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLlklspRE-RRKIIGREIAMIFQEPSSCldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 473 TASIKDNIaygKEDATTEEIK------------AAAEL------ANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVA 534
Cdd:COG4170 105 SAKIGDQL---IEAIPSWTFKgkwwqrfkwrkkRAIELlhrvgiKDHKDIMNSYPH-----------ELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV--VAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIllISHDLESIsQWADTITVLYCGQTVESGPTEQILKSP 250
|
250
....*....|
gi 15226477 612 EGAYSQ-LIR 620
Cdd:COG4170 251 HHPYTKaLLR 260
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1066-1238 |
3.30e-12 |
|
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: 67.82 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1066 SIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIkSLRLKWLR-QQTGLVSQepILFNETIRA-NIAYGKg 1143
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKaDYEGTVRD--LLSSITKDFyTHPYFK- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1144 gdaseSEIVSSAelsnahgfisGLQQGYDTMVGErgiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDA 1223
Cdd:cd03237 97 -----TEIAKPL----------QIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170
....*....|....*..
gi 15226477 1224 LDRVMVN--RTTIVVAH 1238
Cdd:cd03237 158 IRRFAENneKTAFVVEH 174
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1053-1217 |
3.70e-12 |
|
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: 66.75 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1053 ARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNE 1132
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1133 TIRANIAYGKGgDASESEIVSSAELSNAHGFisglqqgYDTMVGergiQLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1212
Cdd:cd03231 89 SVLENLRFWHA-DHSDEQVEEALARVGLNGF-------EDRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
....*
gi 15226477 1213 DAESE 1217
Cdd:cd03231 157 DKAGV 161
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
64-340 |
4.05e-12 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 68.59 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 64 ILGTLGSIGNGLGFPLMTLLFGDLIDAFgENQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLYL 143
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDAL-TAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 144 KTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVgkaIQLL-ATFVGGFVIA--FVRGWLLTLVMLSSIPLLVMA 220
Cdd:cd18541 81 AHLLTLSPSFYQ-KNRTGDLMARATNDLNAVRMALGPGI---LYLVdALFLGVLVLVmmFTISPKLTLIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 221 GALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFC 300
Cdd:cd18541 157 VYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15226477 301 SYALAVWYGGKLILDKGYTGGQV--LNIIIAVLTGSM-SLGQT 340
Cdd:cd18541 237 SFLIVLWYGGRLVIRGTITLGDLvaFNSYLGMLIWPMmALGWV 279
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
761-921 |
4.43e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 68.69 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 761 FWAIIFMVLGFA---SIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVG 837
Cdd:cd18564 53 LLLAAAALVGIAllrGLASY-AGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRLTGDVGAIQDLLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 838 DSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASF 917
Cdd:cd18564 130 SGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAF 209
|
....
gi 15226477 918 CAED 921
Cdd:cd18564 210 GREE 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
395-609 |
5.66e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVV-SLIERFYDPQA-------GDVLIDGINLKEF---QLKWIRSKIG 463
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIdapRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQEPvlFTASIKDNIAYGK----------EDATTEEIKAAAELANAskfvdklpqglDTMVGEHGTQLSGGQKQRIAV 533
Cdd:PRK13547 90 QAAQPA--FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 534 ARAILK---------DPRILLLDEATSALDAESERVVQEALDRIMV--NRTTVVVAHRLS-TVRNADMIAVIHQGKIVEK 601
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAH 236
|
....*...
gi 15226477 602 GSHTELLK 609
Cdd:PRK13547 237 GAPADVLT 244
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
763-921 |
6.49e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 67.98 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 763 AIIFMVLGFASIIAYPAQTFFFAIAGcKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQ 842
Cdd:cd18565 58 GLTVAAFLLESLFQYLSGVLWRRFAQ-RVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANS 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 843 TVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18565 135 IIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAED 213
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
116-323 |
6.92e-12 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 67.88 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 116 TFAAAFLQLSG---WMISGERQAARIRSLYLKTILRQDIAFFDIDtNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATF 192
Cdd:cd18589 46 TIASAVSEFVCdliYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN-QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 193 VGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKH 272
Cdd:cd18589 125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 273 LVTAYKagvIEGGSTGLGLGTLFLVVFCSYALAV---WYGGKLIldkgyTGGQV 323
Cdd:cd18589 205 LQKTYR---LNKKEAAAYAVSMWTSSFSGLALKVgilYYGGQLV-----TAGTV 250
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1060-1265 |
7.88e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1060 FQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI-KSLR---LKWLRQQTGLVSQEPILFNETIR 1135
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrQALQknlVAYVPQSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1136 ANiAYGKGG-----DASESEIVSSAeLSNAhgfisGLQQGYDTMVGErgiqLSGGQKQRVAIARAIVKDPKVLLLDEATS 1210
Cdd:PRK15056 103 MG-RYGHMGwlrraKKRDRQIVTAA-LARV-----DMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1211 ALDAESERVVQDALDRVMVN-RTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDT 1265
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
404-594 |
1.12e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLF----ISSGTTVALVGQSGSGKSTVVSL---------------------IERFydpqAGDVLIDGI-NLKEFQLKW 457
Cdd:PRK13409 87 GFKLYglpiPKEGKVTGILGPNGIGKTTAVKIlsgelipnlgdyeeepswdevLKRF----RGTELQNYFkKLYNGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 458 IRsKIGLVSQEPVLFTASIKdniaygkedattEEIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:PRK13409 163 VH-KPQYVDLIPKVFKGKVR------------ELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 538 LKDPRILLLDEATSALDAEsERV-VQEALDRIMVNRTTVVVAHRLSTVrnaDMIA-VIH 594
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVL---DYLAdNVH 282
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1058-1250 |
1.36e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1058 QIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRL-KWLRQQTGLVSQEPILFN----- 1131
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRrlsvy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1132 ETIRANIAYGKGGDASESEIVSSAELSNAHgfISGLQqgyDTMvgerGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSA 1211
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEQREDRANELMEEFH--IEHLR---DSM----GQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 1212 LDAES----ERVVQDALDR---VMVN----RTTIVVAHRLSTIKNADVIA 1250
Cdd:PRK10895 168 VDPISvidiKRIIEHLRDSglgVLITdhnvRETLAVCERAYIVSQGHLIA 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
384-607 |
1.42e-11 |
|
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: 68.68 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF--YDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IG---------LVSQEPVLF------TASIKDNIA---------YGKEDATTEEIKAAAELA-NASKFVDKLPQGLDTMV 516
Cdd:TIGR03269 78 VGepcpvcggtLEPEEVDFWnlsdklRRRIRKRIAimlqrtfalYGDDTVLDNVLEALEEIGyEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 517 GEH-----GTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTVRN-AD 588
Cdd:TIGR03269 158 LSHrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSD 237
|
250
....*....|....*....
gi 15226477 589 MIAVIHQGKIVEKGSHTEL 607
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
400-608 |
1.57e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIerFYDPQA--GDVLIDGINLKEFQLKWI-RSKIGLVSQEPVLFT-AS 475
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDITDWQTAKImREAVAIVPEGRRVFSrMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYGKEDATTEEIKAAAElanasKFVDKLPQGLDTMVGEHGTqLSGGQKQRIAVARAILKDPRILLLDEATSALda 555
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERIK-----WVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL-- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 556 eSERVVQEALDRIMVNR----TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK11614 169 -APIIIQQIFDTIEQLReqgmTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
716-978 |
1.63e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 66.72 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 716 EIPVLILGSISAAANGVILPIF-GILISSVIkaffqPPKKLKEDTsFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQR 794
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLiKIAIDEYI-----PNGDLSGLL-IIALLFLALNLVNWVASRLRIYLMAKVGQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 795 IRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPL 874
Cdd:cd18545 75 LRQDLFSHLQKLSFSFFDS--RPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 875 IALNGFLYMKFM-KGFSADAKKMYGEASQVANDAVGsIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIgfgFSF 953
Cdd:cd18545 153 LVLVVFLLRRRArKAWQRVRKKISNLNAYLHESISG-IRVIQSFAREDENEEIFDELNRENRKANMRAVRLNAL---FWP 228
|
250 260
....*....|....*....|....*...
gi 15226477 954 FVLFSS---YAASFYVGARLVDDGKTTF 978
Cdd:cd18545 229 LVELISalgTALVYWYGGKLVLGGAITV 256
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1046-1213 |
1.89e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1046 HVSFKYPaRPDVQIFQDLCLSIRAGKTVALVGESGSGKS-TVIALLQRFYDPD--SGEITLDGVEIKSLRLKWLR----Q 1118
Cdd:PRK09473 19 RVTFSTP-DGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLPEKELNklraE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 QTGLVSQEPIL-FNetiraniAYGKGGDASESEIVSSAELSNAHGFISGLQqgydtMVGERGI------------QLSGG 1185
Cdd:PRK09473 98 QISMIFQDPMTsLN-------PYMRVGEQLMEVLMLHKGMSKAEAFEESVR-----MLDAVKMpearkrmkmyphEFSGG 165
|
170 180
....*....|....*....|....*...
gi 15226477 1186 QKQRVAIARAIVKDPKVLLLDEATSALD 1213
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1060-1261 |
1.94e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1060 FQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDG-----VEIKSL----RLKWLRQQTGLVSQEPilf 1130
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALseaeRRRLLRTEWGFVHQHP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1131 NETIR------ANIA----------YGKGGDASeSEIVSSAELSNAHgfisglqqgydtmVGERGIQLSGGQKQRVAIAR 1194
Cdd:PRK11701 99 RDGLRmqvsagGNIGerlmavgarhYGDIRATA-GDWLERVEIDAAR-------------IDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1195 AIVKDPKVLLLDEATSALDAEservVQ----DALdRVMVNR---TTIVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1261
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVS----VQarllDLL-RGLVRElglAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
384-600 |
2.11e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpdeqifrGFS-----LFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWI 458
Cdd:PRK10522 323 LELRNVTFAYQDN-------GFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 459 RSKIGLVSQEPVLFTASIKDniaygkeDATTEEIKAAAELANASKFVDKLpqgldTMVGEH--GTQLSGGQKQRIAVARA 536
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQLLGP-------EGKPANPALVEKWLERLKMAHKL-----ELEDGRisNLKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 537 ILKDPRILLLDEATSALDAESERVV-QEALD--RIMvNRTTVVVAHRLSTVRNADMIAVIHQGKIVE 600
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFyQVLLPllQEM-GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
384-548 |
2.26e-11 |
|
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: 67.90 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPDEQIFR-G-FSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTlGpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTAsikdniAYGKEDATTEEiKAAA-----ELANASKFVDklpQGLDTmvgehgTQLSGGQKQRIAVARA 536
Cdd:COG4615 408 FSAVFSDFHLFDR------LLGLDGEADPA-RAREllerlELDHKVSVED---GRFST------TDLSQGQRKRLALLVA 471
|
170
....*....|..
gi 15226477 537 ILKDPRILLLDE 548
Cdd:COG4615 472 LLEDRPILVFDE 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
401-600 |
3.25e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFY--DPQAGDVLIDGINLkefqlkwirskiglvSQEpvlftASIKD 478
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 479 NIAygkedaTTEEIKAAAELANASKFVDklPQGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:COG2401 105 AIG------RKGDFKDAVELLNAVGLSD--AVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15226477 559 RVVQEALDRIM--VNRTTVVVAHRlSTVRNA---DMIAVIHQGKIVE 600
Cdd:COG2401 173 KRVARNLQKLArrAGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
392-557 |
3.43e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 392 TYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIerfydpqAGdvlIDginlKEFQLKWIRS---KIGLVSQE 468
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD----KEFEGEARPApgiKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 469 PVL-FTASIKDNI-------------------AYGKEDATT----------EEIKAAAELANASKFVD------KLPQGl 512
Cdd:PRK11819 79 PQLdPEKTVRENVeegvaevkaaldrfneiyaAYAEPDADFdalaaeqgelQEIIDAADAWDLDSQLEiamdalRCPPW- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226477 513 DTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 557
Cdd:PRK11819 158 DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1033-1225 |
3.93e-11 |
|
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: 67.27 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1033 RVLDNVkgdIELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDgveiKSLR 1112
Cdd:TIGR03719 317 RLGDKV---IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1113 LKWLRQqtglvSQEPILFNETIRANIAYG----KGGDAsesEIVSSAELSnAHGFISGLQQgydTMVGergiQLSGGQKQ 1188
Cdd:TIGR03719 387 LAYVDQ-----SRDALDPNKTVWEEISGGldiiKLGKR---EIPSRAYVG-RFNFKGSDQQ---KKVG----QLSGGERN 450
|
170 180 190
....*....|....*....|....*....|....*..
