|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
710-1295 |
1.40e-169 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 516.64 E-value: 1.40e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 710 KEKKVSFFRVAALNKPEIPMLILGSIAAVLNGVILPIFGILISSVIKAFFKPPEQlkSDTRFWAIIFMLLGVASMVVFPA 789
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDL--SALLLLLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 790 QTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFV 869
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 870 ASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGI 949
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 950 RQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTTFDSVFRVFFALTMAAVAISQSSSLSPDSSKASNAAASIFAVI 1029
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1030 DRESKIdPSDESGRVLDNVKGDIELRHISFKYPsrPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSG 1109
Cdd:COG1132 319 DEPPEI-PDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1110 QITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTMVGERG 1189
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP-DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1190 VQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVE 1269
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
570 580
....*....|....*....|....*.
gi 1063718281 1270 KGKHETLINiKDGVYASLVQLHLSAS 1295
Cdd:COG1132 555 QGTHEELLA-RGGLYARLYRLQFGEE 579
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
79-641 |
2.20e-165 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 505.47 E-value: 2.20e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 79 LMILGTIGAVGNGLGFPIMTILFGDVIDVFGQNQNSSdvsdKIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAGRIR 158
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLS----ALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 159 SLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVM 238
Cdd:COG1132 98 RDLFEHLLRLPLSFFD-RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 239 SGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNIVIF 318
Cdd:COG1132 177 VLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 319 CTYALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASPCLSAFAAGQAAAYKMFEAIKRKPEIDASDTTgKVLDD 398
Cdd:COG1132 257 LGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGA-VPLPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 399 IRGDIELNNVNFSYParPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIR 478
Cdd:COG1132 336 VRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILK 558
Cdd:COG1132 414 RQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLK 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 559 DPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDpEGAYSQLI 638
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLY 572
|
...
gi 1063718281 639 RLQ 641
Cdd:COG1132 573 RLQ 575
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-1290 |
8.49e-165 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 530.76 E-value: 8.49e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 16 PNRADAETSNSKIHEEDEKELKTESDLKEEKKKteknkqeedeKTKTVPFHKLFAFADSFDIILMILGTIGAVGNGLGFP 95
Cdd:PTZ00265 8 KKDNNSGGGNLSIKDEVEKELNKKGTFELYKKI----------KTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 96 IMTILFGdvidVFGQNQNssdVSDKIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAGRIRSLYLQTILRQDIAFFDv 175
Cdd:PTZ00265 78 FFVSVFG----VIMKNMN---LGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHD- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 176 eTNTGEVVgRMSGDTVLIQ--DAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAalaIVISKMASR 253
Cdd:PTZ00265 150 -NNPGSKL-TSDLDFYLEQvnAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGV---ICNKKVKIN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 254 GQTS--YAKAAV-VVEQTVGSIRTVASFTGEKQAISNYN--KHLVSAY--RAGVFEGastgLGLGTLNIVIFCTYALAVW 326
Cdd:PTZ00265 225 KKTSllYNNNTMsIIEEALVGIRTVVSYCGEKTILKKFNlsEKLYSKYilKANFMES----LHIGMINGFILASYAFGFW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 327 YGGKMILE--------KGYTGGQVLIIIFAVLTGSMSLGQASPCLSAFAAGQAAAYKMFEAIKRKPEIDASDTtGKVLDD 398
Cdd:PTZ00265 301 YGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDD-GKKLKD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 399 IRgDIELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRI-DGINLKEFQLKWI 477
Cdd:PTZ00265 380 IK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWW 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 478 RSKIGLVSQEPVLFTSSIKENIAYG----------------KENATVE-------------------------------- 509
Cdd:PTZ00265 459 RSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemr 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 510 ---EIRKATELANASK------FIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIV 580
Cdd:PTZ00265 539 knyQTIKDSEVVDVSKkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 581 QEALDRIM--VNRTTVVVAHRLSTVRNADMIAVI------------------------------HQGK------------ 616
Cdd:PTZ00265 619 QKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnKDDNnnnnnnnnnkin 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 617 -----IVEKGSHSELLRDPEGAYSQLIRLQEDTKQTEDSTDEQKLS-MESMKRSSlrksslsrslskrsssfSMFGF-PA 689
Cdd:PTZ00265 699 nagsyIIEQGTHDALMKNKNGIYYTMINNQKVSSKKSSNNDNDKDSdMKSSAYKD-----------------SERGYdPD 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 690 GIDTN----NEAIPEK------DIKVSTPIKEKKVSFFRVAALNKPEIPM---------------LILGSIAAVLNGVIL 744
Cdd:PTZ00265 762 EMNGNskheNESASNKksckmsDENASENNAGGKLPFLRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILVAGGLY 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 745 PIFGILISSVIKAFFKPPeQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDET 824
Cdd:PTZ00265 842 PVFALLYAKYVSTLFDFA-NLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQD 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 825 ENSSGAIGARLSADAATVR-GLVGDALaqtvqnlasVTAGLVIAFVASWQLAF----IVLAMLPliglngYIYMKFMVGF 899
Cdd:PTZ00265 921 KHAPGLLSAHINRDVHLLKtGLVNNIV---------IFTHFIVLFLVSMVMSFyfcpIVAAVLT------GTYFIFMRVF 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 900 SADAK-------------------------RMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIV 954
Cdd:PTZ00265 986 AIRARltankdvekkeinqpgtvfaynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLV 1065
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 955 SGI--GFGVSFFVLFSSYAasFYAGARLVDDGKTTFDSVFRVFFALTMAAVAISQSSSLSPDSSKASNAAASIFAVIDRE 1032
Cdd:PTZ00265 1066 NSMlwGFSQSAQLFINSFA--YWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRK 1143
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1033 SKIDPSDESGRVLDN---VKGDIELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYD---- 1105
Cdd:PTZ00265 1144 SNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlknd 1223
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1106 --------------------------------------------------PDSGQITLDGVEIKTLQLKWLRQQTGLVSQ 1135
Cdd:PTZ00265 1224 hhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQ 1303
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1136 EPVLFNETIRANIAYGKgGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLL 1215
Cdd:PTZ00265 1304 EPMLFNMSIYENIKFGK-EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLL 1382
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1216 DEATSALDAESERVVQ----DALDRvmVNRTTVVVAHRLSTIKNADVIAVVKN----GVIVE-KGKHETLINIKDGVYAS 1286
Cdd:PTZ00265 1383 DEATSSLDSNSEKLIEktivDIKDK--ADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYKK 1460
|
....
gi 1063718281 1287 LVQL 1290
Cdd:PTZ00265 1461 YVKL 1464
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
403-641 |
2.76e-136 |
|
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: 415.40 E-value: 2.76e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRdPEGAYSQLIRLQ 641
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1052-1290 |
7.56e-136 |
|
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: 414.24 E-value: 7.56e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASLVQL 1290
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKA 237
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
129-641 |
2.25e-127 |
|
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: 404.85 E-value: 2.25e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 129 VYLGLGTLVAALLQVSGWMisGERQAGRIRSLYLQTILRQDIAFFDVeTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLV 208
Cdd:TIGR02204 67 VALVLALGTAARFYLVTWL--GERVVADIRRAVFAHLISLSPSFFDK-NRSGEVVSRLTTDTTLLQSVIGSSLSMALRNA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 209 STFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNY 288
Cdd:TIGR02204 144 LMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRF 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 289 NKHLVSAYRAGVFEGASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASPCLSAFAA 368
Cdd:TIGR02204 224 GGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 369 GQAAAYKMFEAIKRKPEIDASDTTGKVLDDIRGDIELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVV 448
Cdd:TIGR02204 304 AAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLF 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 449 SLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLP 528
Cdd:TIGR02204 384 QLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALP 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 529 QGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADM 608
Cdd:TIGR02204 464 EGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADR 543
|
490 500 510
....*....|....*....|....*....|...
gi 1063718281 609 IAVIHQGKIVEKGSHSELLRDpEGAYSQLIRLQ 641
Cdd:TIGR02204 544 IVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
716-1289 |
9.90e-127 |
|
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: 408.07 E-value: 9.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 716 FFRVAALNKPEIPMLILGSIAAVLNGVILPIF-GILISSVIkaffkpPEQLkSDTRFWAIIFMLLGVASMVVFP-AQTIF 793
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFtQVVIDRVL------PNQD-LSTLWVLAIGLLLALLFEGLLRlLRSYL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 794 FSIAGCKLVQRIRSMCFEKVVRMEVGWFDETenSSGAIGARLSaDAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQ 873
Cdd:COG2274 220 LLRLGQRIDLRLSSRFFRHLLRLPLSFFESR--SVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 874 LAFIVLAMLPLIGLNGYIYMKFMVgfSADAKRMYEEASQVAN--DAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQ 951
Cdd:COG2274 297 LALVVLLLIPLYVLLGLLFQPRLR--RLSREESEASAKRQSLlvETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 952 GIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTT-----------------FDSVFRVFFALTMAAVAISQssslspd 1014
Cdd:COG2274 375 RRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTlgqliafnilsgrflapVAQLIGLLQRFQDAKIALER------- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1015 sskasnaaasIFAVIDRESKIDPsDESGRVLDNVKGDIELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKS 1094
Cdd:COG2274 448 ----------LDDILDLPPEREE-GRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1095 TVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFI 1174
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDP-DATDEEIIEAARLAGLHDFI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1175 SGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIK 1254
Cdd:COG2274 595 EALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIR 674
|
570 580 590
....*....|....*....|....*....|....*
gi 1063718281 1255 NADVIAVVKNGVIVEKGKHETLINiKDGVYASLVQ 1289
Cdd:COG2274 675 LADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQ 708
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
57-641 |
8.12e-126 |
|
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: 405.37 E-value: 8.12e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 57 DEKTKTVPFHKLFAFADSF--DIILMILGTIGAVGNGLGFPIMT-ILFGDVIdvFGQNQNSSDVsdkiakvalkfvyLGL 133
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYrrLLLQVLLASLLINLLALATPLFTqVVIDRVL--PNQDLSTLWV-------------LAI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 134 GTLVAALLQVS-----GWMIS--GERQAGRIRSLYLQTILRQDIAFFDVETnTGEVVGRMSgDTVLIQDAM-GEKVGKAI 205
Cdd:COG2274 201 GLLLALLFEGLlrllrSYLLLrlGQRIDLRLSSRFFRHLLRLPLSFFESRS-VGDLASRFR-DVESIREFLtGSLLTALL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 206 QLVSTFIGGFVIAFTeGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAI 285
Cdd:COG2274 279 DLLFVLIFLIVLFFY-SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 286 SNYNKHLVSAYRAGvFEGASTGLGLGTLNIVIF-CTYALAVWYGGKMILEKGYTGGQVL---IIIFAVLTGSMSLGQAsp 361
Cdd:COG2274 358 RRWENLLAKYLNAR-FKLRRLSNLLSTLSGLLQqLATVALLWLGAYLVIDGQLTLGQLIafnILSGRFLAPVAQLIGL-- 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 362 cLSAFAAGQAAAYKMFEAIKRKPEIDASDTTgKVLDDIRGDIELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSG 441
Cdd:COG2274 435 -LQRFQDAKIALERLDDILDLPPEREEGRSK-LSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSG 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 442 SGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANAS 521
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLH 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 522 KFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLS 601
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1063718281 602 TVRNADMIAVIHQGKIVEKGSHSELLrDPEGAYSQLIRLQ 641
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELL-ARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
715-1287 |
4.04e-125 |
|
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: 398.71 E-value: 4.04e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 715 SFFRVAALNKPEIPMLILGSIAAVLNGVILPIFGILISSVIKAFF--KPPEQLKSDTRFWAIIFMLLGVASMVvfpaQTI 792
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFggRDRSVLWWVPLVVIGLAVLRGICSFV----STY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 793 FFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASW 872
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 873 QLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQG 952
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 953 IVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTTFDSVFRVFFALTMAAVAISQSSSLSPDSSKASNAAASIFAVIDRE 1032
Cdd:TIGR02203 235 SAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1033 skiDPSDESGRVLDNVKGDIELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQIT 1112
Cdd:TIGR02203 315 ---PEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1113 LDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQL 1192
Cdd:TIGR02203 391 LDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1193 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGK 1272
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGT 550
|
570
....*....|....*
gi 1063718281 1273 HETLINiKDGVYASL 1287
Cdd:TIGR02203 551 HNELLA-RNGLYAQL 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
710-1288 |
2.03e-124 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 401.79 E-value: 2.03e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 710 KEKKVSFFRVAALNKPEIPMLILG---SIAAVLNGVILPIF-GILISSVIKAffKPPEQLKSdtrfwAIIFM-LLGVASM 784
Cdd:TIGR00958 143 SETADLLFRLLGLSGRDWPWLISAfvfLTLSSLGEMFIPFYtGRVIDTLGGD--KGPPALAS-----AIFFMcLLSIASS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 785 VVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGL 864
Cdd:TIGR00958 216 VSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 865 VIAFVASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGP 944
Cdd:TIGR00958 294 GFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEET 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 945 MRTGIRQGIVsgigfgVSFFVLFSSYAASF------YAGARLVDDGKTTFDSVfrVFFALTMAAV--AISQSSSLSPDSS 1016
Cdd:TIGR00958 374 LQLNKRKALA------YAGYLWTTSVLGMLiqvlvlYYGGQLVLTGKVSSGNL--VSFLLYQEQLgeAVRVLSYVYSGMM 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1017 KASNAAASIFAVIDRESKIDPSdeSGRVLDNVKGDIELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTV 1096
Cdd:TIGR00958 446 QAVGASEKVFEYLDRKPNIPLT--GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1097 IALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKgGDATETEIVSAAELSNAHGFISG 1176
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL-TDTPDEEIMAAAKAANAHDFIME 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1177 LQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDalDRVMVNRTTVVVAHRLSTIKNA 1256
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERA 680
|
570 580 590
....*....|....*....|....*....|..