gi 15226477 1189 RVAIARAIVKDPKVLLLDEATSALDAESERVVQDALD 1225
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1065-1266 |
4.60e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.88 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEIT-----LDGVEIKSLRLKwlRQQTGLVSQEPiLFNETIRANIa 1139
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdLLGMKDDEWRAV--RSDIQMIFQDP-LASLNPRMTI- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1140 ygkgGDA-SESEIVSSAELSNAHgfisgLQQGYDTMVGERGI----------QLSGGQKQRVAIARAIVKDPKVLLLDEA 1208
Cdd:PRK15079 118 ----GEIiAEPLRTYHPKLSRQE-----VKDRVKAMMLKVGLlpnlinryphEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1209 TSALDAESE-RVVQ--DALDRVMvNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTL 1266
Cdd:PRK15079 189 VSALDVSIQaQVVNllQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1046-1247 |
5.33e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1046 HVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQ 1125
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1126 EPILFNETIRANIAYG---KGGDASESEIVSSAELSNAHGFISGLqqgydtmvgergiqLSGGQKQRVAIARAIVKDPKV 1202
Cdd:PRK13540 83 SGINPYLTLRENCLYDihfSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15226477 1203 LLLDEATSALDaesERVVQDALDRVMVNR----TTIVVAHRLSTIKNAD 1247
Cdd:PRK13540 149 WLLDEPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQDLPLNKAD 194
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
404-594 |
6.52e-11 |
|
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: 64.31 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLF----ISSGTTVALVGQSGSGKSTVVSLIE--------RFYDPQAGDVLID---GINLKEF-------QLKWIRsK 461
Cdd:cd03236 14 SFKLHrlpvPREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYftkllegDVKVIV-K 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 462 IGLVSQEPVLFTASIKDNIaygkedatteeiKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:cd03236 93 PQYVDLIPKAVKGKVGELL------------KKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 542 RILLLDEATSALDAESE----RVVQEaldRIMVNRTTVVVAHRLSTVrnaDMIA-VIH 594
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRlnaaRLIRE---LAEDDNYVLVVEHDLAVL---DYLSdYIH 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1066-1250 |
7.11e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.35 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1066 SIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDgveikslrLKwlrqqtglVSQEP----ILFNETIRANI--A 1139
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--------LK--------ISYKPqyisPDYDGTVEEFLrsA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1140 YGKGGDAS--ESEIVSSAelsnahgfisGLQQGYDTMVGErgiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE 1217
Cdd:COG1245 426 NTDDFGSSyyKTEIIKPL----------GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190
....*....|....*....|....*....|....*
gi 15226477 1218 RVVQDALDRVMVNR--TTIVVAHRLSTIknaDVIA 1250
Cdd:COG1245 492 LAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1067-1263 |
7.22e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1067 IRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDgVEI--KSLRLKwlRQQTGLVSQepILFNETIRANIAYGKgg 1144
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIsyKPQYIK--PDYDGTVED--LLRSITDDLGSSYYK-- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1145 daseSEIVssaelsnaHGFisGLQQGYDTMVGErgiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDAL 1224
Cdd:PRK13409 435 ----SEII--------KPL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15226477 1225 DRVMVNR--TTIVVAHRLSTIknaDVIAvvkNGVIV---EKGKH 1263
Cdd:PRK13409 497 RRIAEEReaTALVVDHDIYMI---DYIS---DRLMVfegEPGKH 534
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1044-1222 |
1.02e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.11 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1044 LRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITL-DGVEIkslrlkwlrqqtGL 1122
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV------------GY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1123 VSQEPILFNE-TIRANI-------------------AYGKGGDASESEIVSSAEL------SNAHGFISGLQQGYDTM-- 1174
Cdd:TIGR03719 73 LPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAAEQAELqeiidaADAWDLDSQLEIAMDALrc 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1175 -VGERGIQ-LSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES----ERVVQD 1222
Cdd:TIGR03719 153 pPWDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
390-599 |
1.05e-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: 62.67 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 390 YFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKST----VVSLIERFYDPQaGDVLIDGINLKEFQLKWiRSKIGLV 465
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKY-PGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 466 SQE----PVLftasikdniaygkedaTTEE-IKAAAELaNASKFVDKLpqgldtmvgehgtqlSGGQKQRIAVARAILKD 540
Cdd:cd03233 89 SEEdvhfPTL----------------TVREtLDFALRC-KGNEFVRGI---------------SGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 541 PRILLLDEATSALDAEServvqeALDRIMVNRTtvvVAHRLSTVRNA-------------DMIAVIHQGKIV 599
Cdd:cd03233 137 ASVLCWDNSTRGLDSST------ALEILKCIRT---MADVLKTTTFVslyqasdeiydlfDKVLVLYEGRQI 199
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
761-977 |
1.61e-10 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 63.58 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 761 FWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSL 840
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRMALGPGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 841 AQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAE 920
Cdd:cd18541 119 LYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 921 DKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18541 199 EAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTIT 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
404-594 |
1.77e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLF----ISSGTTVALVGQSGSGKSTVVS-----LIERFYDPQAgDVLIDGInLKEFQ-------LKWIRS------- 460
Cdd:COG1245 87 GFRLYglpvPKKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDE-EPSWDEV-LKRFRgtelqdyFKKLANgeikvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 461 KIGLVSQEPVLFTASIKdniaygkedattEEIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:COG1245 165 KPQYVDLIPKVFKGTVR------------ELLEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 541 PRILLLDEATSALD----AESERVVQEALDRimvNRTTVVVAHRLSTVrnaDMIA-VIH 594
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAIL---DYLAdYVH 283
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
398-653 |
1.94e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.19 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDV-LIDGINLKEF---QLKWIRSkiglvSQEPVLFT 473
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFaqhQLEFLRA-----DESPLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 474 ASIkdniaygkedatteeikaaAELANASKFVDKLP----QGldTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEA 549
Cdd:PRK10636 399 ARL-------------------APQELEQKLRDYLGgfgfQG--DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 550 TSALDAESERVVQEALdrIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKiVEkgSHTELLKDpegaYSQ-LIRLQEEKKS 627
Cdd:PRK10636 458 TNHLDLDMRQALTEAL--IDFEGALVVVSHDRHLLRStTDDLYLVHDGK-VE--PFDGDLED----YQQwLSDVQKQENQ 528
|
250 260
....*....|....*....|....*.
gi 15226477 628 DENAAEEQKMSSIESFKQSSLRKSSL 653
Cdd:PRK10636 529 TDEAPKENNANSAQARKDQKRREAEL 554
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
395-563 |
2.08e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKWIRSKIGLVSQ----EPV 470
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHrnamKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 LftaSIKDNIA-----YGKEDATTEEIKAAAELANaskfVDKLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILL 545
Cdd:PRK13539 88 L---TVAENLEfwaafLGGEELDIAAALEAVGLAP----LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWI 150
|
170
....*....|....*...
gi 15226477 546 LDEATSALDAESERVVQE 563
Cdd:PRK13539 151 LDEPTAALDAAAVALFAE 168
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
404-612 |
2.10e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.70 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIrSKIGLVS--QEPVLF---TA---- 474
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFremTVienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 ------SIKDNIAYGKEdATTEEIKAAAE-LANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLD 547
Cdd:PRK11300 102 lvaqhqQLKTGLFSGLL-KTPAFRRAESEaLDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 548 EATSALDAESERVVQEALD--RIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1060-1213 |
2.36e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1060 FQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSL----RLK----WL---RQQTGLVSQEPI 1128
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALstaqRLArglvYLpedRQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1129 LFNetiraniaygkggdaseseivSSAELSNAHGFIsgLQQGYDTMVGER-----GIQ----------LSGGQKQRVAIA 1193
Cdd:PRK15439 359 AWN---------------------VCALTHNRRGFW--IKPARENAVLERyrralNIKfnhaeqaartLSGGNQQKVLIA 415
|
170 180
....*....|....*....|
gi 15226477 1194 RAIVKDPKVLLLDEATSALD 1213
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVD 435
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1070-1260 |
2.61e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.08 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1070 GKTVALVGESGSGKSTVIALLQRFYDPDSGE-ITLDGVEIKSLRLKWLRQqtglvsqepilfnetiraniaygkggdase 1148
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1149 seivssaelsnahgfisglqqgydTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM 1228
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 15226477 1229 V------NRTTIVVAHRLSTIKNADVIAVVKNGVIVEK 1260
Cdd:smart00382 108 LlllkseKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
404-599 |
2.64e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYdPQA---GDVLIDGINLKEFQLKWIRSK-IGLVSQEPVLF-TASIKD 478
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpELSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 479 NIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL-DAES 557
Cdd:TIGR02633 98 NIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEKET 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15226477 558 ERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIV 599
Cdd:TIGR02633 178 EILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
396-567 |
3.55e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 396 RPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLK----EF--QLKWIRSKIG----LV 465
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYhqDLLYLGHQPGikteLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 466 SQEPVLFTASIKDniaygkeDATTEEIKAAAELANASKFVDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILL 545
Cdd:PRK13538 91 ALENLRFYQRLHG-------PGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWI 152
|
170 180
....*....|....*....|..
gi 15226477 546 LDEATSALDAESERVVQEALDR 567
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQ 174
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1056-1261 |
3.80e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1056 DVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALlQRFYDPDSGEITLDGVEIKSLRLKwLRQQTG--LVSQEPILF 1130
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTlskVIAG-HPAYKILEGDILFKGESILDLEPE-ERAHLGifLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1131 NETIRAN---IAYG---KGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGiqLSGGQKQRVAIARAIVKDPKVLL 1204
Cdd:CHL00131 97 PGVSNADflrLAYNskrKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1205 LDEATSALDAESERVVQDALDRVMVNRTTIV-VAH--RLSTIKNADVIAVVKNGVIVEKG 1261
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
763-977 |
3.83e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 62.51 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 763 AIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQ 842
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHER--ETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 843 TVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALngflymkFMKGFSADAKKMYGEA-SQVAN------DAVGSIRTVA 915
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-------ATRWFRRRSSRAYRRArERIAAvnadlqETLAGIRVVQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 916 SFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18546 193 AFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLT 254
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1042-1267 |
3.84e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.82 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYParpDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRL-KWLRQQT 1120
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPILFNE-TIRANIAYGkGGDASESEIvsSAELSNAHGFISGLQqgydtmvgERGIQ----LSGGQKQRVAIARA 1195
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMG-GFFAERDQF--QERIKWVYELFPRLH--------ERRIQragtMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1196 IVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLS--TIKNADVIAVVKNGVIVEKGKHDTLI 1267
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1070-1242 |
4.48e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1070 GKTVALVGESGSGKSTVI-ALLQRFYDPD-SGEITLDGVEIKSLRLKwlrqQTGLVSQEPILFNE-TIRANIAYGKGGDA 1146
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYPHlTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1147 SESeIVSSAELSNAHGFIS--GLQQGYDTMVGE---RGIqlSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE-RVV 1220
Cdd:PLN03211 170 PKS-LTKQEKILVAESVISelGLTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLV 246
|
170 180
....*....|....*....|..
gi 15226477 1221 QDALDRVMVNRTTIVVAHRLST 1242
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSS 268
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
416-600 |
4.58e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 416 ALVGQSGSGKST---VVSLIERF--YDpqaGDVLIDGinlKEFQLKWIRS--KIGLV--SQE----PVLftaSIKDNIAY 482
Cdd:NF040905 31 ALCGENGAGKSTlmkVLSGVYPHgsYE---GEILFDG---EVCRFKDIRDseALGIViiHQElaliPYL---SIAENIFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 483 GKEDATTEEIKAAAELANASKFVDKLpqGL----DTMVGEHGTqlsgGQKQRIAVARAILKDPRILLLDEATSAL-DAES 557
Cdd:NF040905 102 GNERAKRGVIDWNETNRRARELLAKV--GLdespDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAALnEEDS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226477 558 ERVvqeaLDRIMVNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVE 600
Cdd:NF040905 176 AAL----LDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
762-995 |
4.77e-10 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 62.03 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 762 WAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLA 841
Cdd:cd18548 41 TGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDK--FGTSSLITRLTNDVTQVQNFVMMLLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 842 QTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18548 119 MLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNRED 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 922 KVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSV-------FRVFFALTMAAMA 994
Cdd:cd18548 199 YEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSMV 278
|
.
gi 15226477 995 I 995
Cdd:cd18548 279 F 279
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1065-1277 |
5.87e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.54 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQtGLVS--QEPILFNE-TIRANIayg 1141
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQHVRLFREmTVIENL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1142 kggdaseseIVSSAELSNAhGFISGL----------------------QQGYDTMVGERGIQLSGGQKQRVAIARAIVKD 1199
Cdd:PRK11300 102 ---------LVAQHQQLKT-GLFSGLlktpafrraesealdraatwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1200 PKVLLLDEATSALDAESERVVQDALD--RVMVNRTTIVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTLINIKDGVYAS 1276
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVIKAY 251
|
.
gi 15226477 1277 L 1277
Cdd:PRK11300 252 L 252
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
719-977 |
8.29e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 61.34 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 719 VLILGSISAAAnGVILPIfgiLISSVI-KAFFQPpkklkeDTS--FWAIIFMV-LGFASIIAYPAQTFFFAIAGCKLVQR 794
Cdd:cd18550 4 VLLLILLSALL-GLLPPL---LLREIIdDALPQG------DLGllVLLALGMVaVAVASALLGVVQTYLSARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 795 IRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPL 874
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTR--TRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 875 IALNGFLYMKFMKGFSADAKKMYGEASQVAND--AVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVsGIGFGFS 952
Cdd:cd18550 152 FVLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALA-GRWFFAA 230
|
250 260
....*....|....*....|....*.
gi 15226477 953 FFVLFSSYAASFY-VGARLVDDGKTT 977
Cdd:cd18550 231 LGLFTAIGPALVYwVGGLLVIGGGLT 256
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1044-1216 |
1.31e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1044 LRHVSFKYParPDVQIFQDLCLSIRAGKTVALVGESGSGKSTV---IALLqrfyDPDS-GEITL-DGVEIkslrlkwlrq 1118
Cdd:PRK11819 9 MNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLlriMAGV----DKEFeGEARPaPGIKV---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1119 qtGLVSQEPILFNE-TIRANI-------------------AYGKGGDASESEIVSSAEL------SNAHGFISGLQQG-- 1170
Cdd:PRK11819 73 --GYLPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFDALAAEQGELqeiidaADAWDLDSQLEIAmd 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1171 ------YDTMVGergiQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES 1216
Cdd:PRK11819 151 alrcppWDAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
398-622 |
1.59e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI--ERFYDPQAGDVLIDGINLKEFQLKWIRSK-IGLVSQEPV---- 470
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVeipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 ----LFTASIKDNIAYGKEDATTEEIKAAAELANASKFVdKLPQGLDTMVGEHGtqLSGGQKQRIAVARAILKDPRILLL 546
Cdd:PRK09580 93 vsnqFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALL-KMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 547 DEATSALDAESERVVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLIRLQ 622
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGYGWLTEQQ 248
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
398-572 |
1.68e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLK------EFQLKWIRSKIGLvsqEPVL 471
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlctyQKQLCFVGHRSGI---NPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 472 ftaSIKDNIAYGKEDATTE-EIKAAAELANASKFVDkLPQGLdtmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEAT 550
Cdd:PRK13540 90 ---TLRENCLYDIHFSPGAvGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180
....*....|....*....|..
gi 15226477 551 SALDaesERVVQEALDRIMVNR 572
Cdd:PRK13540 156 VALD---ELSLLTIITKIQEHR 174
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
719-930 |
2.21e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 60.22 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 719 VLILGSISAAANGVILPIFGILISSVIKAffqppkkLKEDTSFWAIIFMVLGFASI-----IAYPAQTFFFAIAGCKLVQ 793
Cdd:cd18563 4 GFLLMLLGTALGLVPPYLTKILIDDVLIQ-------LGPGGNTSLLLLLVLGLAGAyvlsaLLGILRGRLLARLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 794 RIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLP 873
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDK--RQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 874 LIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKK 930
Cdd:cd18563 155 LVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEA 211
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
714-986 |
2.69e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 59.80 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 714 KPEIPVLILGSISAAANGVILPIFgilISSVIKAFFQPpkklKEDTSFWAIIFMVLGFASIIAypAQTFFFAIAGCKL-- 791
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLL---TKYAIDHFITP----GTLDGLTGFILLYLGLILIQA--LSVFLFIRLAGKIem 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 792 -VQR-IRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVL 869
Cdd:cd18540 72 gVSYdLRKKAFEHLQTLSFSYFDK--TPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 870 AMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEgPMKN-GIRQGIVSGIg 948
Cdd:cd18540 150 AVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTE-EMRRaSVRAARLSAL- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15226477 949 fgFSFFVLFSSYAAS---FYVGARLVDDGKTTFdSVFRVFF 986
Cdd:cd18540 228 --FLPIVLFLGSIATalvLWYGGILVLAGAITI-GTLVAFI 265
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
714-977 |
2.77e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 59.77 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 714 KPEIPVLILGSISAAANGVILPIF-GILISSVIkaffqpPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLV 792
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFfQILIDDII------PSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 793 QRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSaDAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAML 872
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFET--RKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLII 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 873 PLIALNGFLYMKFMKgfSADAKKMYGEASQVAN--DAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFG 950
Cdd:cd18570 152 PLYILIILLFNKPFK--KKNREVMESNAELNSYliESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSS 229
|
250 260
....*....|....*....|....*..
gi 15226477 951 FSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18570 230 IKGLISLIGSLLILWIGSYLVIKGQLS 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1066-1262 |
6.56e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1066 SIRAGKTVALVGESGSGKST---VIALLQRFYDPDSGE-ITLDGVEIKSLRLKWLRQQTGlvSQEPILFNETIRA-NIAY 1140
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVsslAIMGLIDYPGRVMAEkLEFNGQDLQRISEKERRNLVG--AEVAMIFQDPMTSlNPCY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1141 GKGgdaseSEIVSSAELSNAHGFISGLQQGYD--TMVGergI------------QLSGGQKQRVAIARAIVKDPKVLLLD 1206
Cdd:PRK11022 107 TVG-----FQIMEAIKVHQGGNKKTRRQRAIDllNQVG---IpdpasrldvyphQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1207 EATSALDAESERVVQDALDRVMV--NRTTIVVAHRLSTI-KNADVIAVVKNGVIVEKGK 1262
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
411-591 |
6.61e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 411 SGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVL-IDGINLKEFQLKWIRskiglvsqepvlftasikdniaygkedatt 489
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 490 eeikaaaelanaskfvdklpqglDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALD--- 566
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180
....*....|....*....|....*....
gi 15226477 567 ----RIMVNRTTVVVAHRLSTVRNADMIA 591
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
403-609 |
7.02e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN----LKEFqlkwiRSKIGLV----SQ----EPV 470
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrRKEF-----ARRIGVVfgqrSQlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 LFTASIKDNIaYGKEDATTEE-IKAAAELANASKFvdklpqgLDTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEA 549
Cdd:COG4586 114 IDSFRLLKAI-YRIPDAEYKKrLDELVELLDLGEL-------LDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 550 TSALDAESERVVQEALDRImvNR---TTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEY--NRergTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1031-1244 |
7.55e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.15 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1031 SGRVLDNVKGdIELRHVSFKYPARpDVQIfQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveiks 1110
Cdd:TIGR00954 442 RGIVEYQDNG-IKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1111 lrlkwlRQQTGLVSQEPILFNETIRANIAYGKGGDASESEIVSSAEL----SNAH-GFISGLQQGYDTMVGERGIqLSGG 1185
Cdd:TIGR00954 514 ------KGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLeqilDNVQlTHILEREGGWSAVQDWMDV-LSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1186 QKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNRTTIVVAHRLSTIK 1244
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
404-581 |
9.01e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKWIRSK----IGLVSQE----PVLftaS 475
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQElnliPQL---T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 476 IKDNIAYGKEDATT-EEIKAAAELANASKFVDKL--PQGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:PRK10762 96 IAENIFLGREFVNRfGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190
....*....|....*....|....*....|...
gi 15226477 553 L-DAESE---RVVQEALDRimvNRTTVVVAHRL 581
Cdd:PRK10762 172 LtDTETEslfRVIRELKSQ---GRGIVYISHRL 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
404-591 |
9.76e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 404 GFSLFISSGT-----TVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDginLK-EFQLKWIRSKI-GLVSQepvlFTASI 476
Cdd:PRK13409 352 DFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSYKPQYIKPDYdGTVED----LLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 477 KDNIAygkedatTEEIKAaaELANaskfvdklPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE 556
Cdd:PRK13409 425 TDDLG-------SSYYKS--EIIK--------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180 190
....*....|....*....|....*....|....*..
gi 15226477 557 SERVVQEALDRIMVNR--TTVVVAHRLSTVrnaDMIA 591
Cdd:PRK13409 488 QRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1042-1264 |
1.07e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEItldgveikslrlKWlrqqtg 1121
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 lvsqepilfneTIRANIAYGKGGDASESEivssaELSNAHGFISGLQQGYD--TMVgeRGI----------------QLS 1183
Cdd:PRK15064 379 -----------SENANIGYYAQDHAYDFE-----NDLTLFDWMSQWRQEGDdeQAV--RGTlgrllfsqddikksvkVLS 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1184 GGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDrvMVNRTTIVVAH------RLSTiknaDVIAVVKNGVI 1257
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHdrefvsSLAT----RIIEITPDGVV 514
|
....*..
gi 15226477 1258 VEKGKHD 1264
Cdd:PRK15064 515 DFSGTYE 521
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
406-600 |
1.14e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKWIR----SKIGLVSQE----PVLftaSIK 477
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTaalaAGVAIIYQElhlvPEM---TVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 478 DNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLD--TMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDA 555
Cdd:PRK11288 98 ENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 556 -ESE---RVVQEALDRimvNRTTVVVAHRLSTV-RNADMIAVIHQGKIVE 600
Cdd:PRK11288 174 rEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
63-262 |
1.47e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 57.96 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 63 MILGTLGSIGNGLgFPLM-TLLFGDLIDAFGENQTNTTDKVSK------VALKFVWLGIGTFAAAFLQ-----LSGWMIS 130
Cdd:cd18565 1 LVLGLLASILNRL-FDLApPLLIGVAIDAVFNGEASFLPLVPAslgpadPRGQLWLLGGLTVAAFLLEslfqyLSGVLWR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 131 GERQAAR--IRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTL 208
Cdd:cd18565 80 RFAQRVQhdLRTDTYDHVQRLDMAFFE-DRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 209 VMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGE 262
Cdd:cd18565 159 VALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAE 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1048-1237 |
1.56e-08 |
|
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: 56.12 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1048 SFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKST---VIALLQRFYDPDSGEITLDGVEIKSLRLKWlRQQTGLVS 1124
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1125 QEPILFNE-TIRaniaygkggdasesEIVSSAELSNAHGFISGlqqgydtmvgergiqLSGGQKQRVAIARAIVKDPKVL 1203
Cdd:cd03233 90 EEDVHFPTlTVR--------------ETLDFALRCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15226477 1204 LLDEATSALDAEServvqdALD-----RVMVN--RTTIVVA 1237
Cdd:cd03233 141 CWDNSTRGLDSST------ALEilkciRTMADvlKTTTFVS 175
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
384-562 |
1.58e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVL--------------IDGIN 449
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 450 LkefqlkwirskiglvSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELAnaskfvdklpqgLDTMVgehgtQLSGGQKQ 529
Cdd:PLN03073 587 L---------------SSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLA------------LQPMY-----TLSGGQKS 634
|
170 180 190
....*....|....*....|....*....|....