gi 1063718281 1257 DVIAVVKNGVIVEKGKHETLINiKDGVYASLV 1288
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLME-DQGCYKHLV 711
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
102-638 |
1.63e-119 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 388.31 E-value: 1.63e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 102 GDVIDVFGQNQNSSDVSDKIAKVALkfvyLGLGTLVAALLQVSGWMISGERQAGRIRSLYLQTILRQDIAFFDvETNTGE 181
Cdd:TIGR00958 185 GRVIDTLGGDKGPPALASAIFFMCL----LSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD-ENKTGE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 182 VVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKA 261
Cdd:TIGR00958 260 LTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 262 AVVVEQTVGSIRTVASFTGEKQAISNYN---KHLVSAYRAGVFEGA-----STGLGLGTLNIVIfctyalavWYGGKMIL 333
Cdd:TIGR00958 340 NQVAEEALSGMRTVRSFAAEEGEASRFKealEETLQLNKRKALAYAgylwtTSVLGMLIQVLVL--------YYGGQLVL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 334 EKGYTGGQVLiiifAVLTGSMSLGQASPCLSAFAAGQAAAY----KMFEAIKRKPEIdaSDTTGKVLDDIRGDIELNNVN 409
Cdd:TIGR00958 412 TGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSGMMQAVgaseKVFEYLDRKPNI--PLTGTLAPLNLEGLIEFQDVS 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 410 FSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPV 489
Cdd:TIGR00958 486 FSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPV 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 490 LFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEAT 569
Cdd:TIGR00958 566 LFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 570 SALDAESERIVQEalDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSElLRDPEGAYSQLI 638
Cdd:TIGR00958 646 SALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ-LMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
720-1035 |
1.28e-113 |
|
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: 358.30 E-value: 1.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 720 AALNKPEIPMLILGSIAAVLNGVILPIFGILISSVIKAFFKP-PEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAG 798
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPdDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 799 CKLVQRIRSMCFEKVVRMEVGWFDETENSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIV 878
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 879 LAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIG 958
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 959 FGVSFFVLFSSYAASFYAGARLVDDGKTTFDSVFRVFFALTMAAVAISQSSSLSPDSSKASNAAASIFAVIDRESKI 1035
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
403-637 |
1.33e-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: 1.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLrDPEGAYSQL 637
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL-AQGGVYAKL 233
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
80-364 |
6.33e-110 |
|
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: 347.54 E-value: 6.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 80 MILGTIGAVGNGLGFPIMTILFGDVIDVFGQ----NQNSSDVSDKIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAG 155
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 156 RIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPL 235
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD-KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 236 LVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNI 315
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063718281 316 VIFCTYALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASPCLS 364
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQ 288
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1052-1287 |
1.79e-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: 341.13 E-value: 1.79e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRP-GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASL 1287
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
730-1291 |
7.92e-107 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 349.70 E-value: 7.92e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIKAFFKppeqlKSDTRFwaIIFMLLGVASMVVFPAQTIFFS------IAGcKLVQ 803
Cdd:PRK11176 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFG-----KADRSV--LKWMPLVVIGLMILRGITSFISsyciswVSG-KVVM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 804 RIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLP 883
Cdd:PRK11176 99 TMRRRLFGHMMGMPVSFFDK--QSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 884 LIGLNGYIYMKfmvGFSADAKRMYEEASQVANDAVGSI---RTVASFcAEEKVMKMYKKKCEGPMRtgiRQG--IVSG-- 956
Cdd:PRK11176 177 IVSIAIRVVSK---RFRNISKNMQNTMGQVTTSAEQMLkghKEVLIF-GGQEVETKRFDKVSNRMR---QQGmkMVSAss 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 957 -----IGFGVSFFVLFSSYAASFYAGARLVDDGktTFDSVFRVFFALT----------------MAAVaisqssslspds 1015
Cdd:PRK11176 250 isdpiIQLIASLALAFVLYAASFPSVMDTLTAG--TITVVFSSMIALMrplksltnvnaqfqrgMAAC------------ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1016 skasnaaASIFAVIDRESKidpSDESGRVLDNVKGDIELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKST 1095
Cdd:PRK11176 316 -------QTLFAILDLEQE---KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKST 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1096 VIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGGDATETEIVSAAELSNAHGFIS 1175
Cdd:PRK11176 385 IANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFIN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1176 GLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKN 1255
Cdd:PRK11176 465 KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK 544
|
570 580 590
....*....|....*....|....*....|....*.
gi 1063718281 1256 ADVIAVVKNGVIVEKGKHETLINiKDGVYAslvQLH 1291
Cdd:PRK11176 545 ADEILVVEDGEIVERGTHAELLA-QNGVYA---QLH 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
65-644 |
9.47e-106 |
|
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: 346.32 E-value: 9.47e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 65 FHKLFAFADSFDIILmILGTIGAVGNGLGFPIMTILFGDVID-VFGQNQNSSDVSDKIAKVALkFVYLGLGTLVA--ALL 141
Cdd:TIGR02203 2 FRRLWSYVRPYKAGL-VLAGVAMILVAATESTLAALLKPLLDdGFGGRDRSVLWWVPLVVIGL-AVLRGICSFVStyLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 142 QVSGWMISGerqagrIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGD------------TVLIQDAMgekvgkaiqlvs 209
Cdd:TIGR02203 80 WVSNKVVRD------IRVRMFEKLLGLPVSFFD-RQPTGTLLSRITFDseqvasaatdafIVLVRETL------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 210 TFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYN 289
Cdd:TIGR02203 141 TVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 290 KHLVSAYRAGVFEGASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASPCLSAFAAG 369
Cdd:TIGR02203 221 AVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 370 QAAAYKMFEAIKRKPEIDasdTTGKVLDDIRGDIELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVS 449
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 450 LIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGK-ENATVEEIRKATELANASKFIDKLP 528
Cdd:TIGR02203 377 LIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 529 QGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADM 608
Cdd:TIGR02203 457 LGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADR 536
|
570 580 590
....*....|....*....|....*....|....*.
gi 1063718281 609 IAVIHQGKIVEKGSHSELLrDPEGAYSQLIRLQEDT 644
Cdd:TIGR02203 537 IVVMDDGRIVERGTHNELL-ARNGLYAQLHNMQFRE 571
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
375-653 |
3.47e-105 |
|
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: 346.04 E-value: 3.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 375 KMFEAIKRKPEI-DASDTtgKVLDDIRGDIELNNVNFSYpaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIER 453
Cdd:COG5265 331 RMFDLLDQPPEVaDAPDA--PPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 454 FYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDT 533
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDT 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 534 MVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIH 613
Cdd:COG5265 487 RVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLE 566
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1063718281 614 QGKIVEKGSHSELLRDpEGAYSQLIRLQEDTKQTEDSTDE 653
Cdd:COG5265 567 AGRIVERGTHAELLAQ-GGLYAQMWARQQEEEEAEEALAA 605
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1026-1290 |
6.54e-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: 342.57 E-value: 6.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1026 FAVIDRESKI-DPSDesGRVLDNVKGDIELRHISFKYpsRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFY 1104
Cdd:COG5265 333 FDLLDQPPEVaDAPD--APPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1105 DPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTM 1184
Cdd:COG5265 409 DVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP-DASEEEVEAAARAAQIHDFIESLPDGYDTR 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1185 VGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKN 1264
Cdd:COG5265 488 VGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEA 567
|
250 260
....*....|....*....|....*.
gi 1063718281 1265 GVIVEKGKHETLINiKDGVYASLVQL 1290
Cdd:COG5265 568 GRIVERGTHAELLA-QGGLYAQMWAR 592
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1052-1287 |
2.61e-102 |
|
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: 324.57 E-value: 2.61e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRP-DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASL 1287
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 ... |
403-641 |
3.39e-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: 318.79 E-value: 3.39e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLrDPEGAYSQLIRLQ 641
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
157-641 |
1.16e-98 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 327.36 E-value: 1.16e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 157 IRSLYLQTILRQDIAFFDVETnTGEVVGRMSGDTVLIQDAMGekvGKAIQLV---STFIGGFVIAFTEGWLLTLVMVSSI 233
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQS-TGTLLSRITYDSEQVASSSS---GALITVVregASIIGLFIMMFYYSWQLSLILIVIA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 234 PLLvmsgaALAI-VISK----MASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNK----------HLVSAyra 298
Cdd:PRK11176 176 PIV-----SIAIrVVSKrfrnISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKvsnrmrqqgmKMVSA--- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 299 gvfEGASTGLglgtlnIVIFCTYALA-VWYGGKM--ILEKgYTGGQvliiiFAVLTGSMsLGQASPCLSAFAAGQAAAYK 375
Cdd:PRK11176 248 ---SSISDPI------IQLIASLALAfVLYAASFpsVMDT-LTAGT-----ITVVFSSM-IALMRPLKSLTNVNAQFQRG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 376 M------FEAIKRKPEIDasdtTGK-VLDDIRGDIELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVV 448
Cdd:PRK11176 312 MaacqtlFAILDLEQEKD----EGKrVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 449 SLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENA-TVEEIRKATELANASKFIDKL 527
Cdd:PRK11176 387 NLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKM 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 528 PQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNAD 607
Cdd:PRK11176 467 DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
|
490 500 510
....*....|....*....|....*....|....