gi 15226477 530 RIAVARAILKDPRILLLDEATSALDAES-ERVVQ 562
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
52-321 |
1.68e-08 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 57.40 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 52 FAFAdsfdFLLMILGTLGSIgnglgfpLMTLLFGDLIDAFGENQTNTTDKVSKVALKFVWLGIGTFAAAFLQ--LSGWMi 129
Cdd:cd18544 1 FILA----LLLLLLATALEL-------LGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQtyLLQKL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 130 sGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLV 209
Cdd:cd18544 69 -GQRIIYDLRRDLFSHIQRLPLSFFD-RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 210 MLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGL 289
Cdd:cd18544 147 SLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFAL 226
|
250 260 270
....*....|....*....|....*....|..
gi 15226477 290 GLGTLFLVVFCSYALAVWYGGKLILDKGYTGG 321
Cdd:cd18544 227 FRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
794-921 |
1.93e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 57.11 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 794 RIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGdSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLP 873
Cdd:cd18543 73 DLRTDLFAHLQRLDGAFHDR--WQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLP 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15226477 874 LIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18543 150 PLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRER 197
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
720-990 |
2.06e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 57.16 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 720 LILGSISAAANGVILPIFGILISSVIKAFFQPPKKLkedTSFWAIIFMVLGfasiiAYPAQTFFFAI-------AGCKLV 792
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL---GLLLGLALLLLG-----AYLLRALLNFLriylnhvAEQKVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 793 QRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAML 872
Cdd:cd18778 73 ADLRSDLYDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 873 PLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEgpmknGIRQGIVSGIgFGFS 952
Cdd:cd18778 151 PFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSR-----RYRKAQLRAM-KLWA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15226477 953 FFVLFSSYAASF------YVGARLVDDGKTTFDSVFRVFFALTM 990
Cdd:cd18778 225 IFHPLMEFLTSLgtvlvlGFGGRLVLAGELTIGDLVAFLLYLGL 268
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
406-620 |
2.31e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLI--------------ERFYDpqagdvlIDGINLKEFQL-KWIRSKIGLVSQEP- 469
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDD-------IDLLRLSPRERrKLVGHNVSMIFQEPq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 470 --VLFTASIKDNIAYGKEDATTE---------EIKAAAELANASKFVDKlpqglDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PRK15093 100 scLDPSERVGRQLMQNIPGWTYKgrwwqrfgwRKRRAIELLHRVGIKDH-----KDAMRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV--VAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQTVETAPSKELVTTPHHPY 254
|
....*.
gi 15226477 616 SQ-LIR 620
Cdd:PRK15093 255 TQaLIR 260
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
387-596 |
2.34e-08 |
|
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: 55.33 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 387 KDVYFTYP-ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTV---------VSLIErfydpqaGDVLIDGINLKE-FQl 455
Cdd:cd03232 7 KNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLldvlagrktAGVIT-------GEILINGRPLDKnFQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 456 kwiRSkIGLVSQEPVLFtasikdniaygkEDATTEEikaaaelanASKFVDKLpQGldtmvgehgtqLSGGQKQRIAVAR 535
Cdd:cd03232 79 ---RS-TGYVEQQDVHS------------PNLTVRE---------ALRFSALL-RG-----------LSVEQRKRLTIGV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 536 AILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTV--RNADMIAVIHQG 596
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
406-602 |
2.63e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKW-IRSKIGLVSQE-PVLFTASIKDNIAYG 483
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElSVIDELTVLENLYIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 484 KE-----------DATTEEIKAAAELANASKFVDklpqgLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:PRK09700 105 RHltkkvcgvniiDWREMRVRAAMMLLRVGLKVD-----LDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15226477 553 L-DAESERVVQeALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:PRK09700 176 LtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
401-597 |
2.82e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIE-RFYDPQ-AGDVLIDGINLKefqlKWIRSKIGLVSQEPVL------- 471
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPT----KQILKRTGFVTQDDILyphltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 472 ----FTASIKDNIAYGKEDATTEEIKAAAELAnaskfvdkLPQGLDTMVGEHGTQ-LSGGQKQRIAVARAILKDPRILLL 546
Cdd:PLN03211 159 etlvFCSLLRLPKSLTKQEKILVAESVISELG--------LTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 547 DEATSALDAESE-RVVQEALDRIMVNRTTVVVAHRLST--VRNADMIAVIHQGK 597
Cdd:PLN03211 231 DEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
384-620 |
2.98e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKwiRSKIG 463
Cdd:PRK15056 7 IVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQ--KNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQE-------PVLftasIKDNIAYGKEDATTEEIKAAAElanASKFVDKLPQGLDTMVGEHGT--QLSGGQKQRIAVA 534
Cdd:PRK15056 82 YVPQSeevdwsfPVL----VEDVVMMGRYGHMGWLRRAKKR---DRQIVTAALARVDMVEFRHRQigELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 535 RAILKDPRILLLDEATSALDAESE-RVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG--SHTELLKDP 611
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGptETTFTAENL 234
|
....*....
gi 15226477 612 EGAYSQLIR 620
Cdd:PRK15056 235 ELAFSGVLR 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
384-584 |
3.95e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVlidginLKEFQLkwirsKIG 463
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKL-----RIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 LVSQ----EPVL-FTASIKDNIAYGKEDAtteEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAIL 538
Cdd:PRK09544 71 YVPQklylDTTLpLTVNRFLRLRPGTKKE---DILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226477 539 KDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTV 584
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRreLDCAVLMVSHDLHLV 184
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
368-557 |
4.65e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 368 DSYSTNGKVLDD--IKGDI-ELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVS-LIERFYDP--QA 440
Cdd:TIGR00956 741 ESDDVNDEKDMEkeSGEDIfHWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVTTGviTG 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 441 GDVLIDGINLKE-FQlkwiRSkIGLVSQEPV-LFTASIKDNIAYgkedatTEEIKAAAELANASK--FVDKLPQGL---- 512
Cdd:TIGR00956 821 GDRLVNGRPLDSsFQ----RS-IGYVQQQDLhLPTSTVRESLRF------SAYLRQPKSVSKSEKmeYVEEVIKLLemes 889
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226477 513 --DTMVGEHGTQLSGGQKQRIAVARAILKDPRILL-LDEATSALDAES 557
Cdd:TIGR00956 890 yaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
403-599 |
5.44e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLI--ERfyDPQAGDVLIDGINLKEFQ-LKWIRSKIGLVSQEP-----VLfTA 474
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRlgrglVP-DM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 SIKDNIA----YGKEDATTEEIKAAAELANASKFVDKL---PQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLD 547
Cdd:COG3845 352 SVAENLIlgryRRPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 548 EATSALDAES-----ERVVQEA------------LDRIMvnrttvvvahRLStvrnaDMIAVIHQGKIV 599
Cdd:COG3845 428 QPTRGLDVGAiefihQRLLELRdagaavllisedLDEIL----------ALS-----DRIAVMYEGRIV 481
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1042-1221 |
5.91e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEItldgVEIKSLRLKWLRQQ-- 1119
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV----FRSAKVRMAVFSQHhv 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1120 TGL-VSQEPILF---------NETIRANI-AYGKGGDASeseivssaelsnahgfisgLQQGYdtmvgergiQLSGGQKQ 1188
Cdd:PLN03073 583 DGLdLSSNPLLYmmrcfpgvpEQKLRAHLgSFGVTGNLA-------------------LQPMY---------TLSGGQKS 634
|
170 180 190
....*....|....*....|....*....|....
gi 15226477 1189 RVAIARAIVKDPKVLLLDEATSALDAES-ERVVQ 1221
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1068-1252 |
7.37e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.07 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1068 RAGKTVALVGESGSGKSTVIALLQ--------RFYDPDSGEITLD---GVEIKSLrLKWLRQQTGLVSQEPILFNETIRA 1136
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNY-FTKLLEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1137 niAYGKGGDASES--------EIVSSAELSNahgfisglqqgydtmVGERGI-QLSGGQKQRVAIARAIVKDPKVLLLDE 1207
Cdd:cd03236 103 --VKGKVGELLKKkdergkldELVDQLELRH---------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226477 1208 ATSALDAEsERVVQDALDRVMV--NRTTIVVAHRLSTIKN-ADVIAVV 1252
Cdd:cd03236 166 PSSYLDIK-QRLNAARLIRELAedDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
137-336 |
7.61e-08 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 55.53 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 137 RIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSgDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFE-TRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 217 LvmagALLAIVIAKTASRGQTAYAKAATVVE----QTIGSIRTVASFTGEKQAI----SNYNKHLVTAYKAGVIEGGSTG 288
Cdd:cd18570 154 Y----ILIILLFNKPFKKKNREVMESNAELNsyliESLKGIETIKSLNAEEQFLkkieKKFSKLLKKSFKLGKLSNLQSS 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226477 289 LGLgtlfLVVFCSYALAVWYGGKLILDKGYTGGQVL--NIIIAVLTGSMS 336
Cdd:cd18570 230 IKG----LISLIGSLLILWIGSYLVIKGQLSLGQLIafNALLGYFLGPIE 275
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
388-591 |
8.83e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 388 DVYFTYPARpdEQIFRGFSLFISSGT-----TVALVGQSGSGKSTVVSLIERFYDPQAGDVlidginlkEFQLKwirski 462
Cdd:COG1245 339 ETLVEYPDL--TKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 glvsqepvlftasikdnIAY------GKEDATTEEI--KAAAELANASKF---------VDKLpqgLDTMVGEhgtqLSG 525
Cdd:COG1245 403 -----------------ISYkpqyisPDYDGTVEEFlrSANTDDFGSSYYkteiikplgLEKL---LDKNVKD----LSG 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTVrnaDMIA 591
Cdd:COG1245 459 GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
61-323 |
9.21e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 55.18 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 61 LLMILGTLGsIGNGLGfPLMTLLFGDLID-AFGENQTNTtdkvskvalkFVWLGIGTFAAAFLQ---------LSGWMis 130
Cdd:cd18550 1 LALVLLLIL-LSALLG-LLPPLLLREIIDdALPQGDLGL----------LVLLALGMVAVAVASallgvvqtyLSARI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 131 GERQAARIRSLYLKTILRQDIAFFdIDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVM 210
Cdd:cd18550 67 GQGVMYDLRVQLYAHLQRMSLAFF-TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 211 LSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQT--IGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTG 288
Cdd:cd18550 146 LVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGR 225
|
250 260 270
....*....|....*....|....*....|....*
gi 15226477 289 LGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQV 323
Cdd:cd18550 226 WFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTL 260
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1061-1268 |
9.89e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.48 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQqTGLV----SQ----EPILfnE 1132
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQlwwdLPAI--D 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1133 TIRANIA-YGkggdaseseiVSSAEL-SNAHGFISGLQQG--YDTMVgeRgiQLSGGQKQRVAIARAIVKDPKVLLLDEA 1208
Cdd:COG4586 116 SFRLLKAiYR----------IPDAEYkKRLDELVELLDLGelLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1209 TSALDAESERVVQDALDRvmVNR---TTIVVA-HRLSTIKN-ADVIAVVKNGVIVEKGKHDTLIN 1268
Cdd:COG4586 182 TIGLDVVSKEAIREFLKE--YNRergTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1027-1213 |
1.09e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1027 PSVESGRVLdnvkgdIELRHVSFKyPARPDVQIfQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGV 1106
Cdd:COG3845 249 APAEPGEVV------LEVENLSVR-DDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1107 EIKSLRLKWL-----------RQQTGLVSQEPILFN---ETIRaNIAYGKGGdaseseIVSSAEL-SNAHGFISGLQ--- 1168
Cdd:COG3845 321 DITGLSPRERrrlgvayipedRLGRGLVPDMSVAENlilGRYR-RPPFSRGG------FLDRKAIrAFAEELIEEFDvrt 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226477 1169 QGYDTMVGergiQLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1213
Cdd:COG3845 394 PGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
763-932 |
1.31e-07 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 54.78 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 763 AIIFMVL-GFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLA 841
Cdd:cd18589 38 AITVMSLlTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDS--NQTGDIVSRVTTDTEDMSESLSENLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 842 QTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18589 116 LLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEE 195
|
170
....*....|.
gi 15226477 922 KVMNMYSKKCE 932
Cdd:cd18589 196 GEAQRYRQRLQ 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
384-579 |
1.64e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVlidginlkefqlKWirskig 463
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 464 lvsqepvlftaSIKDNIAYGKEDAtteeikaAAELANASKFVD-----KLPQGLDTMV-GEHG-------------TQLS 524
Cdd:PRK15064 379 -----------SENANIGYYAQDH-------AYDFENDLTLFDwmsqwRQEGDDEQAVrGTLGrllfsqddikksvKVLS 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 525 GGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDriMVNRTTVVVAH 579
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSH 493
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1067-1252 |
1.65e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1067 IRAGKTVALVGESGSGKSTVIALLqrfydpdSGEIT--LDGVEIKSlrlKW---LRQQTGLVSQEPI--LFNETIRA--N 1137
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIpnLGDYEEEP---SWdevLKRFRGTELQNYFkkLYNGEIKVvhK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1138 IAY---------GKGGDASE--------SEIVSSAELSNahgfisglqqgydtmVGERGI-QLSGGQKQRVAIARAIVKD 1199
Cdd:PRK13409 166 PQYvdlipkvfkGKVRELLKkvdergklDEVVERLGLEN---------------ILDRDIsELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 1200 PKVLLLDEATSALDAEsERV-VQDALDRVMVNRTTIVVAHRLSTIKN-ADVIAVV 1252
Cdd:PRK13409 231 ADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1057-1214 |
2.61e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1057 VQIFQDLCLSIRAGKTVALVGESGSGKST---VIAL-LQRFYDPDSGEITLDGV---EIKslrlkwlRQQTG-------- 1121
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTllkTIASnTDGFHIGVEGVITYDGItpeEIK-------KHYRGdvvynaet 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1122 ------LVSQEPILFNETIRANIAYGKGGDaSESEIVSSAELSNAhgfISGLQQGYDTMVGE---RGIqlSGGQKQRVAI 1192
Cdd:TIGR00956 147 dvhfphLTVGETLDFAARCKTPQNRPDGVS-REEYAKHIADVYMA---TYGLSHTRNTKVGNdfvRGV--SGGERKRVSI 220
|
170 180
....*....|....*....|..
gi 15226477 1193 ARAIVKDPKVLLLDEATSALDA 1214
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDS 242
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1065-1216 |
2.86e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLqrfydpdSGEITLDGVEI---KSLRLKWLRQ-----QTGLVsqepilFN---ET 1133
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeQDLIVARLQQdpprnVEGTV------YDfvaEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1134 IRANIAYGK---------GGDASESEIVSSAEL------SNAHGFISGLQQ-------GYDTMVGErgiqLSGGQKQRVA 1191
Cdd:PRK11147 91 IEEQAEYLKryhdishlvETDPSEKNLNELAKLqeqldhHNLWQLENRINEvlaqlglDPDAALSS----LSGGWLRKAA 166
|
170 180
....*....|....*....|....*
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAES 1216
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1042-1238 |
3.11e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPdvqIFQDLCLSIRAGKTVALVGESGSGKSTVIALL-----QRFydpdSGEITLDGVEIKSLRLKW- 1115
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGY----SNDLTLFGRRRGSGETIWd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1116 LRQQTGLVSQEPIL---FNETIRANIAYGKGGDASESEIVSSAELSNAHGFISGLqqGYDTMVGERGIQ-LSGGQKQRVA 1191
Cdd:PRK10938 334 IKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSWGQQRLAL 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15226477 1192 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTT--IVVAH 1238
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSH 460
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1042-1225 |
3.61e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITL-DGVEIkslrlkwlrqqt 1120
Cdd:PRK11819 325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKL------------ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQ--EPILFNETIRANIAYG----KGGDAsesEIVSSAELSnAHGFISGLQQgydTMVGergiQLSGGQKQRVAIAR 1194
Cdd:PRK11819 390 AYVDQsrDALDPNKTVWEEISGGldiiKVGNR---EIPSRAYVG-RFNFKGGDQQ---KKVG----VLSGGERNRLHLAK 458
|
170 180 190
....*....|....*....|....*....|.
gi 15226477 1195 AIVKDPKVLLLDEATSALDAESERVVQDALD 1225
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1055-1212 |
3.63e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1055 PDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEI--KSLRlKWLRQQTGLVSQEPILFNE 1132
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSK-EALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1133 -TIRANIAYG----KGGDASESEIVSS-----AELsnahgfisglqqGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKV 1202
Cdd:PRK10982 88 rSVMDNMWLGryptKGMFVDQDKMYRDtkaifDEL------------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170
....*....|
gi 15226477 1203 LLLDEATSAL 1212
Cdd:PRK10982 156 VIMDEPTSSL 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1040-1213 |
3.72e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1040 GDI--ELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKS-TVIALLQRFYDPDSGEITLDG--VEIKSLR-- 1112
Cdd:PRK13549 256 GEVilEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIRNPQqa 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1113 -------LKWLRQQTGLVSQEPILFNETIRANIAYGKGGdasesEIVSSAELSNAHGFISGLQqgYDTMVGERGI-QLSG 1184
Cdd:PRK13549 336 iaqgiamVPEDRKRDGIVPVMGVGKNITLAALDRFTGGS-----RIDDAAELKTILESIQRLK--VKTASPELAIaRLSG 408
|
170 180
....*....|....*....|....*....
gi 15226477 1185 GQKQRVAIARAIVKDPKVLLLDEATSALD 1213
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1063-1240 |
4.10e-07 |
|
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: 55.02 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1063 LCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSlRLKWLRQQTGLVSQ----EPILFNETIRANI 1138
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfdaiDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1139 AYGKGGDASESEIVSSAELSNAhgfisGLQQGYDTMVGergiQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESER 1218
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSL-----GLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180
....*....|....*....|...
gi 15226477 1219 VVQDALDRVMVN-RTTIVVAHRL 1240
Cdd:TIGR01257 2108 MLWNTIVSIIREgRAVVLTSHSM 2130
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
405-598 |
4.28e-07 |
|
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: 54.06 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 405 FSLfiSSGTTVALVGQSGSGKSTVVSLIERFYDPQ-AGDVLIDG--INLKEFQlKWIRSKIGLVSQE-------PVL--- 471
Cdd:TIGR02633 281 FSL--RRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPA-QAIRAGIAMVPEDrkrhgivPILgvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 472 --FTASIKDNIAY-GKEDATTEE--IKAAAELANASKFVDKLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLL 546
Cdd:TIGR02633 358 knITLSVLKSFCFkMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 547 DEATSALD----AESERVV-QEALDRIMVnrttVVVAHRLSTVRN-ADMIAVIHQGKI 598
Cdd:TIGR02633 428 DEPTRGVDvgakYEIYKLInQLAQEGVAI----IVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
759-978 |
4.59e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 52.98 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 759 TSFWAIIFMVLGFASIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSaDAATIRG-LVG 837
Cdd:cd18782 42 YVIGVVMLVAALLEAVLTA-LRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDK--RPVGELSTRIS-ELDTIRGfLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 838 DSLAQTVQNLSSILAgLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASF 917
Cdd:cd18782 118 TALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQ 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 918 CAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTF 978
Cdd:cd18782 197 NAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTL 257
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
412-590 |
5.54e-07 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 52.62 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 412 GTTVALVGQSGSGKSTVV------SLIERFY----DPQAGDVlIDGINLKEfqlkwirsKIGLVSQEPV----------- 470
Cdd:cd03271 21 GVLTCVTGVSGSGKSSLIndtlypALARRLHlkkeQPGNHDR-IEGLEHID--------KVIVIDQSPIgrtprsnpaty 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 471 --LFTaSIKD----------------NIAY-GKE-----DATTEEikaAAEL-ANASKFVDKLPQ----GLDTM-VGEHG 520
Cdd:cd03271 92 tgVFD-EIRElfcevckgkrynretlEVRYkGKSiadvlDMTVEE---ALEFfENIPKIARKLQTlcdvGLGYIkLGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 521 TQLSGGQKQRIAVARAILKDPR---ILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRNADMI 590
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWI 241
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
60-315 |
5.57e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 52.92 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIGNGLGFPLMTllfGDLIDAFGENQtNTTDKVSKVALkfvwLGIGTFAA-AFLQ-LSGWM--ISGERQA 135
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLI---RELVDLVTIGS-KSLGLLLGLAL----LLLGAYLLrALLNfLRIYLnhVAEQKVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 136 ARIRS-LYLKtILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSI 214
Cdd:cd18778 73 ADLRSdLYDK-LQRLSLRYFD-DRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 215 PLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKhLVTAYKAGVIEGGSTGLGLGTl 294
Cdd:cd18778 151 PFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEA-LSRRYRKAQLRAMKLWAIFHP- 228
|
250 260
....*....|....*....|....
gi 15226477 295 fLVVF---CSYALAVWYGGKLILD 315
Cdd:cd18778 229 -LMEFltsLGTVLVLGFGGRLVLA 251
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
765-977 |
8.98e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 52.20 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 765 IFMVLGFASIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLsADAATIRGLVGDSLAQTV 844
Cdd:cd18566 48 VVIAILLESLLRL-LRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFER--EPSGAHLERL-NSLEQIREFLTGQALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 845 QNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMK-----GFSADAKKMygeasQVANDAVGSIRTVASFCA 919
Cdd:cd18566 124 LDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRralkeRSRADERRQ-----NFLIETLTGIHTIKAMAM 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 920 E----DKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAasfyVGARLVDDGKTT 977
Cdd:cd18566 199 EpqmlRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVA----FGALLVINGDLT 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1042-1213 |
1.03e-06 |
|
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: 52.90 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1042 IELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKS-TVIALLQRFYDPDSGEITLDGVEI------KSLRLK 1114
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVdirnpaQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1115 WL-----RQQTGLVSQEPILFNETIRANIAYGKGG---DASESEIVSSA----ELSNAHGFISglqqgydtmVGergiQL 1182
Cdd:TIGR02633 338 IAmvpedRKRHGIVPILGVGKNITLSVLKSFCFKMridAAAELQIIGSAiqrlKVKTASPFLP---------IG----RL 404
|
170 180 190
....*....|....*....|....*....|.
gi 15226477 1183 SGGQKQRVAIARAIVKDPKVLLLDEATSALD 1213
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
385-566 |
1.16e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIdGINLKefqlkwirskIGL 464
Cdd:PRK11147 321 EMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----------VAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 VSQ-----EPvlfTASIKDNIAYGKEDATTEEIKAAAelanASKFVDKL--PQGLDTMVgehgTQLSGGQKQRIAVARAI 537
Cdd:PRK11147 387 FDQhraelDP---EKTVMDNLAEGKQEVMVNGRPRHV----LGYLQDFLfhPKRAMTPV----KALSGGERNRLLLARLF 455
|
170 180
....*....|....*....|....*....