gi 1063718281 608 MIAVIHQGKIVEKGSHSELLRDpEGAYSQLIRLQ 641
Cdd:PRK11176 547 EILVVEDGEIVERGTHAELLAQ-NGVYAQLHKMQ 579
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
718-1277 |
2.48e-98 |
|
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: 325.94 E-value: 2.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 718 RVAALNKPEIPMLILGSIAAVLNGVILPIFGILISSVI-KAFFKppEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSI 796
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLIIG--GAPLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 797 AGCKLVQRIRSMCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVqnLASVTAGLVIAFVA--SWQL 874
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLLTEGVEALDGYFARYLPQLF--LAALVPLLILVAVFplDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 875 AFIVLAMLPLIGLngyiymkFM--VGFSADAK--RMYEEASQVAN---DAVGSIRTVASFCAEEKVMKMYKKKCEG---- 943
Cdd:COG4988 161 GLILLVTAPLIPL-------FMilVGKGAAKAsrRQWRALARLSGhflDRLRGLTTLKLFGRAKAEAERIAEASEDfrkr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 944 PMRTgIRqgivsgIGFgVSFFVL-FSSY----AASFYAGARLVDdGKTTFdsvFRVFFAL-------------------T 999
Cdd:COG4988 234 TMKV-LR------VAF-LSSAVLeFFASlsiaLVAVYIGFRLLG-GSLTL---FAALFVLllapefflplrdlgsfyhaR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1000 MAAVAisqssslspdsskasnAAASIFAVIDRESKIDPSDESGRVLDNvKGDIELRHISFKYPSRPdvQIFQDLCLSIRA 1079
Cdd:COG4988 302 ANGIA----------------AAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1080 GKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDATET 1159
Cdd:COG4988 363 GERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRP-DASDE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1160 EIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMV 1239
Cdd:COG4988 442 ELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK 521
|
570 580 590
....*....|....*....|....*....|....*...
gi 1063718281 1240 NRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLI 1277
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
401-627 |
5.30e-98 |
|
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: 312.24 E-value: 5.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYpaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSK 480
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 560
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 561 RILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELL 627
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
375-628 |
4.57e-93 |
|
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: 311.31 E-value: 4.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 375 KMFEAIKRKPEIDASDTTgKVLDDIRGDIELNNVNFSYPARpeEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERF 454
Cdd:COG4988 310 KIFALLDAPEPAAPAGTA-PLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 455 YDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTM 534
Cdd:COG4988 387 LPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 535 VGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQ 614
Cdd:COG4988 467 LGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDD 546
|
250
....*....|....
gi 1063718281 615 GKIVEKGSHSELLR 628
Cdd:COG4988 547 GRIVEQGTHEELLA 560
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1025-1288 |
1.45e-91 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 308.04 E-value: 1.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1025 IFAVIDRESKIDPSdesgrvldNVKGDIELRHISFKYPSRPdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFY 1104
Cdd:PRK13657 316 VPDVRDPPGAIDLG--------RVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1105 DPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTM 1184
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHDFIERKPDGYDTV 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1185 VGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKN 1264
Cdd:PRK13657 465 VGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
250 260
....*....|....*....|....
gi 1063718281 1265 GVIVEKGKHETLINiKDGVYASLV 1288
Cdd:PRK13657 545 GRVVESGSFDELVA-RGGRFAALL 567
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
396-641 |
2.10e-91 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 307.27 E-value: 2.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 396 LDDIRGDIELNNVNFSYPARPeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLK 475
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 476 WIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARA 555
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLrDPEGAYS 635
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV-ARGGRFA 564
|
....*.
gi 1063718281 636 QLIRLQ 641
Cdd:PRK13657 565 ALLRAQ 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1050-1281 |
3.03e-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: 291.05 E-value: 3.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDIELRHISFKYpsRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQ 1129
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKD 1209
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRP-NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1210 PKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIKD 1281
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
131-640 |
9.07e-88 |
|
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: 296.68 E-value: 9.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 131 LGLGTLVA--ALLQVSGWMIS------------------------------GER---------QAGRIRSLYLQTILRQD 169
Cdd:COG4987 23 LGLLTLLAgiGLLALSGWLIAaaalappilnlfvpivgvrafaigrtvfryLERlvshdatlrLLADLRVRLYRRLEPLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 170 IAFFdVETNTGEVVGRMSGDTvliqDAMGEKVGKAIQ--LVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVI 247
Cdd:COG4987 103 PAGL-ARLRSGDLLNRLVADV----DALDNLYLRVLLplLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 248 SKMASRGQTSYAKAAVVVEQTVGSIRTVASFT------GEKQAISNYNKHLVSA-YRAGVFEGASTGLGLGTLNIVIfct 320
Cdd:COG4987 178 RLGRRAGRRLAAARAALRARLTDLLQGAAELAaygaldRALARLDAAEARLAAAqRRLARLSALAQALLQLAAGLAV--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 321 yALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASPCLSAFAAGQAAAYKMFEAIKRKPEIDASDTTGKVLDDir 400
Cdd:COG4987 255 -VAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGG-- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYPARPEeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSK 480
Cdd:COG4987 332 PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 560
Cdd:COG4987 411 IAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 561 RILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPeGAYSQLIRL 640
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1052-1290 |
3.48e-86 |
|
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: 280.14 E-value: 3.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYpsRPD-VQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQT 1130
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLFNETIRANIAYGKGGDATEtEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDP 1210
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSME-RVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1211 KVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASLVQL 1290
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLYQL 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
716-1290 |
6.10e-86 |
|
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: 291.67 E-value: 6.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 716 FFRVAALNKPEIPMLILG---SIAAVLNGVILPIF-GILISsviKAFFKPPeqlksdtrfwaiIFMLLGVASMVvfpaqt 791
Cdd:COG4987 3 LLRLLRLLRPHRGRLLLGvllGLLTLLAGIGLLALsGWLIA---AAALAPP------------ILNLFVPIVGV------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 792 IFFSI---------------AGCKLVQRIRSMCFEKVVRMEVGWFdeTENSSGAIGARLSADAATVRGLVGDALAQTVqn 856
Cdd:COG4987 62 RAFAIgrtvfrylerlvshdATLRLLADLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLYLRVLLPLL-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 857 LASVTAGLVIAFVA--SWQLAFIVLAMLPLIGLNG-YIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKV 933
Cdd:COG4987 138 VALLVILAAVAFLAffSPALALVLALGLLLAGLLLpLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 934 MKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGktTFDSVFRVFFALTMAAV--AISQSSSL 1011
Cdd:COG4987 218 LARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAG--ALSGPLLALLVLAALALfeALAPLPAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1012 SPDSSKASNAAASIFAVIDRESKIdpSDESGRVLDNVKGDIELRHISFKYPSRPDvQIFQDLCLSIRAGKTIALVGESGS 1091
Cdd:COG4987 296 AQHLGRVRAAARRLNELLDAPPAV--TEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1092 GKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAH 1171
Cdd:COG4987 373 GKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP-DATDEELWAALERVGLG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1172 GFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLS 1251
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
570 580 590
....*....|....*....|....*....|....*....
gi 1063718281 1252 TIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASLVQL 1290
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLA-QNGRYRQLYQR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1046-1267 |
1.21e-84 |
|
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: 275.50 E-value: 1.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1046 DNVKGDIELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKW 1125
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 LRQQTGLVSQEPVLFNETIRANIAYGKGGDATEtEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARA 1205
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFE-CVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVI 1267
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
403-641 |
1.83e-82 |
|
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: 269.74 E-value: 1.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYpaRPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKI 481
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 561
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 562 ILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDpEGAYSQLIRLQ 641
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
397-617 |
7.73e-82 |
|
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: 267.41 E-value: 7.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 397 DDIRGDIELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKW 476
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 IRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAI 556
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 557 LKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKI 617
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
225-643 |
2.87e-81 |
|
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: 282.02 E-value: 2.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 225 LTLVMVSSIPL-LVMSGAALAIVISKMASRGQTSYAKAAVVVEqTVGSIRTVASFTGEKQAISNYNKHLvSAYRAGVFEG 303
Cdd:TIGR01846 280 LTGVVIGSLVCyALLSVFVGPILRKRVEDKFERSAAATSFLVE-SVTGIETIKATATEPQFQNRWDRQL-AAYVAASFRV 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 304 ASTG-LGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQvlIIIFAVLTGSMSlgqaSPCLSAFAAgqaaaYKMFE---- 378
Cdd:TIGR01846 358 TNLGnIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ--LVAFNMLAGRVT----QPVLRLAQL-----WQDFQqtgi 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 379 AIKRKPEI-----DASDTTGKVLDDIRGDIELNNVNFSY-PARPEeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIE 452
Cdd:TIGR01846 427 ALERLGDIlnsptEPRSAGLAALPELRGAITFENIRFRYaPDSPE--VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 453 RFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLD 532
Cdd:TIGR01846 505 RLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYN 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 533 TMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVI 612
Cdd:TIGR01846 585 TEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVL 664
|
410 420 430
....*....|....*....|....*....|.
gi 1063718281 613 HQGKIVEKGSHSELLRDpEGAYSQLIRLQED 643
Cdd:TIGR01846 665 EKGQIAESGRHEELLAL-QGLYARLWQQQSG 694
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
403-616 |
5.94e-80 |
|
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: 260.01 E-value: 5.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIaygkenatveeirkatelanaskfidklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGK 616
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1052-1265 |
3.12e-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: 3.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIaygkggdateteivsaaelsnahgfisglqqgydtmvgergvqLSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNG 1265
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
730-1005 |
7.27e-77 |
|
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: 256.25 E-value: 7.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIKAF------FKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQ 803
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 804 RIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLP 883
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 884 LIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSF 963
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1063718281 964 FVLFSSYAASFYAGARLVDDGKTTFDSVFRVFFALTMAAVAI 1005
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSL 280
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
76-386 |
1.49e-76 |
|
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: 256.22 E-value: 1.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 76 DIILMILGTIGAVGNGLGFPIMTILFGDVIDVFgQNQNSSDVSDKIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAG 155
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVF-SLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 156 RIRSLYLQTILRQDIAFFDVETN-TGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIP 234
Cdd:cd18578 86 RLRKLAFRAILRQDIAWFDDPENsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 235 LLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLN 314
Cdd:cd18578 166 LLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQ 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 315 IVIFCTYALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASPCLSAFAAGQAAAYKMFEAIKRKPEI 386
Cdd:cd18578 246 SLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1027-1289 |
6.25e-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: 249.42 E-value: 6.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1027 AVIDREskiDPSDesGRVLDNVKGDIELRHISFKYPSRPdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDP 1106
Cdd:TIGR01192 315 SVFQRE---EPAD--APELPNVKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1107 DSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTMVG 1186
Cdd:TIGR01192 388 TVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGRE-GATDEEVYEAAKAAAAHDFILKRSNGYDTLVG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1187 ERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGV 1266
Cdd:TIGR01192 467 ERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGR 546
|
250 260
....*....|....*....|...