gi 15226477 538 LKDPRILLLDEATSALDAESERVVQEALD 566
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
60-335 |
1.21e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 51.63 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSigngLGFPLMTllfGDLIDAFgeNQTNTTDKVSKVALKFVWLGIGTFAAAFLqlSGWMIS--GERQAAR 137
Cdd:cd18548 5 PLFKLLEVLLE----LLLPTLM---ADIIDEG--IANGDLSYILRTGLLMLLLALLGLIAGIL--AGYFAAkaSQGFGRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 138 IRS-LYLKTilrQDIAFFDIDT-NTGEVVGRMSGDTVLIQDAmgekVGKAIQLLA----TFVGGFVIAFVRGWLLTLVML 211
Cdd:cd18548 74 LRKdLFEKI---QSFSFAEIDKfGTSSLITRLTNDVTQVQNF----VMMLLRMLVrapiMLIGAIIMAFRINPKLALILL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 212 SSIPLLVmagALLAIVIAKTA---SRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNY---NKHLV-TAYKAGVIeg 284
Cdd:cd18548 147 VAIPILA---LVVFLIMKKAIplfKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFdkaNDDLTdTSLKAGRL-- 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 285 gsTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQV-------LNIIIAVLTGSM 335
Cdd:cd18548 222 --MALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
409-582 |
1.45e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 409 ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwiRSKIGLVSQEPVLFTASIKDNIAY------ 482
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIYpdssed 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 483 ----GKEDATTEEIKAAAELANaskfVDKLPQGLDTmVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:TIGR00954 544 mkrrGLSDKDLEQILDNVQLTH----ILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
170 180
....*....|....*....|....
gi 15226477 559 RVVQEALDRimVNRTTVVVAHRLS 582
Cdd:TIGR00954 619 GYMYRLCRE--FGITLFSVSHRKS 640
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
757-887 |
1.61e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 51.35 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 757 EDTSFWAIIFMVLGF-ASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGL 835
Cdd:cd18580 35 SSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDT--TPSGRILNRFSKDIGLIDEE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15226477 836 VGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVlamLPLIALNGFLYMKFMK 887
Cdd:cd18580 113 LPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL---PPLLVVYYLLQRYYLR 161
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1066-1213 |
1.65e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1066 SIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGveikSLRLKWLRQQTGLVSQEPI------------LFNET 1133
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQLAWVNQETPALPQPALeyvidgdreyrqLEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1134 IRAN-------IAYGKGG-DASESEIVSSAELSNAHGFisGLQQgydTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLL 1205
Cdd:PRK10636 99 HDANerndghaIATIHGKlDAIDAWTIRSRAASLLHGL--GFSN---EQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
....*...
gi 15226477 1206 DEATSALD 1213
Cdd:PRK10636 174 DEPTNHLD 181
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
115-279 |
1.92e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 50.95 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 115 GTFAAAFLQLSGWMisGER--QAARIRSLylKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATF 192
Cdd:cd18546 53 WVAQRAQTRLTGRT--GERllYDLRLRVF--AHLQRLSLDFHE-RETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 193 VGGFVIAFVRGWLLTLVMLSSIPLLvmagALLAIVIAKTASRgqtAYAKA--------ATVVEqTIGSIRTVASFTGEKQ 264
Cdd:cd18546 128 VGIAVVLLVLDPRLALVALAALPPL----ALATRWFRRRSSR---AYRRAreriaavnADLQE-TLAGIRVVQAFRRERR 199
|
170
....*....|....*
gi 15226477 265 AISNYnKHLVTAYKA 279
Cdd:cd18546 200 NAERF-AELSDDYRD 213
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1062-1249 |
2.32e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1062 DLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR---LKWLRQQTGLVSQEpilfneTIRANI 1138
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLEM------TVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1139 AYGkggdaseSEIVSSAELSNA--HGFisglqqGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES 1216
Cdd:PRK13541 92 KFW-------SEIYNSAETLYAaiHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180 190
....*....|....*....|....*....|....*
gi 15226477 1217 ERVVQDaLDRVMVNRTTIVV--AHRLSTIKNADVI 1249
Cdd:PRK13541 159 RDLLNN-LIVMKANSGGIVLlsSHLESSIKSAQIL 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1065-1277 |
2.58e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLK---------WLRQQTGLVSQEPILFNETIR 1135
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEqlqklvsdeWQRNNTDMLSPGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1136 aniaygkggdasesEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAE 1215
Cdd:PRK10938 104 --------------EIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 1216 SERVVQDALDRVMVNRTTIV-VAHRLSTIKN-ADVIAVVKNGVIVEKGKHDTLINikDGVYASL 1277
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ--QALVAQL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1181-1252 |
2.61e-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: 51.71 E-value: 2.61e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226477 1181 QLSGGQKQRVAIARAIVKDPKVLLLDEATSALD----AESERVVQDALDRvmvNRTTIVVAHRLSTI-KNADVIAVV 1252
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAILdYLADYVHIL 285
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
60-321 |
2.73e-06 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 50.54 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 60 FLLMILGTLGSIGNGLGFPLmtlLFGDLIDAFGENQtNTTDkVSKVALKFVWLGIGTFAAAFLQ--LSGWMisGERQAAR 137
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPY---LIKIAIDEYIPNG-DLSG-LLIIALLFLALNLVNWVASRLRiyLMAKV--GQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 138 IRS-LYLKtILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18545 75 LRQdLFSH-LQKLSFSFFD-SRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 217 LVmagaLLAIVIAKTASRG-QTAYAKAATV---VEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGViegGSTGLGLG 292
Cdd:cd18545 153 LV----LVVFLLRRRARKAwQRVRKKISNLnayLHESISGIRVIQSFAREDENEEIFDELNRENRKANM---RAVRLNAL 225
|
250 260 270
....*....|....*....|....*....|..
gi 15226477 293 TLFLVVFCS---YALAVWYGGKLILDKGYTGG 321
Cdd:cd18545 226 FWPLVELISalgTALVYWYGGKLVLGGAITVG 257
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1044-1264 |
2.92e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1044 LRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPD---SGEITLDGVEIKSLRLkwlRQQT 1120
Cdd:PLN03140 165 LGMLGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP---RKTS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1121 GLVSQEPI-------------------------LFNETIR----ANIAYGKGGD----ASESEIVSSAELSNAHGFISGL 1167
Cdd:PLN03140 242 AYISQNDVhvgvmtvketldfsarcqgvgtrydLLSELARrekdAGIFPEAEVDlfmkATAMEGVKSSLITDYTLKILGL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1168 QQGYDTMVGE---RGIqlSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDR-VMVNRTTIVVahrlSTI 1243
Cdd:PLN03140 322 DICKDTIVGDemiRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQiVHLTEATVLM----SLL 395
|
250 260
....*....|....*....|....*...
gi 15226477 1244 KNA-------DVIAVVKNGVIVEKGKHD 1264
Cdd:PLN03140 396 QPApetfdlfDDIILLSEGQIVYQGPRD 423
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
422-598 |
2.98e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 422 GSGKSTVVSLIERFYDPQ-AGDVLIDGINLK-EFQLKWIRSKIGLVSQE-------PVLftaSIKDNIAYGKED--ATTE 490
Cdd:PRK13549 298 GAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgivPVM---GVGKNITLAALDrfTGGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 491 EIKAAAELANASKFVDKL---PQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD--AESE------R 559
Cdd:PRK13549 375 RIDDAAELKTILESIQRLkvkTASPELAIA----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyklinQ 450
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15226477 560 VVQEALDRIMvnrttvvVAHRLSTVRN-ADMIAVIHQGKI 598
Cdd:PRK13549 451 LVQQGVAIIV-------ISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
400-582 |
3.93e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSL---------IErfydpqaGDVLIDGINLKEFQLKWIRskiGLVSQ--- 467
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVlagrktggyIE-------GDIRISGFPKKQETFARIS---GYCEQndi 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 468 --------EPVLFTASIKDNIAYGKEDAT--TEEIKAAAELANASkfvdklpqglDTMVGEHG-TQLSGGQKQRIAVARA 536
Cdd:PLN03140 964 hspqvtvrESLIYSAFLRLPKEVSKEEKMmfVDEVMELVELDNLK----------DAIVGLPGvTGLSTEQRKRLTIAVE 1033
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEAL-DRIMVNRTTVVVAHRLS 582
Cdd:PLN03140 1034 LVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1067-1216 |
4.53e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1067 IRAGKTVALVGESGSGKSTVI-ALLQRFydpDSGEITLD-----GVEIKSLrlkwLRQQTGLVSQEPI-LFNETIRania 1139
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLnVLAERV---TTGVITGGdrlvnGRPLDSS----FQRSIGYVQQQDLhLPTSTVR---- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1140 ygkggdasESEIVS-----SAELSNAHGF--------ISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLL-L 1205
Cdd:TIGR00956 855 --------ESLRFSaylrqPKSVSKSEKMeyveevikLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170
....*....|.
gi 15226477 1206 DEATSALDAES 1216
Cdd:TIGR00956 927 DEPTSGLDSQT 937
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1041-1265 |
5.67e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1041 DIELRHVSFKYPARpdvQIFQDLCLSIRAGKTVALVGESGSGKSTVI-ALLQRFYD--PDSGEI-----TLDGVEIKSL- 1111
Cdd:PLN03073 177 DIHMENFSISVGGR---DLIVDASVTLAFGRHYGLVGRNGTGKTTFLrYMAMHAIDgiPKNCQIlhveqEVVGDDTTALq 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1112 --------RLKWLRQQTGLVSQEPILFNETIRANiAYGKGGDASESEIVS----------------SAElSNAHGFISGL 1167
Cdd:PLN03073 254 cvlntdieRTQLLEEEAQLVAQQRELEFETETGK-GKGANKDGVDKDAVSqrleeiykrlelidayTAE-ARAASILAGL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1168 QQGYDtMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALdrVMVNRTTIVVAHR---LSTIK 1244
Cdd:PLN03073 332 SFTPE-MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHArefLNTVV 408
|
250 260
....*....|....*....|.
gi 15226477 1245 nADVIAVVKNGVIVEKGKHDT 1265
Cdd:PLN03073 409 -TDILHLHGQKLVTYKGDYDT 428
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1057-1241 |
5.70e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1057 VQIFQDLCLSIRAGKTVALVGESGSGKSTVIALL--QRFYDPDSGEITLDGVEIKS---LRLKWLRQQTGLVS-----QE 1126
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQetfARISGYCEQNDIHSpqvtvRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1127 PILFNETIRANIAYGKGGDAS-ESEIVSSAELSNAHgfisglqqgyDTMVGERGIQ-LSGGQKQRVAIARAIVKDPKVLL 1204
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMfVDEVMELVELDNLK----------DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190
....*....|....*....|....*....|....*...
gi 15226477 1205 LDEATSALDAESERVVQDAL-DRVMVNRTTIVVAHRLS 1241
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
758-884 |
6.90e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 49.39 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 758 DTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVG 837
Cdd:cd18604 41 SVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDT--TPVGRILNRFSKDIETIDSELA 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15226477 838 DSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMK 884
Cdd:cd18604 119 DSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLR 165
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1180-1252 |
7.49e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 7.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1180 IQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN--RTTIVVAHRLSTIKN-ADVIAVV 1252
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYlSDRIHVF 145
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
407-557 |
7.70e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 407 LFISSGTTVALVGQSGSGKSTVVSLIerfydpqAGDVLID-GINLKEFQLKWIRskigLVSQEPVLFTASIKDNIAYG-K 484
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDLIVAR----LQQDPPRNVEGTVYDFVAEGiE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 485 EDA-----------------------TTEEIKAAAELANASKFVDKLPQGL-------DTMVGEhgtqLSGGQKQRIAVA 534
Cdd:PRK11147 93 EQAeylkryhdishlvetdpseknlnELAKLQEQLDHHNLWQLENRINEVLaqlgldpDAALSS----LSGGWLRKAALG 168
|
170 180
....*....|....*....|...
gi 15226477 535 RAILKDPRILLLDEATSALDAES 557
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIET 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
486-651 |
8.11e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 486 DATTEEIKAAAELANASKFVDklpqgldtMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEAL 565
Cdd:PLN03073 316 DAYTAEARAASILAGLSFTPE--------MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 566 drIMVNRTTVVVAHRLSTVrNADMIAVIHQgkivekgsHTELLKDPEGAYSQLIRLQEEKKSDENAA---EEQKMSSIES 642
Cdd:PLN03073 388 --LKWPKTFIVVSHAREFL-NTVVTDILHL--------HGQKLVTYKGDYDTFERTREEQLKNQQKAfesNERSRSHMQA 456
|
170
....*....|....*..
gi 15226477 643 F--------KQSSLRKS 651
Cdd:PLN03073 457 FidkfrynaKRASLVQS 473
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
831-992 |
9.50e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 49.10 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 831 TIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKG-----FSADAKKMygeaSQVAn 905
Cdd:cd18568 110 KIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRnsreiFQANAEQQ----SFLV- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 906 DAVGSIRTVASFCAEDKV----MNMYSKKCEGPMKnGIRQGIVSGIGFGFSFFVlfsSYAASFYVGARLVDDGKTTFDSV 981
Cdd:cd18568 185 EALTGIATIKALAAERPIrwrwENKFAKALNTRFR-GQKLSIVLQLISSLINHL---GTIAVLWYGAYLVISGQLTIGQL 260
|
170
....*....|...
gi 15226477 982 --FRVFFALTMAA 992
Cdd:cd18568 261 vaFNMLFGSVINP 273
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1056-1263 |
1.21e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1056 DVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALL--QRFYDPDSGEITLDGVEIKSLRLKwLRQQTG--LVSQEPI--- 1128
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGifMAFQYPVeip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1129 -----LFNETirANIAYGKGGDASESEIVSSAELSNAHgfISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVL 1203
Cdd:PRK09580 92 gvsnqFFLQT--ALNAVRSYRGQEPLDRFDFQDLMEEK--IALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226477 1204 LLDEATSALDAESERVVQDALDRVM-VNRTTIVVAH--RLSTIKNADVIAVVKNGVIVEKGKH 1263
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
486-607 |
1.53e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.63 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 486 DATTEEikaaaelanASKFVDKLP---QGLDTMV---------GEHGTQLSGGQKQRIAVARAILKD---PRILLLDEAT 550
Cdd:TIGR00630 790 DMTVEE---------AYEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPT 860
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 551 SALDAESERVVQEALDRIMVNRTTVVV-AHRLSTVRNADMIAVI------HQGKIVEKGSHTEL 607
Cdd:TIGR00630 861 TGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1061-1249 |
1.65e-05 |
|
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: 46.93 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIallqrfydpdsgeitldgveikslrlkwlrqQTGLVSQEPILFNETIRANiay 1140
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLV-------------------------------NEGLYASGKARLISFLPKF--- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1141 gkggdaSESEIVSSAELSnahgFISGLQQGYDTMvGERGIQLSGGQKQRVAIARAIVKDPK--VLLLDEATSALDAESER 1218
Cdd:cd03238 58 ------SRNKLIFIDQLQ----FLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|..
gi 15226477 1219 VVQDALDR-VMVNRTTIVVAHRLSTIKNADVI 1249
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWI 158
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1065-1258 |
2.16e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1065 LSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIK------SLRLKWL-----RQQTGLVSQEPILFNET 1133
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdAIRAGIMlcpedRKAEGIIPVHSVADNIN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1134 IRANIAYGKGGdaseSEIVSSAELSNAHGFISGLQqgYDTMVGERGI-QLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1212
Cdd:PRK11288 354 ISARRHHLRAG----CLINNRWEAENADRFIRSLN--IKTPSREQLImNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15226477 1213 D--AESE--RVVQDALDRvmvNRTTIVVAHRL-STIKNADVIAVVKNGVIV 1258
Cdd:PRK11288 428 DvgAKHEiyNVIYELAAQ---GVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1061-1249 |
2.96e-05 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.22 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVI------ALLQRFYDpdSGEITLDGVEIKSLR-LKWLRQqtglVSQEPIlfNET 1133
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHL--KKEQPGNHDRIEGLEhIDKVIV----IDQSPI--GRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1134 IRANIA-YGK-------------GGDASESEIV-------SSAELSN-----AHGF----------ISGLQQ---GYDTM 1174
Cdd:cd03271 84 PRSNPAtYTGvfdeirelfcevcKGKRYNRETLevrykgkSIADVLDmtveeALEFfenipkiarkLQTLCDvglGYIKL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 1175 vGERGIQLSGGQKQRVAIARAIVK---DPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVA-HRLSTIKNADVI 1249
Cdd:cd03271 164 -GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWI 241
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
385-672 |
3.11e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 385 ELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefQLKWIRSKIGL 464
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 465 VSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDklpQGLDTMvgehgtqlSGGQKQRIAVARAILKDPRIL 544
Cdd:PRK13545 97 NGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIY---QPVKTY--------SSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 545 LLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTVRNADMIAV-IHQGKIVEKGSHTELLKDpegaYSQLIRL- 621
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDH----YDEFLKKy 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15226477 622 -QEEKKSDENAAEEQkmssIESFKQSSLRKSSLGRSLSKggsSRGNSSRHSF 672
Cdd:PRK13545 242 nQMSVEERKDFREEQ----ISQFQHGLLQEDQTGRERKR---KKGKKTSRKF 286
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1041-1268 |
3.17e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1041 DIELRHVSFKYPARPdVQIFQDLCLSIRAGKTVALVGESGSGKStVIALLQRFYDPDSGEITLDGV---EIKSLRLKwLR 1117
Cdd:PRK15093 5 DIRNLTIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKS-LIAKAICGVTKDNWRVTADRMrfdDIDLLRLS-PR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 QQTGLVSQE-PILFNETIRANiaygkggDASES---EIVSSAELSNAHG-----------------FISGLQQGYDTMvG 1176
Cdd:PRK15093 82 ERRKLVGHNvSMIFQEPQSCL-------DPSERvgrQLMQNIPGWTYKGrwwqrfgwrkrraiellHRVGIKDHKDAM-R 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1177 ERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTI-VVAHRLSTI-KNADVIAVVK 1253
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTIlLISHDLQMLsQWADKINVLY 233
|
250
....*....|....*
gi 15226477 1254 NGVIVEKGKHDTLIN 1268
Cdd:PRK15093 234 CGQTVETAPSKELVT 248
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1061-1213 |
3.47e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1061 QDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLR-----------LKWLRQQTGLVSQEPIL 1129
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1130 FNETIrANIAYGKGGdaseSEIVSSAEL-SNAHGFISGLQ---QGYDTMVGergiQLSGGQKQRVAIARAIVKDPKVLLL 1205
Cdd:PRK10982 345 FNSLI-SNIRNYKNK----VGLLDNSRMkSDTQWVIDSMRvktPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILML 415
|
....*...
gi 15226477 1206 DEATSALD 1213
Cdd:PRK10982 416 DEPTRGID 423
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1075-1238 |
3.66e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1075 LVGESGSGKSTVIALLQRFYDPDSGEITLDgveiKSLRLKWLRQ-----------------QTGL--VSQEpilfNETIR 1135
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD----PNERLGKLRQdqfafeeftvldtvimgHTELweVKQE----RDRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1136 ANiaygkgGDASESEIVSSAELSNAHGFISG-----------------LQQGYDTMVgergiQLSGGQKQRVAIARAIVK 1198
Cdd:PRK15064 104 AL------PEMSEEDGMKVADLEVKFAEMDGytaearagelllgvgipEEQHYGLMS-----EVAPGWKLRVLLAQALFS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDAL-DRvmvNRTTIVVAH 1238
Cdd:PRK15064 173 NPDILLLDEPTNNLDINTIRWLEDVLnER---NSTMIIISH 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1052-1213 |
3.73e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1052 PARPDVQIFQDLCLSIRAGKTVALVGESGSGKsTVIA--LLQRFYDPD-SGEITLDG--VEIKSLR------LKWL---R 1117
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELAmsVFGRSYGRNiSGTVFKDGkeVDVSTVSdaidagLAYVtedR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1118 QQTGLVSQEPILFNETIrANIaygkGGDASESEIVSSAELSNAHGFISGLQ---QGYDTMVGergiQLSGGQKQRVAIAR 1194
Cdd:NF040905 347 KGYGLNLIDDIKRNITL-ANL----GKVSRRGVIDENEEIKVAEEYRKKMNiktPSVFQKVG----NLSGGNQQKVVLSK 417
|
170
....*....|....*....
gi 15226477 1195 AIVKDPKVLLLDEATSALD 1213
Cdd:NF040905 418 WLFTDPDVLILDEPTRGID 436
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
405-606 |
3.80e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 405 FSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLK----WIRSKIGLV----SQEPVLFTASI 476
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRsprdAIRAGIMLCpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 477 KDNI---AYGKEDATTEEIKAAAELANASKFVDKL----PQGlDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEA 549
Cdd:PRK11288 349 ADNInisARRHHLRAGCLINNRWEAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 550 TSALD--AESE--RVVQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTE 606
Cdd:PRK11288 424 TRGIDvgAKHEiyNVIYELAAQ---GVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
400-609 |
5.25e-05 |
|
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: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLFISSGTTVALVGQSGSGKST----VVSLIERFYDPQAGDVLIDGINLKEFQlKWIRSKIGLVSQE----PVL 471
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIK-KHYRGDVVYNAETdvhfPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 472 FTASIKDNIAYGKEDATteEIKAAAELANASKFVD------KLPQGLDTMVGEHGTQ-LSGGQKQRIAVARAILKDPRIL 544
Cdd:TIGR00956 154 TVGETLDFAARCKTPQN--RPDGVSREEYAKHIADvymatyGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 545 LLDEATSALDAEServvqeALDRIMVNRTTVVVAHRLSTV------RNA----DMIAVIHQGKIVEKGSHTELLK 609
Cdd:TIGR00956 232 CWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
407-553 |
5.70e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 407 LFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQlKWIRSKIGLVSQE-PVLFTASIKDNIAYG 483
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSK-EALENGISMVHQElNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 484 KEDATTEEIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:PRK10982 98 RYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1182-1213 |
5.77e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 5.77e-05
10 20 30
....*....|....*....|....*....|..
gi 15226477 1182 LSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1213
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
523-581 |
5.78e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 5.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226477 523 LSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVN--RTTVVVAHRL 581
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDL 132
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1034-1259 |
7.01e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1034 VLDNVKGDI--ELRHVSfkypaRPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIK-S 1110
Cdd:PRK09700 256 NVSNLAHETvfEVRNVT-----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1111 LRLKWLRQQTGLVSQ---EPILF-NETIRANIAY----------GKGGDASESEIVSSAElsNAHGFISGLQQGYDTMVG 1176
Cdd:PRK09700 331 SPLDAVKKGMAYITEsrrDNGFFpNFSIAQNMAIsrslkdggykGAMGLFHEVDEQRTAE--NQRELLALKCHSVNQNIT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1177 ErgiqLSGGQKQRVAIARAIVKDPKVLLLDEATSALD----AESERVVQDALDRvmvNRTTIVVAHRLSTIKNA-DVIAV 1251
Cdd:PRK09700 409 E----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQLADD---GKVILMVSSELPEIITVcDRIAV 481
|
....*...
gi 15226477 1252 VKNGVIVE 1259
Cdd:PRK09700 482 FCEGRLTQ 489
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
400-554 |
7.28e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 400 QIFRGFSLF-------ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkEFQLKWirskiglVSQE-PVL 471
Cdd:PRK10636 8 QIRRGVRVLldnatatINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQLAW-------VNQEtPAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 472 FTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTM---------------VGEHGTQL-------SGGQKQ 529
Cdd:PRK10636 77 PQPALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIdawtirsraasllhgLGFSNEQLerpvsdfSGGWRM 156
|
170 180
....*....|....*....|....*
gi 15226477 530 RIAVARAILKDPRILLLDEATSALD 554
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
419-587 |
7.61e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 419 GQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQ---LKWIRSKIGLVSQEPVLftasikDNIAYgkedatTEEIKAA 495
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLEMTVF------ENLKF------WSEIYNS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 496 AELANASKFVDKLPQGLDtmvgEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEaLDRIMVNRTTV 575
Cdd:PRK13541 101 AETLYAAIHYFKLHDLLD----EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGI 175
|
170
....*....|....