gi 1063718281 1267 IVEKGKHETLINiKDGVYASLVQ 1289
Cdd:TIGR01192 547 LIEKGSFQELIQ-KDGRFYKLLR 568
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
401-621 |
6.74e-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: 236.33 E-value: 6.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYPARPEEQIfRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSK 480
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 560
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 561 RILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 621
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1050-1271 |
3.05e-67 |
|
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: 225.93 E-value: 3.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDIELRHISFKYPSRPDVQIfQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQ 1129
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLFNETIRANIAYGkGGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKD 1209
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1210 PKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
206-639 |
4.73e-67 |
|
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: 237.86 E-value: 4.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 206 QLVSTFIGGFVI---AFTEGWLLTLVMvssipllvMSGAALAIVISKMAsRGQTSYAKAAVV---------VEQTVGSIR 273
Cdd:TIGR01192 136 QHLATFVALFLLiptAFAMDWRLSIVL--------MVLGILYILIAKLV-MQRTKNGQAAVEhhyhnvfkhVSDSISNVS 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 274 TVASF---TGEKQAISNYNKHLVSA-YRAGVFEGASTGLGLGTLNIVIFCTYALavwygGKMILEKGYTG-GQVLIII-F 347
Cdd:TIGR01192 207 VVHSYnriEAETSALKQFTNNLLSAqYPVLDWWALASGLNRMASTISMMCILVI-----GTVLVIKGELSvGEVIAFIgF 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 348 A-VLTGSmsLGQASPCLSAFAAGQAAAYKMF---EAIKRKPE-IDASDttgkvLDDIRGDIELNNVNFSYPArpEEQIFR 422
Cdd:TIGR01192 282 AnLLIGR--LDQMSGFITQIFEARAKLEDFFdleDSVFQREEpADAPE-----LPNVKGAVEFRHITFEFAN--SSQGVF 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYG 502
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLG 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 503 KENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQE 582
Cdd:TIGR01192 433 REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKN 512
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 583 ALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDpEGAYSQLIR 639
Cdd:TIGR01192 513 AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK-DGRFYKLLR 568
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
401-622 |
3.02e-66 |
|
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: 223.14 E-value: 3.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYpaRPEEQ-IFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRS 479
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFTSSIKENIAYGKEnATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGS 622
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
728-1262 |
2.58e-65 |
|
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: 231.41 E-value: 2.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 728 PMLILGSIAAVLNGVILPIFGILISSVIKAFFKPPEQLkSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRS 807
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPL-AELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 808 MCFEKVVRMEVGWfdetenssgaIGARLSADAAT--VRGLvgDALA------QTVQNLASVTAGLVIAFV--ASWQLAFI 877
Cdd:TIGR02857 82 RLLEAVAALGPRW----------LQGRPSGELATlaLEGV--EALDgyfaryLPQLVLAVIVPLAILAAVfpQDWISGLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 878 VLAMLPLIGLngyiymkFM--VGFSADAK--RMYEEASQVAN---DAVGSIRTVASFCAE-------EKVMKMYKKKCeg 943
Cdd:TIGR02857 150 LLLTAPLIPI-------FMilIGWAAQAAarKQWAALSRLSGhflDRLRGLPTLKLFGRAkaqaaaiRRSSEEYRERT-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 944 pMRTgIRQGIVSGigFGVSFFVLFSSYAASFYAGARLVDdGKTTFdsvFRVFFAL-------------------TMAAVA 1004
Cdd:TIGR02857 221 -MRV-LRIAFLSS--AVLELFATLSVALVAVYIGFRLLA-GDLDL---ATGLFVLllapefylplrqlgaqyhaRADGVA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1005 isqssslspdsskasnAAASIFAVIDRESKIDPSDESgrVLDNVKGDIELRHISFKYPSRPDVqiFQDLCLSIRAGKTIA 1084
Cdd:TIGR02857 293 ----------------AAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1085 LVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDATETEIVSA 1164
Cdd:TIGR02857 353 LVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARP-DASDAEIREA 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1165 AELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTV 1244
Cdd:TIGR02857 432 LERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVL 511
|
570
....*....|....*...
gi 1063718281 1245 VVAHRLSTIKNADVIAVV 1262
Cdd:TIGR02857 512 LVTHRLALAALADRIVVL 529
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
315-1289 |
3.24e-65 |
|
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: 243.70 E-value: 3.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 315 IVIFCTYALAVWYGGKMIL--EKGYtggqVLIIIFAVLTGSMSLgqaSPCLSAFAAGQAAAYKMFEAIKRKPEIDASDTT 392
Cdd:TIGR00957 553 LVALITFAVYVTVDENNILdaEKAF----VSLALFNILRFPLNI---LPMVISSIVQASVSLKRLRIFLSHEELEPDSIE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 393 GKVLDDIRGD-IELNNVNFSYpARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlke 471
Cdd:TIGR00957 626 RRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----- 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 472 fqlkwirsKIGLVSQEPVLFTSSIKENIAYGK---ENATVEEIRKATELANaskfIDKLPQGLDTMVGEHGTQLSGGQKQ 548
Cdd:TIGR00957 700 --------SVAYVPQQAWIQNDSLRENILFGKalnEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQ 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 549 RIAVARAILKDPRILLLDEATSALDAESERIVQEAL---DRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSE 625
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQE 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 626 LLrDPEGAYSQLIR----------LQEDTKQTEDSTDEQKLSMESMKRSSLRKSSLSRSLSKRSSSFSMfgfpagiDTNN 695
Cdd:TIGR00957 848 LL-QRDGAFAEFLRtyapdeqqghLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSG-------DQSR 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 696 EAIPEKDIKVStpikEKKVSFFRVAALNKPEIPMLILGSI-----AAVLNGVILPIFGILISSV--------IKAFFKPP 762
Cdd:TIGR00957 920 HHGSSAELQKA----EAKEETWKLMEADKAQTGQVELSVYwdymkAIGLFITFLSIFLFVCNHVsalasnywLSLWTDDP 995
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 763 --EQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETenSSGAIGARLSADAA 840
Cdd:TIGR00957 996 mvNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERT--PSGNLVNRFSKELD 1073
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 841 TVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVlamlPLIGLNGYIYMKFMVGFSADAKRMyEEASQVA-----N 915
Cdd:TIGR00957 1074 TVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVII----PPLGLLYFFVQRFYVASSRQLKRL-ESVSRSPvyshfN 1148
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 916 DAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTgIRQGIVSG--IGFGVSF----FVLFSSYAA-----SFYAGarLVddG 984
Cdd:TIGR00957 1149 ETLLGVSVIRAFEEQERFIHQSDLKVDENQKA-YYPSIVANrwLAVRLECvgncIVLFAALFAvisrhSLSAG--LV--G 1223
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 985 KTTFDSVfRVFFALTMaavaisqssslspDSSKASNAAASIFAVIDRESKIDPSDESGRVLDNVK--------GDIELRH 1056
Cdd:TIGR00957 1224 LSVSYSL-QVTFYLNW-------------LVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAppsgwpprGRVEFRN 1289
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1057 ISFKYpsRPDVQ-IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQ 1135
Cdd:TIGR00957 1290 YCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ 1367
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1136 EPVLFNETIRANIayGKGGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLL 1215
Cdd:TIGR00957 1368 DPVLFSGSLRMNL--DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVL 1445
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1216 DEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIKdGVYASLVQ 1289
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
403-612 |
3.01e-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: 228.33 E-value: 3.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 562
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVI 612
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
378-639 |
4.68e-64 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 228.94 E-value: 4.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 378 EAIKRKPEIDASDTTGKVLDdiRGDIELNNVNFSYPARPEeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDP 457
Cdd:PRK11160 316 EITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 458 QSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKlPQGLDTMVGE 537
Cdd:PRK11160 393 QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 538 HGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKI 617
Cdd:PRK11160 472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
250 260
....*....|....*....|..
gi 1063718281 618 VEKGSHSELLRDpEGAYSQLIR 639
Cdd:PRK11160 552 IEQGTHQELLAQ-QGRYYQLKQ 572
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
77-641 |
5.91e-64 |
|
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: 231.38 E-value: 5.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGnGLGFPIMT-ILFGDVIdvfgqnqnSSDVSDKIAKVALKFVYLGLGTLV------AALLQVSGWMiS 149
Cdd:TIGR03797 139 LAILAMGLLGTLL-GMLVPIATgILIGTAI--------PDADRSLLVQIALALLAAAVGAAAfqlaqsLAVLRLETRM-D 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 150 GERQAGRIRSLylqtiLRQDIAFFDVETnTGEVVGRMSGDTvliqdAMGEKVGKAIqlVSTFIGGFVIAFTEG------W 223
Cdd:TIGR03797 209 ASLQAAVWDRL-----LRLPVSFFRQYS-TGDLASRAMGIS-----QIRRILSGST--LTTLLSGIFALLNLGlmfyysW 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 224 LLTLVMVssipllVMsgAALAIVISKMASRGQTSYAKAAVVVEQTVGSIrTVASFTG---------EKQAISNYNKhLVS 294
Cdd:TIGR03797 276 KLALVAV------AL--ALVAIAVTLVLGLLQVRKERRLLELSGKISGL-TVQLINGisklrvagaENRAFARWAK-LFS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 295 AYRAGVFEGASTGLGLGTLNIV--IFCTYALaVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQaspcLSAFAAGQAA 372
Cdd:TIGR03797 346 RQRKLELSAQRIENLLTVFNAVlpVLTSAAL-FAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQ----LSNTLISILA 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 373 AYKMFEAIK----RKPEIDASDTTGKVLddiRGDIELNNVNFSYpaRPE-EQIFRGFSLSISSGSTVALVGQSGSGKSTV 447
Cdd:TIGR03797 421 VIPLWERAKpileALPEVDEAKTDPGKL---SGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 448 VSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAyGKENATVEEIRKATELANASKFIDKL 527
Cdd:TIGR03797 496 LRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAEDIRAM 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 528 PQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRttVVVAHRLSTVRNAD 607
Cdd:TIGR03797 575 PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNAD 652
|
570 580 590
....*....|....*....|....*....|....