gi 15226477 576 VV--AHRLSTVRNA 587
Cdd:PRK13541 176 VLlsSHLESSIKSA 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
402-598 |
8.51e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 402 FRGFSLFISSGTTVALVGQSGSGKStvvSLIERFY---DPQAGDVLIDGINLKEFQLKwIRSKIGLV-----SQEPVLF- 472
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 473 TASIKDNIAY------------GKEDATTEEIKAAAELanasKFvdklpqgldtmvgEHGTQ----LSGGQKQRIAVARA 536
Cdd:PRK15439 355 DAPLAWNVCAlthnrrgfwikpARENAVLERYRRALNI----KF-------------NHAEQaartLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226477 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKI 598
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
406-639 |
9.35e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefQLKWIRSKIGLVSQEPVLftasikDNIAYGK- 484
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQLTGI------ENIEFKMl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 485 -EDATTEEIKA-AAELANASKFVDKLPQGLdtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDaesERVVQ 562
Cdd:PRK13546 112 cMGFKRKEIKAmTPKIIEFSELGEFIYQPV--------KKYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTFAQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 563 EALDRIM----VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDpegaYSQLIRLQEEKKSDENAAEEQKM 637
Cdd:PRK13546 181 KCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK----YEAFLNDFKKKSKAEQKEFRNKL 256
|
..
gi 15226477 638 SS 639
Cdd:PRK13546 257 DE 258
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
788-921 |
1.36e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 45.52 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 788 GCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFV 867
Cdd:cd18549 70 GARIETDMRRDLFEHLQKLSFSFFDN--NKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLI 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15226477 868 VLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18549 148 VFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEE 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
475-598 |
1.36e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 475 SIKDNI---AYGKEDATTEEIKAAAELANASKFVD----KLPqGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLD 547
Cdd:PRK10762 346 SVKENMsltALRYFSRAGGSLKHADEQQAVSDFIRlfniKTP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILD 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 548 EATSALD--AESE------RVVQEALDRIMVNRTTVVVahrlstVRNADMIAVIHQGKI 598
Cdd:PRK10762 421 EPTRGVDvgAKKEiyqlinQFKAEGLSIILVSSEMPEV------LGMSDRILVMHEGRI 473
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
146-271 |
2.42e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 44.75 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 146 ILRQDIAFFDiDTNTGEVVGRMSGDTVLIqdamGEKVGKAIQLL----ATFVGGFVIAFVRGWLLTLVMLSSIPLLvmag 221
Cdd:cd18549 85 LQKLSFSFFD-NNKTGQLMSRITNDLFDI----SELAHHGPEDLfisiITIIGSFIILLTINVPLTLIVFALLPLM---- 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226477 222 ALLAIVIAK------TASRGQTA--YAKaatvVEQTIGSIRTVASFTGEKQAISNYNK 271
Cdd:cd18549 156 IIFTIYFNKkmkkafRRVREKIGeiNAQ----LEDSLSGIRVVKAFANEEYEIEKFDE 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
403-631 |
2.63e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlKWIRSKI---------GLVSQepvLF- 472
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVcpriaympqGLGKN---LYp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 473 TASIKDNIAY--------GKE-DATTEEIKAAAELAnasKFVDKlPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRI 543
Cdd:NF033858 92 TLSVFENLDFfgrlfgqdAAErRRRIDELLRATGLA---PFADR-PAG----------KLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 544 LLLDEATSALDAESERVVQEALDRIMVNRT--TVVVAhrlstvrNADM--------IAVIHQGKIVEKGSHTELL----- 608
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVA-------TAYMeeaerfdwLVAMDAGRVLATGTPAELLartga 230
|
250 260
....*....|....*....|...
gi 15226477 609 KDPEGAYSQLirLQEEKKSDENA 631
Cdd:NF033858 231 DTLEAAFIAL--LPEEKRRGHQP 251
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1043-1253 |
3.53e-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: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1043 ELRHVSFKYParPDVQIFqdlclsirAGKTVALVGESGSGKSTVIallqrfydpdsgeitldgveikslrlkwlrQQTGL 1122
Cdd:cd03227 4 LGRFPSYFVP--NDVTFG--------EGSLTIITGPNGSGKSTIL------------------------------DAIGL 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1123 VsqepilfneTIRANIAYGKGGDASESEIVSSAELSnahgFISGLqqgydtmvgergIQLSGGQKQRVAIARAI----VK 1198
Cdd:cd03227 44 A---------LGGAQSATRRRSGVKAGCIVAAVSAE----LIFTR------------LQLSGGEKELSALALILalasLK 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226477 1199 DPKVLLLDEATSALDAESERVVQDALDRVMVN-RTTIVVAHRLSTIKNADVIAVVK 1253
Cdd:cd03227 99 PRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
411-590 |
4.25e-04 |
|
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: 42.98 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 411 SGTTVaLVGQSGSGKSTvvslierfydpqagdvLIDGINLKEFQLKwIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTE 490
Cdd:cd03240 22 SPLTL-IVGQNGAGKTT----------------IIEALKYALTGEL-PPNSKGGAHDPKLIREGEVRAQVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 491 EIKAAAELA--NASKFVdklPQG-LDTMVGEHGTQLSGGQKQ------RIAVARAILKDPRILLLDEATSALDAEServV 561
Cdd:cd03240 84 KYTITRSLAilENVIFC---HQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---I 157
|
170 180 190
....*....|....*....|....*....|....*
gi 15226477 562 QEALDRIM------VNRTTVVVAHRLSTVRNADMI 590
Cdd:cd03240 158 EESLAEIIeerksqKNFQLIVITHDEELVDAADHI 192
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
522-604 |
7.02e-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: 41.58 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 522 QLSGGQKQRIAVARAI---LKDPRIL-LLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRNADmiAVIHQG 596
Cdd:cd03227 77 QLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELAD--KLIHIK 154
|
....*...
gi 15226477 597 KIVEKGSH 604
Cdd:cd03227 155 KVITGVYK 162
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1176-1266 |
7.14e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 1176 GERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLstIKNADVIA----V 1251
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQY--MEEAEQLAheltV 216
|
90
....*....|....*
gi 15226477 1252 VKNGVIVEKGKHDTL 1266
Cdd:NF000106 217 IDRGRVIADGKVDEL 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
499-607 |
8.88e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 499 ANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA 578
Cdd:NF000106 123 ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|.
gi 15226477 579 HRL--STVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:NF000106 201 TQYmeEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
759-878 |
9.48e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 42.85 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 759 TSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDepENSSGTIGARLSADAATIRGLVGD 838
Cdd:cd18606 34 QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD--TTPLGRILNRFSKDTDVLDNELPD 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15226477 839 SLAQTVQNLSSILA--GLIIAFLACWQLAFVVLAMLPLIALN 878
Cdd:cd18606 112 SLRMFLYTLSSIIGtfILIIIYLPWFAIALPPLLVLYYFIAN 153
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
523-602 |
9.54e-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: 41.54 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 523 LSGGQKQRIAVARAILKDPR--ILLLDEATSALDAESERVVQEALDRIMVNRTTV-VVAHRLSTVRNADMI------AVI 593
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTViLIEHNLDVLSSADWIidfgpgSGK 167
|
....*....
gi 15226477 594 HQGKIVEKG 602
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
384-566 |
1.04e-03 |
|
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: 43.39 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLI-DGInlkefqlkwirsKI 462
Cdd:TIGR03719 323 IEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 463 GLVSQEpvlftasiKDNIAYGKedATTEEIKAAAEL-----------ANASKFVDKlpqGLD--TMVGehgtQLSGGQKQ 529
Cdd:TIGR03719 388 AYVDQS--------RDALDPNK--TVWEEISGGLDIiklgkreipsrAYVGRFNFK---GSDqqKKVG----QLSGGERN 450
|
170 180 190
....*....|....*....|....*....|....*..
gi 15226477 530 RIAVARAILKDPRILLLDEATSALDAESERVVQEALD 566
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
854-977 |
1.38e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 42.42 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 854 LIIAFLAcWQLAFVVLAMLPLIALNGFLYMKFMKGFSadaKKMYGEASQ---VANDAVGSIRTVASFCAEDKVMNMYSKK 930
Cdd:cd18587 133 AVIALIG-GPLALVPLVAIPLVLLYGLLLQKPLRRLV---EESMRESAQknaLLVESLSGLETIKALGAEGRMQRRWEEA 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15226477 931 CEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18587 209 VAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELT 255
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1182-1249 |
1.76e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226477 1182 LSGGQKQRVAIARAIVKD---PKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVV-AHRLSTIKNADVI 1249
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYI 901
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
758-888 |
2.41e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 41.39 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 758 DTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDepENSSGTIGARLSADAATIRGLVG 837
Cdd:cd18599 56 DLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFD--TTPTGRILNRFSKDLDEVDVRLP 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15226477 838 DSLAQTVQNLSSILAGLIIaflACWQLAFVVLAMLPLIALNGFLYMKFMKG 888
Cdd:cd18599 134 FTLENFLQNVLLVVFSLII---IAIVFPWFLIALIPLAIIFVFLSKIFRRA 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
362-554 |
2.96e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 362 ERRPNIdsystnGKVLddikgdIELKD--VYftYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKS-TVVSLIERFYDP 438
Cdd:NF040905 248 ERTPKI------GEVV------FEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 439 Q-AGDVLIDGinlKEFQLKWIRskiglvsqepvlftASIKDNIAYGKEDATT------EEIKAAAELAN----------- 500
Cdd:NF040905 314 NiSGTVFKDG---KEVDVSTVS--------------DAIDAGLAYVTEDRKGyglnliDDIKRNITLANlgkvsrrgvid 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 501 -------ASKFVDKL----PqGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 554
Cdd:NF040905 377 eneeikvAEEYRKKMniktP-SVFQKVG----NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
763-977 |
3.46e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 40.96 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 763 AIIFMVLGFASIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSAdAATIRGLVGDSLAQ 842
Cdd:cd18783 46 IGVVIALLFEGILGY-LRRYLLLVATTRIDARLALRTFDRLLSLPIDFFER--TPAGVLTKHMQQ-IERIRQFLTGQLFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 843 TVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDK 922
Cdd:cd18783 122 TLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPR 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226477 923 VMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18783 202 QRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLT 256
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
836-977 |
3.79e-03 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 40.95 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 836 VGDSLAQtVQNLSSI---LAG---------------LIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFsADAKKMY 897
Cdd:cd18588 98 VGDTVAR-VRELESIrqfLTGsaltlvldlvfsvvfLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRR-LEEKFQR 175
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 898 GEASQ-VANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKT 976
Cdd:cd18588 176 GAENQsFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGEL 255
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gi 15226477 977 T 977
Cdd:cd18588 256 T 256
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| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
511-602 |
5.04e-03 |
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ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.93 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226477 511 GLD--TMVGEHGTqLSGGQKQRIAVARAI---LKDPrILLLDEATSALDAESERVVQEALDRIM-VNRTTVVVAHRLSTV 584
Cdd:cd03270 125 GLGylTLSRSAPT-LSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTI 202
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90 100
....*....|....*....|....
gi 15226477 585 RNADMI------AVIHQGKIVEKG 602
Cdd:cd03270 203 RAADHVidigpgAGVHGGEIVAQG 226
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| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
522-567 |
8.34e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.83 E-value: 8.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226477 522 QLSGGQKQRIA-------------VARAILKDPRILLLDEATSALDAESERVVQEALDR 567
Cdd:pfam13558 32 GLSGGEKQLLAylplaaalaaqygSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
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