gi 1063718281 608 MIAVIHQGKIVEKGSHSELLRDpEGAYSQLIRLQ 641
Cdd:TIGR03797 653 RIYVLDAGRVVQQGTYDELMAR-EGLFAQLARRQ 685
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
708-1289 |
5.86e-63 |
|
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: 228.69 E-value: 5.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 708 PIKEKKVSFFRVAAL----NKPEIPMLILGSIAAVLNGVILPIF-GILISSVIkaffkpPEQLKSdtrfwaiIFMLLGVA 782
Cdd:TIGR03797 115 PLPDKALGLRDLLRFalrgARRDLLAILAMGLLGTLLGMLVPIAtGILIGTAI------PDADRS-------LLVQIALA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 783 SMVVFPAQTIFfsiagcKLVQRIRSMCFEKVV-------------RMEVGWFdeTENSSGAIGARLSAdAATVRGLVGDA 849
Cdd:TIGR03797 182 LLAAAVGAAAF------QLAQSLAVLRLETRMdaslqaavwdrllRLPVSFF--RQYSTGDLASRAMG-ISQIRRILSGS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 850 laqTVQNLASVTAG---LVIAFVASWQLAFIVLAM-LPLIGLNGYIYMkFMVGFSadaKRMYEEASQVANDAVGSIRTVA 925
Cdd:TIGR03797 253 ---TLTTLLSGIFAllnLGLMFYYSWKLALVAVALaLVAIAVTLVLGL-LQVRKE---RRLLELSGKISGLTVQLINGIS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 926 SF---CAEEKV----MKMYKKKCEGPMRTGIRQGIVSGigFGVSFFVLFSS---YAASFYAGARLVDDGK-TTFDSVFRV 994
Cdd:TIGR03797 326 KLrvaGAENRAfarwAKLFSRQRKLELSAQRIENLLTV--FNAVLPVLTSAalfAAAISLLGGAGLSLGSfLAFNTAFGS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 995 FfalTMAAVAISQSSSLSPDSSKASNAAASIFAVI--DRESKIDPSDESGRvldnvkgdIELRHISFKYpsRPD-VQIFQ 1071
Cdd:TIGR03797 404 F---SGAVTQLSNTLISILAVIPLWERAKPILEALpeVDEAKTDPGKLSGA--------IEVDRVTFRY--RPDgPLILD 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1072 DLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAyg 1151
Cdd:TIGR03797 471 DVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-- 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1152 kgGDA--TETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERV 1229
Cdd:TIGR03797 549 --GGAplTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAI 626
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1230 VQDALDRVMVNRttVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASLVQ 1289
Cdd:TIGR03797 627 VSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REGLFAQLAR 683
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1050-1271 |
3.19e-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: 3.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDIELRHISFKYpsRPDVQ-IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQ 1128
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNETIRANIA-YGKggdATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIV 1207
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpFGE---YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
425-639 |
5.75e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 223.18 E-value: 5.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYdPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKE 504
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 505 NATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEAL 584
Cdd:PRK11174 449 DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 585 DRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPeGAYSQLIR 639
Cdd:PRK11174 529 NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLA 582
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
154-659 |
1.90e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 218.04 E-value: 1.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 154 AGRIRSLYLQTILRQDIAFFdVETNTGEVVGRMSGDTVLIQDAMGEKVgkaIQLVSTFIGG----FVIAFTEGWLLTLVm 229
Cdd:PRK10789 68 AVELREDFYRQLSRQHPEFY-LRHRTGDLMARATNDVDRVVFAAGEGV---LTLVDSLVMGcavlIVMSTQISWQLTLL- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 230 vSSIPLLVMsgaalAIVISKMASRGQTSY--AKAAVV-----VEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFE 302
Cdd:PRK10789 143 -ALLPMPVM-----AIMIKRYGDQLHERFklAQAAFSslndrTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 303 GASTGLGLGTLNIVIFCTYALAVWYGGKMilekgytggqvliiifaVLTGSMSLGQAS-----------PCLSAFAagqa 371
Cdd:PRK10789 217 ARIDARFDPTIYIAIGMANLLAIGGGSWM-----------------VVNGSLTLGQLTsfvmylglmiwPMLALAW---- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 372 aaykMFEAIKR--------------KPEIDASDttgKVLDDIRGDIELNNVNFSYPARpEEQIFRGFSLSISSGSTVALV 437
Cdd:PRK10789 276 ----MFNIVERgsaaysriramlaeAPVVKDGS---EPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGIC 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 438 GQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATEL 517
Cdd:PRK10789 348 GPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 518 ANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA 597
Cdd:PRK10789 428 ASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISA 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 598 HRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPeGAYSQLIRLQedtkQTEDSTDEQKLSME 659
Cdd:PRK10789 508 HRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ----QLEAALDDAPEIRE 564
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
80-361 |
1.33e-58 |
|
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: 204.82 E-value: 1.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 80 MILGTIGAVGNGLGFPIMTILFGDVIDVF------GQNQNSSDVSDKIA----------KVALKFVYLGLGTLVAALLQV 143
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtNITGNSSGLNSSAGpfekleeemtLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 144 SGWMISGERQAGRIRSLYLQTILRQDIAFFDVETnTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGW 223
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVND-TGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 224 LLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEG 303
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 304 ASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASP 361
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVP 297
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
397-641 |
1.59e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 213.04 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 397 DDIR----GDIELNNVNFSYpaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF 472
Cdd:PRK10790 331 NDDRplqsGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 473 QLKWIRSKIGLVSQEPVLFTSSIKENIAYGKeNATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAV 552
Cdd:PRK10790 409 SHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 553 ARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDpEG 632
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QG 566
|
....*....
gi 1063718281 633 AYSQLIRLQ 641
Cdd:PRK10790 567 RYWQMYQLQ 575
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
773-1292 |
2.28e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 212.66 E-value: 2.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 773 AIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQ 852
Cdd:PRK10790 68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDT--QPVGQLISRVTNDTEVIRDLYVTVVAT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 853 TVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYIYMKF-------MVGFSADAKRMYEEasqVAN--DAVGSIRT 923
Cdd:PRK10790 146 VLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYstpivrrVRAYLADINDGFNE---VINgmSVIQQFRQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 924 VASFCA-------EEKVMKMYKKKCEG----PMRTGIRQGIVSG------------IGFGVSffvlfssYAASFYAGaRL 980
Cdd:PRK10790 223 QARFGErmgeasrSHYMARMQTLRLDGfllrPLLSLFSALILCGllmlfgfsasgtIEVGVL-------YAFISYLG-RL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 981 VDD--GKTTFDSVfrvffaLTMAAVAisqssslspdsskasnaAASIFAVIDRESKIDPSDEsgRVLDNvkGDIELRHIS 1058
Cdd:PRK10790 295 NEPliELTTQQSM------LQQAVVA-----------------GERVFELMDGPRQQYGNDD--RPLQS--GRIDIDNVS 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1059 FKYpsRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPV 1138
Cdd:PRK10790 348 FAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPV 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 LFNETIRANIAYGKggDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEA 1218
Cdd:PRK10790 426 VLADTFLANVTLGR--DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1219 TSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASLVQLHL 1292
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA-AQGRYWQMYQLQL 576
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
150-638 |
4.63e-58 |
|
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: 214.22 E-value: 4.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 150 GERQAGRIRSLYLQTILRQDIAFFDVEtNTGEVVGRMSgDTVLIQDAMGEKVgkaiqlVSTF-------IGGFVIAFTEG 222
Cdd:TIGR01193 224 GQRLSIDIILSYIKHLFELPMSFFSTR-RTGEIVSRFT-DASSIIDALASTI------LSLFldmwilvIVGLFLVRQNM 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 223 WLLTLVMVSsIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQA-------ISNY-NKHLVS 294
Cdd:TIGR01193 296 LLFLLSLLS-IPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERyskidseFGDYlNKSFKY 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 295 AYRAGVFEGASTGLGLgTLNIVIfctyalaVWYGGKMILEKGYTGGQV-----LIIIFAV-LTGSMSLGQASPCLSAFAA 368
Cdd:TIGR01193 375 QKADQGQQAIKAVTKL-ILNVVI-------LWTGAYLVMRGKLTLGQLitfnaLLSYFLTpLENIINLQPKLQAARVANN 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 369 GQAAAYKMFEAIKRKPEIDASDTtgkvlddIRGDIELNNVNFSYPARPEeqIFRGFSLSISSGSTVALVGQSGSGKSTVV 448
Cdd:TIGR01193 447 RLNEVYLVDSEFINKKKRTELNN-------LNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGKSTLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 449 SLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYG-KENATVEEIRKATELANASKFIDKL 527
Cdd:TIGR01193 518 KLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENM 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 528 PQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE-RIVQEALDriMVNRTTVVVAHRLSTVRNA 606
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEkKIVNNLLN--LQDKTIIFVAHRLSVAKQS 675
|
490 500 510
....*....|....*....|....*....|..
gi 1063718281 607 DMIAVIHQGKIVEKGSHSELLrDPEGAYSQLI 638
Cdd:TIGR01193 676 DKIIVLDHGKIIEQGSHDELL-DRNGFYASLI 706
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1028-1289 |
1.34e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 206.98 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1028 VIDRESKIDPSDESGRVLDnvKGDIELRHISFKYPSRPDvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPD 1107
Cdd:PRK11160 317 ITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1108 SGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRAN--IAYGKGGDATETEIVSAAELSNAhgfisgLQ--QGYDT 1183
Cdd:PRK11160 394 QGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNllLAAPNASDEALIEVLQQVGLEKL------LEddKGLNA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1184 MVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVK 1263
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMD 547
|
250 260
....*....|....*....|....*.
gi 1063718281 1264 NGVIVEKGKHETLINiKDGVYASLVQ 1289
Cdd:PRK11160 548 NGQIIEQGTHQELLA-QQGRYYQLKQ 572
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1051-1278 |
2.54e-56 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 206.10 E-value: 2.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1051 DIELRHisFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQT 1130
Cdd:PRK10789 315 DVNIRQ--FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLFNETIRANIAYGKGgDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDP 1210
Cdd:PRK10789 392 AVVSQTPFLFSDTVANNIALGRP-DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1211 KVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
730-1005 |
3.64e-55 |
|
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: 194.80 E-value: 3.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIKAFFK------------------PPEQLKSDTRFWAIIFMLLGVASMVVFPAQT 791
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNggmtnitgnssglnssagPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 792 IFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVAS 871
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 872 WQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQ 951
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 952 GIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTTFDSVFRVFFALTMAAVAI 1005
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSA 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1073-1287 |
7.44e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.00 E-value: 7.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1073 LCLSIRAGKTIALVGESGSGKSTVIALLQRFYdPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGK 1152
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1153 GgDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQD 1232
Cdd:PRK11174 448 P-DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1233 ALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASL 1287
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQ-AGGLFATL 580
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
80-354 |
1.77e-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: 188.62 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 80 MILGTIGAVGNGLGFPIMTILFGDVIDVFgqNQNSSDVSDKIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAGRIRS 159
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL--LPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 160 LYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMS 239
Cdd:pfam00664 79 KLFKKILRQPMSFFD-TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 240 GAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNIVIFC 319
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063718281 320 TYALAVWYGGKMILEKGYTGGQVLIII--FAVLTGSM 354
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVAFLslFAQLFGPL 274
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
403-631 |
3.83e-53 |
|
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: 186.00 E-value: 3.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPV--LFTSSIKENIAYGKEN-----ATVEE-IRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVAR 554
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENlglprEEIRErVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
129-600 |
5.72e-53 |
|
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: 195.27 E-value: 5.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 129 VYLGLGTLVAA--LLQVSGWMIS----------------GERQAGRIRSL--YLQTILRQDIAF---------------- 172
Cdd:TIGR02868 19 VLLGALALGSAvaLLGVSAWLISraaemppvlylsvaavAVRAFGIGRAVfrYLERLVGHDAALrslgalrvrvyerlar 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 173 ----FDVETNTGEVVGRMSGDTvliqDAMGEKVGKAIQ--LVSTFIGGFVIAFTeGWLLT---LVMVSSIPLLVMSGAAL 243
Cdd:TIGR02868 99 qalaGRRRLRRGDLLGRLGADV----DALQDLYVRVIVpaGVALVVGAAAVAAI-AVLSVpaaLILAAGLLLAGFVAPLV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 244 AIVISKMA----SRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAgvfegASTGLGLGTLNIVIFC 319
Cdd:TIGR02868 174 SLRAARAAeqalARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERR-----AAAATALGAALTLLAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 320 --TYALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASPCLSAFAAGQAAAYKMFEAIKRKPEI-DASDTTGKVL 396
Cdd:TIGR02868 249 glAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVaEGSAPAAGAV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 397 DDIRGDIELNNVNFSYPARPEeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKW 476
Cdd:TIGR02868 329 GLGKPTLELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 IRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAI 556
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARAL 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1063718281 557 LKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRL 600
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
403-1289 |
1.90e-52 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 202.66 E-value: 1.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIdginlkefqlkwIRSKIG 482
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIAYGkenATVEEIR--KATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 560
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFG---SPFDPERyeRAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 561 RILLLDEATSALDAESERIV-QEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDpeGAYSQliR 639
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN--GPLFQ--K 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 640 LQEDTKQTEDSTDEQKLSMESMKRSSLRKSSLSRslskrsssfsmfGFPAGIDTNNEAIPEKDIKVSTPIKEKKVSFFRV 719
Cdd:PLN03130 836 LMENAGKMEEYVEENGEEEDDQTSSKPVANGNAN------------NLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKV 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 720 AALNKPEipmliLGSIAAVLngvILPIFGILI------SSVIKAFFKPPEQLKS-DTRFWAIIFMLLGVASMVVFPAQTI 792
Cdd:PLN03130 904 LERYKNA-----LGGAWVVM---ILFLCYVLTevfrvsSSTWLSEWTDQGTPKThGPLFYNLIYALLSFGQVLVTLLNSY 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 793 FFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAA----TVRGLVGDALAQTVQNLASVtagLVIAF 868
Cdd:PLN03130 976 WLIMSSLYAAKRLHDAMLGSILRAPMSFFHT--NPLGRIINRFAKDLGdidrNVAVFVNMFLGQIFQLLSTF---VLIGI 1050
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 869 VASWQLafivLAMLPLIGL--NGYIYMKfmvGFSADAKRM--------YEEASQVANdAVGSIRtvaSFCAEEKVMKMYK 938
Cdd:PLN03130 1051 VSTISL----WAIMPLLVLfyGAYLYYQ---STAREVKRLdsitrspvYAQFGEALN-GLSTIR---AYKAYDRMAEING 1119
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 939 KKCEGPMR-----------TGIRQGIVSG--IGFGVSFFVLFSSYAASFYAgarlvddgkttfdsvfrvfFALTMA---A 1002
Cdd:PLN03130 1120 RSMDNNIRftlvnmssnrwLAIRLETLGGlmIWLTASFAVMQNGRAENQAA-------------------FASTMGlllS 1180
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1003 VAISQSSSLSPDSSKASNAAASIFAVIDRESKIDPSDESGRVLDNVK--------GDIELRHISFKYpsRPDVQ-IFQDL 1073
Cdd:PLN03130 1181 YALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRpppgwpssGSIKFEDVVLRY--RPELPpVLHGL 1258
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1074 CLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANI-AYGK 1152
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdPFNE 1338
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1153 GGDATETEIVSAAELSNAhgfISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQD 1232
Cdd:PLN03130 1339 HNDADLWESLERAHLKDV---IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQK 1415
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1233 ALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIKDGVYASLVQ 1289
Cdd:PLN03130 1416 TIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
226-1289 |
3.62e-52 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 201.74 E-value: 3.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 226 TLVMVSSIPLLvmsgaalAIVISKM---ASRGQTSYAKAAVVVEQTVGSIRTVASFTGEK------QAISNYNkhlVSAY 296
Cdd:PLN03232 447 SLILFLLIPLQ-------TLIVRKMrklTKEGLQWTDKRVGIINEILASMDTVKCYAWEKsfesriQGIRNEE---LSWF 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 297 RAGVFEGASTGLGLGTLNIVI-FCTYALAVWYGGKMILEKGYTGgqvlIIIFAVLTGSMSLgqASPCLSAFAAGQAAAYK 375
Cdd:PLN03232 517 RKAQLLSAFNSFILNSIPVVVtLVSFGVFVLLGGDLTPARAFTS----LSLFAVLRSPLNM--LPNLLSQVVNANVSLQR 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 376 MFEAIKRKPEIDASDTTgkvLDDIRGDIELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIerfy 455
Cdd:PLN03232 591 IEELLLSEERILAQNPP---LQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM---- 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 456 dpqSGEvridgINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATvEEIRKATELANASKFIDKLPQGLDTMV 535
Cdd:PLN03232 664 ---LGE-----LSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFES-ERYWRAIDVTALQHDLDLLPGRDLTEI 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 536 GEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE-SERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQ 614
Cdd:PLN03232 735 GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSE 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 615 GKIVEKGSHSELLRDPEgaysQLIRLQEDTKQTeDSTDEQKLSMESMkrsslrksslsrslskrsssfSMFGFPAGIDTN 694
Cdd:PLN03232 815 GMIKEEGTFAELSKSGS----LFKKLMENAGKM-DATQEVNTNDENI---------------------LKLGPTVTIDVS 868
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 695 NEAIPE-------KDIKVSTPIKEKKVSFFRVAALNKPEIPMLILGSIAAVLNgVILPIFGILiSSVIKAFFKPPEQLKS 767
Cdd:PLN03232 869 ERNLGStkqgkrgRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCY-LTTEVLRVS-SSTWLSIWTDQSTPKS 946
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 768 -DTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADaatvrglV 846
Cdd:PLN03232 947 ySPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKD-------I 1017
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 847 GDaLAQTVQNLASVTAGLVIAFVASWQLAFIV-----LAMLPLIGL--NGYIYMKfmvGFSADAKRM--------YEEAS 911
Cdd:PLN03232 1018 GD-IDRNVANLMNMFMNQLWQLLSTFALIGTVstislWAIMPLLILfyAAYLYYQ---STSREVRRLdsvtrspiYAQFG 1093
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 912 QVANdAVGSIRtvaSFCAEEKVMKMYKKKCEGPMRTGI------RQGIVSGIGFGVSFFVLFSSYAASFYAGArlvdDGK 985
Cdd:PLN03232 1094 EALN-GLSSIR---AYKAYDRMAKINGKSMDNNIRFTLantssnRWLTIRLETLGGVMIWLTATFAVLRNGNA----ENQ 1165
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 986 TTFDSVFRVFFALTMAAVAISQSSSLSPDSSKASNAAAS-IFAVIDRESKIDPSDESGRVLDN--VKGDIELRHISFKY- 1061
Cdd:PLN03232 1166 AGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVErVGNYIDLPSEATAIIENNRPVSGwpSRGSIKFEDVHLRYr 1245
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1062 PSRPDVqiFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFN 1141
Cdd:PLN03232 1246 PGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1142 ETIRANI-AYGKGGDATETEIVSAAELSNAhgfISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1220
Cdd:PLN03232 1324 GTVRFNIdPFSEHNDADLWEALERAHIKDV---IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1221 ALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIKDGVYASLVQ 1289
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
718-1250 |
4.23e-52 |
|
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: 192.58 E-value: 4.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 718 RVAALNKPEIPMLILGSIAAVLNGV----ILPIFGILISsviKAFFKPPeqlksdtrfwaiiFMLLGVAsmvvfPAQTIF 793
Cdd:TIGR02868 3 RILPLLKPRRRRLALAVLLGALALGsavaLLGVSAWLIS---RAAEMPP-------------VLYLSVA-----AVAVRA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 794 FSI---------------AGCKLVQRIRSMCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVqnLA 858
Cdd:TIGR02868 62 FGIgravfrylerlvghdAALRSLGALRVRVYERLARQALAGRRRL--RRGDLLGRLGADVDALQDLYVRVIVPAG--VA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 859 SVTAGLVIAFVA--SWQLAFIVLAMLPLIGLngyiymkFMVGFSADAKRMYEEA--------SQVANDAVGSIRTVASFC 928
Cdd:TIGR02868 138 LVVGAAAVAAIAvlSVPAALILAAGLLLAGF-------VAPLVSLRAARAAEQAlarlrgelAAQLTDALDGAAELVASG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 929 AEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGK-----------TTFdSVFRVFFA 997
Cdd:TIGR02868 211 ALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRlapvtlavlvlLPL-AAFEAFAA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 998 LTMAAVAISQSSSLSPDsskasnaaasIFAVIDRESKI-DPSDESGRVLDNVKGDIELRHISFKYPSRPDVqiFQDLCLS 1076
Cdd:TIGR02868 290 LPAAAQQLTRVRAAAER----------IVEVLDAAGPVaEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPV--LDGVSLD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1077 IRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGgDA 1156
Cdd:TIGR02868 358 LPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARP-DA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1157 TETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDR 1236
Cdd:TIGR02868 437 TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA 516
|
570
....*....|....
gi 1063718281 1237 VMVNRTTVVVAHRL 1250
Cdd:TIGR02868 517 ALSGRTVVLITHHL 530
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
730-1003 |
8.91e-52 |
|
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: 183.61 E-value: 8.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNG 889
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 890 YIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSS 969
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063718281 970 YAASFYAGARLVDDGKTTFDS--VFRVFFALTMAAV 1003
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
400-628 |
2.61e-51 |
|
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: 191.11 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 400 RGDIELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKefqlKWIRS 479
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 K----IGLVSQEPVLFTSSIKENIAyGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARA 555
Cdd:COG4618 403 ElgrhIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRI-MVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLR 628
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1037-1291 |
6.00e-50 |
|
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: 186.88 E-value: 6.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1037 PSDESGRVLDNVKGDIELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGV 1116
Cdd:COG4618 316 PAEPERMPLPRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1117 EIKTlqlkWLRQQ----TGLVSQEPVLFNETIRANIAygKGGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQL 1192
Cdd:COG4618 395 DLSQ----WDREElgrhIGYLPQDVELFDGTIAENIA--RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1193 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
250 260
....*....|....*....|
gi 1063718281 1272 KhetliniKDGVYASLVQLH 1291
Cdd:COG4618 549 P-------RDEVLARLARPA 561
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1045-1288 |
9.56e-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: 189.18 E-value: 9.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1045 LDNVKGDIELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLK 1124
Cdd:TIGR01193 467 LNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQTGLVSQEPVLFNETIRANIAYGKGGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIAR 1204
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESERVVQDALDRvMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVY 1284
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD-RNGFY 702
|
....
gi 1063718281 1285 ASLV 1288
Cdd:TIGR01193 703 ASLI 706
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
400-627 |
7.61e-49 |
|
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: 183.32 E-value: 7.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 400 RGDIELNNVNFSyPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRS 479
Cdd:TIGR01842 314 EGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRIMVNR-TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELL 627
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
403-636 |
9.50e-48 |
|
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: 179.33 E-value: 9.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE--QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWI 477
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 478 RSKIGLVSQEPvlFTS-----SIKENIAYGKENATV---EEIR-KATELANA----SKFIDKLPQgldtmvgehgtQLSG 544
Cdd:COG1123 341 RRRVQMVFQDP--YSSlnprmTVGDIIAEPLRLHGLlsrAERReRVAELLERvglpPDLADRYPH-----------ELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 545 GQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 621
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
250
....*....|....*
gi 1063718281 622 SHSELLRDPEGAYSQ 636
Cdd:COG1123 488 PTEEVFANPQHPYTR 502
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
404-616 |
2.88e-47 |
|
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: 168.41 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGL 483
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 484 VSQEP--VLFTSSIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVARA 555
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLpeEEIEErveeALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGK 616
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1052-1248 |
8.56e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.92 E-value: 8.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIAYG---KGGDATETEIVSAAElsnahgfisglQQGYDTMVGERGV-QLSGGQKQRVAIARAIV 1207
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPfqlRERKFDRERALELLE-----------RLGLPPDILDKPVeRLSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAH 1248
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
403-626 |
9.48e-47 |
|
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: 167.36 E-value: 9.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYD-----PQSGEVRIDG--INLKEFQLK 475
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 476 WIRSKIGLVSQEPVLFTSSIKENIAYG------KENATVEEI-RKATELAnaskfidklpqGLDTMVGE--HGTQLSGGQ 546
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKA-----------ALWDEVKDrlHALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 547 KQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSE 625
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 1063718281 626 L 626
Cdd:cd03260 227 I 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
403-621 |
1.63e-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: 164.79 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQlKWIRSKIG 482
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIaygkenatveeirkatelanaskfidklpqgldtmvgehGTQLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 621
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
403-617 |
2.13e-46 |
|
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: 164.31 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIaygkenatveeirkatelanaskfidklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRI-MVNRTTVVVAHRLSTVRNADMIAVIHQGKI 617
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1052-1271 |
2.70e-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: 164.41 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQlKWLRQQTG 1131
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIaygkggdateteivsaaelsnahgfisglqqgydtmvgerGVQLSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
403-617 |
4.82e-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: 4.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIA----YGKENATVEEIRKATELANASKFIdklpqgLDTMVGEhgtqLSGGQKQRIAVARAILK 558
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDI------LDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 559 DPRILLLDEATSALDAESERIVQEALDRIM--VNRTTVVVAH--RLSTvRNADMIAVIHQGKI 617
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpEQIE-RVADRVLTLEAGRL 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
412-1289 |
6.01e-46 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 181.90 E-value: 6.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 412 YPARPEEqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVridginlkefqlkWIRSKIGLVSQEPVLF 491
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 492 TSSIKENIAYGKENATvEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSA 571
Cdd:PTZ00243 734 NATVRGNILFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 572 LDAE-SERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPegAYSQLI-RLQEDTKQTED 649
Cdd:PTZ00243 813 LDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATLAaELKENKDSKEG 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 650 STDEQKLSMESMKRSSLRKSSLSRSLSKRSSSfsmfGFPAGIDTNNEAIPEKDIKVSTPIKEKK-VSFFRVAAlnkpeip 728
Cdd:PTZ00243 891 DADAEVAEVDAAPGGAVDHEPPVAKQEGNAEG----GDGAALDAAAGRLMTREEKASGSVPWSTyVAYLRFCG------- 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 729 mlilGSIAAvlnGVILPIFG----ILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIA---GCKL 801
Cdd:PTZ00243 960 ----GLHAA---GFVLATFAvtelVTVSSGVWLSMWSTRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAmrrGSRN 1032
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 802 VQRIrsmCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASwqlAFIVLAM 881
Cdd:PTZ00243 1033 MHRD---LLRSVSRGTMSFFDTT--PLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQ---PFVLVAL 1104
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 882 LPLiglnGYIYMKFMVGFSAdAKRMYEEASQVANDAVGSI--------RTVASFCAEEKVMKMYKKKCEGPMRTGIRQGI 953
Cdd:PTZ00243 1105 VPC----GYLYYRLMQFYNS-ANREIRRIKSVAKSPVFTLleealqgsATITAYGKAHLVMQEALRRLDVVYSCSYLENV 1179
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 954 VSG-IGFGVSFF--VLFSSYAASFYAGARLVddgkTTFDSVFRVFFALTMAA------------VAISQSSSLSPDSSKA 1018
Cdd:PTZ00243 1180 ANRwLGVRVEFLsnIVVTVIALIGVIGTMLR----ATSQEIGLVSLSLTMAMqttatlnwlvrqVATVEADMNSVERLLY 1255
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1019 SNAAASIFAVIDRESKID--------PSDESGRVLdnvkgdIELRHISFKYPSrpDVQ----IFQDLCLSIRAG------ 1080
Cdd:PTZ00243 1256 YTDEVPHEDMPELDEEVDalerrtgmAADVTGTVV------IEPASPTSAAPH--PVQagslVFEGVQMRYREGlplvlr 1327
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1081 ---------KTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIayG 1151
Cdd:PTZ00243 1328 gvsfriaprEKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV--D 1405
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1152 KGGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVK-DPKVLLLDEATSALDAESERVV 1230
Cdd:PTZ00243 1406 PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQI 1485
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1231 QDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIKDGVYASLVQ 1289
Cdd:PTZ00243 1486 QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVE 1544
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
403-631 |
1.77e-45 |
|
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: 163.91 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWIR 478
Cdd:cd03258 2 IELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEPVLFTS-SIKENIAYGKENATV---EEIRKATELANaskFIdklpqGLDTMVGEHGTQLSGGQKQRIAVAR 554
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVpkaEIEERVLELLE---LV-----GLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 1063718281 630 PE 631
Cdd:cd03258 232 PQ 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
403-621 |
4.22e-45 |
|
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: 162.68 E-value: 4.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG---INLKEFQLKWIR 478
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEPvlFTS-----SIKENIA-----YGKENATVEEIRKATELA----NASKFIDKLPQgldtmvgehgtQLSG 544
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAeplriHGKLSKKEARKEAVLLLLvgvgLPEEVLNRYPH-----------ELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 545 GQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 621
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1052-1276 |
9.08e-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: 161.58 E-value: 9.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYD-----PDSGQITLDGVEIKTLQLK-- 1124
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQTGLVSQEPVLFNETIRANIAYG------KGGDATEtEIVSAAeLSNAhgfisglqqGYDTMVGER--GVQLSGGQ 1196
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELD-ERVEEA-LRKA---------ALWDEVKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHET 1275
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 1063718281 1276 L 1276
Cdd:cd03260 227 I 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
403-631 |
1.10e-44 |
|
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: 162.98 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKW-IRSKI 481
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEP--VLFTSSIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVA 553
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLGVprEEMRKrvdeALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 554 RAILKDPRILLLDEATSALDAESERIVQEALDRIM--VNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
403-636 |
1.43e-44 |
|
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: 161.89 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQ-IFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKI 481
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPvlFTS-----SIKENIA-------YGKENATVEEIRKATELANAskFIDKLPQgldtmvgehgtQLSGGQKQR 549
Cdd:COG1124 82 QMVFQDP--YASlhprhTVDRILAeplrihgLPDREERIAELLEQVGLPPS--FLDRYPH-----------QLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 550 IAVARAILKDPRILLLDEATSALDAeserIVQ----EALDRIMVNR--TTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS 622
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELT 222
|
250
....*....|....
gi 1063718281 623 HSELLRDPEGAYSQ 636
Cdd:COG1124 223 VADLLAGPKHPYTR 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
403-628 |
1.65e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.38 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfQLKWIRSKIG 482
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENI-----AYGKENATVEE-IRKATELANaskfidkLPQGLDTMVGehgtQLSGGQKQRIAVARA 555
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARErIDELLELFG-------LTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHSELLR 628
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1052-1277 |
2.57e-44 |
|
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: 160.58 E-value: 2.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPV--LFNETIRANIAYG---KGGDATETE--IVSAAELSNahgfISGLQqgydtmvgERGV-QLSGGQKQRVAIA 1203
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenLGLPREEIRerVEEALELVG----LEHLA--------DRPPhELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1204 RAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTI-KNADVIAVVKNGVIVEKGKHETLI 1277
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
401-622 |
4.17e-44 |
|
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: 159.11 E-value: 4.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYpaRPE-EQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRS 479
Cdd:cd03369 5 GEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFTSSIKENI-AYGKEnaTVEEIRKATElanaskfidklpqgldtmVGEHGTQLSGGQKQRIAVARAILK 558
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 559 DPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGS 622
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
403-631 |
5.51e-43 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 160.24 E-value: 5.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLI---ERfydPQSGEVRIDGIN---LKEFQLK 475
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDltaLSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 476 WIRSKIGLVSQEPVLFTS-SIKENIAYGKENATV--EEIR-KATELanaskfidklpqgLDtMVG--EHG----TQLSGG 545
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALPLEIAGVpkAEIRkRVAEL-------------LE-LVGlsDKAdaypSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 546 QKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEK 620
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
250
....*....|.
gi 1063718281 621 GSHSELLRDPE 631
Cdd:COG1135 223 GPVLDVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
403-619 |
1.02e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.97 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKST---VVSLIERfydPQSGEVRIDGIN---LKEFQL- 474
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDissLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 475 KWIRSKIGLVSQE----PVLftsSIKENIA----YGKENATvEEIRKATELANA---SKFIDKLPqgldtmvgehgTQLS 543
Cdd:COG1136 82 RLRRRHIGFVFQFfnllPEL---TALENVAlpllLAGVSRK-ERRERARELLERvglGDRLDHRP-----------SQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 544 GGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLSTVRNADMIAVIHQGKIVE 619
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
403-628 |
1.41e-42 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 155.74 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWIRS 479
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFTS-SIKENIAYG-KENATV--EEIRKATELanaskfidKLpqgldTMVGEHGT------QLSGGQKQR 549
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlREHTRLseEEIREIVLE--------KL-----EAVGLRGAedlypaELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 550 IAVARAILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSEL 626
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 1063718281 627 LR 628
Cdd:cd03261 225 RA 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1045-1277 |
1.54e-42 |
|
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: 164.44 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1045 LDNVKGDIELRHISFKYPSrPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLK 1124
Cdd:TIGR01842 310 LPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQTGLVSQEPVLFNETIRANIAYgKGGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIAR 1204
Cdd:TIGR01842 389 TFGKHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR-TTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLI 1277
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
403-630 |
2.32e-42 |
|
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: 155.54 E-value: 2.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIA-------YGKEnatvEEIRKATELAnasKFIDKLPQGLdtmVGEHGTQLSGGQKQRIAVAR 554
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIAlvpkllkWPKE----KIRERADELL---ALVGLDPAEF---ADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1052-1267 |
2.39e-42 |
|
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: 152.76 E-value: 2.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYP--SRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQ 1129
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLFNETIRANIaygkggdateteivsaaelsnahgfisglqqgydtmvgergvqLSGGQKQRVAIARAIVKD 1209
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1210 PKVLLLDEATSALDAESERVVQDALDRV-MVNRTTVVVAHRLSTIKNADVIAVVKNGVI 1267
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1050-1271 |
2.92e-42 |
|
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: 153.72 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDIELRHISFKYpsRPDV-QIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQ 1128
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNETIRANI-AYGKGGDAtetEIVSAAELSnahgfisglqqgydtmvgERGVQLSGGQKQRVAIARAIV 1207
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYSDE---EIYGALRVS------------------EGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1052-1278 |
3.16e-42 |
|
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: 162.77 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP--DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWL 1126
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 RQQTGLVSQEPVL-FNE--TIRANIA-----YGKGGDATETEIVsaAELSNAHgfisGLQQGYdtmVGERGVQLSGGQKQ 1198
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAeplrlHGLLSRAERRERV--AELLERV----GLPPDL---ADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1199 RVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHET 1275
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEE 491
|
...
gi 1063718281 1276 LIN 1278
Cdd:COG1123 492 VFA 494
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
403-631 |
3.81e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 154.77 E-value: 3.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL--KEFQLKWIRSK 480
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENIAYGKEnaTVEEIRKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLAPI--KVKKMSKAEAEERAMELLERV--GLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 560 PRILLLDEATSALDAEserIVQEALDrIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:COG1126 155 PKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1052-1269 |
3.91e-42 |
|
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: 154.96 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP-DVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRfydPDSGQITLDGVEIKTLQLKWLR 1127
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 QQTGLVSQEPVL-FN--ETIRANIA---YGKGGDATETEIVSAAELsnahgfiSGLQQGYdtmVGERGVQLSGGQKQRVA 1201
Cdd:COG1124 79 RRVQMVFQDPYAsLHprHTVDRILAeplRIHGLPDREERIAELLEQ-------VGLPPSF---LDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1202 IARAIVKDPKVLLLDEATSALDAeserVVQ----DALDRVMVNR--TTVVVAHRLSTIKN-ADVIAVVKNGVIVE 1269
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVE 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1052-1269 |
4.62e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 4.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPS-RPDVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRfydPDSGQITLDGVEIKTL---QLK 1124
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQT-GLVSQEPVLFNE-TIRANIAY-----GKGGDATETEIVSAAE---LSN-AHGFISglqqgydtmvgergvQLS 1193
Cdd:COG1136 82 RLRRRHiGFVFQFFNLLPElTALENVALplllaGVSRKERRERARELLErvgLGDrLDHRPS---------------QLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1194 GGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLSTIKNADVIAVVKNGVIVE 1269
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
403-628 |
5.76e-42 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 153.98 E-value: 5.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWIRS 479
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFTS-SIKENIAYG-KENATV--EEIRK-------ATELANAskfIDKLPqgldtmvgehgTQLSGGQKQ 548
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREHTDLseAEIRElvlekleLVGLPGA---ADKMP-----------SELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 549 RIAVARAILKDPRILLLDEATSALDAE-SERIV------QEALdrimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEK 620
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPItSAVIDelirelRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
....*...
gi 1063718281 621 GSHSELLR 628
Cdd:COG1127 224 GTPEELLA 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1053-1265 |
9.96e-42 |
|
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: 152.24 E-value: 9.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGL 1132
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1133 VSQEP--VLFNETIRANIAYG---KGGDatETEIVSAAELSNAHGFISGLQqgydtmvgERGV-QLSGGQKQRVAIARAI 1206
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGlenLGLP--EEEIEERVEEALELVGLEGLR--------DRSPfTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 1207 VKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTIKN-ADVIAVVKNG 1265
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1052-1271 |
2.18e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 155.62 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP-DVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRfydPDSGQITLDGVEIKTL---QLK 1124
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALserELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQTGLVSQEPVLFNE-TIRANIAY-----GKGGDATETEIvsaAELsnahgfisgLQqgydtMVG--ERG----VQL 1192
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALpleiaGVPKAEIRKRV---AEL---------LE-----LVGlsDKAdaypSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1193 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR----TTVVVAHRLSTIKN-ADVIAVVKNGVI 1267
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD--INRelglTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....
gi 1063718281 1268 VEKG 1271
Cdd:COG1135 220 VEQG 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
403-616 |
3.00e-41 |
|
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: 150.70 E-value: 3.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQ--IFRGFSLSISSGSTVALVGQSGSGKSTVVSLI--ErfYDPQSGEVRIDGinlkefqlkwir 478
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 sKIGLVSQEPVLFTSSIKENIAYGKE--NATVEEIRKATELanaSKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAI 556
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKACAL---EPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 557 LKDPRILLLDEATSALDAE-SERIVQEAL-DRIMVNRTTVVVAHRLSTVRNADMIAVIHQGK 616
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1052-1265 |
4.53e-41 |
|
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: 149.26 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL--QLKWLRQQ 1129
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLF-NETIRANIAYGkggdateteivsaaelsnahgfisglqqgydtmvgergvqLSGGQKQRVAIARAIVK 1208
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1209 DPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLS-TIKNADVIAVVKNG 1265
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1052-1278 |
6.45e-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: 150.81 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP-DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLR 1127
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 QQTGLVSQEPVLFN-ETIRANIAY-----GKGGDATETEIVSAAELSNahgfISGLQQGYDTmvgergvQLSGGQKQRVA 1201
Cdd:cd03258 82 RRIGMIFQHFNLLSsRTVFENVALpleiaGVPKAEIEERVLELLELVG----LEDKADAYPA-------QLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1202 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR----TTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETL 1276
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRD--INRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
..
gi 1063718281 1277 IN 1278
Cdd:cd03258 229 FA 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
421-570 |
7.92e-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: 147.41 E-value: 7.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLF-TSSIKENI 499
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 500 AYGkenATVEEIRKATELANASKFIDKLPQG--LDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATS 570
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1070-1220 |
8.00e-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: 147.41 E-value: 8.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1070 FQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNE-TIRANI 1148
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1149 AYGkggdATETEIVSAAELSNAHGFISGLQQGY--DTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1220
Cdd:pfam00005 81 RLG----LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1051-1271 |
1.36e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 153.72 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1051 DIELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL--QlkwlRQ 1128
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppE----KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLF-NETIRANIAYG---KGGDATE-TEIVSAA-ELSNahgfISGLqqgydtmvGERGV-QLSGGQKQRVA 1201
Cdd:COG3842 78 NVGMVFQDYALFpHLTVAENVAFGlrmRGVPKAEiRARVAELlELVG----LEGL--------ADRYPhQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1202 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAHRLS---TIknADVIAVVKNGVIVEKG 1271
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
403-616 |
2.11e-40 |
|
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: 147.33 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL--KEFQLKWIRSK 480
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENIAYGkenatveeirkatelanaskfidklpqgldtmvgehgtqLSGGQKQRIAVARAILKD 559
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGK 616
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
403-627 |
2.58e-40 |
|
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: 149.62 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfQLKWIRSKIG 482
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAY--------GKEN-ATVEEIRKATELanaSKFIDKLpqgldtmVGEhgtqLSGGQKQRIAV 552
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfaelyglfDEELkKRIEELIELLGL---EEFLDRR-------VGE----LSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 553 ARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGSHSELL 627
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1052-1271 |
2.76e-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: 148.44 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwlRQQTG 1131
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLF-NETIRANIAYG----KGGDATETEIVSAAELsnahgfisglqqgydtMVGERGV------QLSGGQKQRV 1200
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGlklrGVPKAEIRARVRELLE----------------LVGLEGLlnryphELSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTVVVAHRLS-TIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
403-617 |
3.24e-40 |
|
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: 148.41 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF----QLKWI 477
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 478 RSKIGLVSQEPVLFTS-SIKENIAYGkenATVEEIRKATELANASKFIDK--LPQGLDTMVGehgtQLSGGQKQRIAVAR 554
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLERvgLGDRLNHYPS----ELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLSTVRNADMIAVIHQGKI 617
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
403-619 |
3.38e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 148.39 E-value: 3.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfqlkwIRSKI 481
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFT-SSIKENIAYGKENATV------EEIRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVAR 554
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVpkaearERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRIMV-NRTTVV-VAHRLS-TVRNADMIAVIHQ--GKIVE 619
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1052-1271 |
3.40e-40 |
|
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: 148.81 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPD-VQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLR 1127
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 QQTGLVSQEPVL-FN--ETIRANIA-----YGKGGDATETEIVSAAELSnahgfisGLQQGyDTMVGERGVQLSGGQKQR 1199
Cdd:cd03257 82 KEIQMVFQDPMSsLNprMTIGEQIAeplriHGKLSKKEARKEAVLLLLV-------GVGLP-EEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1200 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALD--RVMVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
403-621 |
3.48e-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: 148.05 E-value: 3.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLkeFQLKWIRSKIG 482
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPqgldtmvgehgTQLSGGQKQRIAVARA 555
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRArvreLLELVGLEGLLNRYP-----------HELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKG 621
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
83-357 |
3.88e-40 |
|
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: 150.86 E-value: 3.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 83 GTIGAVGNGLGFPIMTILFGDVIDVFGQNQNSSDVSDKIA--KVALKFVYLGLGTLVAALLQVSGWMISGERQAGRIRSL 160
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRAlnQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 161 YLQTILRQDIAFFDVeTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSG 240
Cdd:cd18780 81 LFSAIIAQEIAFFDV-TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 241 AALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNIVIFCT 320
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063718281 321 YALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLG 357
Cdd:cd18780 240 IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFA 276
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
128-639 |
3.92e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 162.84 E-value: 3.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 128 FVY--LGLGTlVAALLQVSGWMISGERQAG-RIRSLYLQTILRQDIAFFdvETN-TGEVVGRMSGDTVLIQ----DAMGE 199
Cdd:PLN03232 954 VVYalLGFGQ-VAVTFTNSFWLISSSLHAAkRLHDAMLNSILRAPMLFF--HTNpTGRVINRFSKDIGDIDrnvaNLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 200 KVGKAIQLVSTFIggfVIafteGWLLTLVMVSSIPLLVMSGAA-LAIVISKMASRGQTSYAKAAVVVE-----QTVGSIR 273
Cdd:PLN03232 1031 FMNQLWQLLSTFA---LI----GTVSTISLWAIMPLLILFYAAyLYYQSTSREVRRLDSVTRSPIYAQfgealNGLSSIR 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 274 TVASFtgEKQAISNyNKHLVSAYRAGVFEGASTG---LGLGTLN-IVIFCTYALAVWYGGKMILEKGYTGGQVLIIIFAV 349
Cdd:PLN03232 1104 AYKAY--DRMAKIN-GKSMDNNIRFTLANTSSNRwltIRLETLGgVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTL 1180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 350 -LTGSMS--LGQASPCLSAFAAGQaaayKMFEAIKRKPEIDASDTTGKVLDD--IRGDIELNNVNFSYpaRPE-EQIFRG 423
Cdd:PLN03232 1181 nITTLLSgvLRQASKAENSLNSVE----RVGNYIDLPSEATAIIENNRPVSGwpSRGSIKFEDVHLRY--RPGlPPVLHG 1254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 424 FSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENI-AYG 502
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFS 1334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 503 KENATveEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQE 582
Cdd:PLN03232 1335 EHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQR 1412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 583 ALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQLIR 639
Cdd:PLN03232 1413 TIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
403-632 |
6.48e-40 |
|
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: 156.22 E-value: 6.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQ---SGEVRIDGINLKEFQLKWIRS 479
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEP--VLFTSSIKENIAYGKENATV--EEIR-KATELANASkfidklpqGLDTMVGEHGTQLSGGQKQRIAVAR 554
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLsrAEARaRVLELLEAV--------GLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 1063718281 632 G 632
Cdd:COG1123 236 A 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
403-631 |
1.31e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 148.60 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEP--VLFTSSIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVAR 554
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKKVppKKMKDiiddLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA--HRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1052-1278 |
2.41e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.36 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWlRQQTG 1131
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANI-----AYGKGGDATETEIVSAAELSnahgfisGLQQGYDTMVGergvQLSGGQKQRVAIARA 1205
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELF-------GLTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTI-KNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1052-1281 |
3.57e-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: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLRQ 1128
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNE-TIRANIAYG--KGGDATETEIVSAAELSnahgfisgLQqgydtMVGERGV------QLSGGQKQR 1199
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlrEHTDLSEAEIRELVLEK--------LE-----LVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1200 VAIARAIVKDPKVLLLDEATSALDAESERVV-------QDALdrvmvNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
250
....*....|
gi 1063718281 1272 KHETLINIKD 1281
Cdd:COG1127 225 TPEELLASDD 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
403-627 |
1.08e-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: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVL-FTSSIKENIAYG---------KENATVEEI-RKATELANASKFIDKLpqgldtmVgehgTQLSGGQKQRIA 551
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgRPSAEDREAvEEALERTGLEHLADRP-------V----DELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 552 VARAILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELL 627
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1052-1278 |
1.09e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 144.75 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI--KTLQLKWLRQQ 1129
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLF-NETIRANIAYG----KGGDATETEIVSAAELsnahgfisglqqgydTMVG--ERG----VQLSGGQKQ 1198
Cdd:COG1126 79 VGMVFQQFNLFpHLTVLENVTLApikvKKMSKAEAEERAMELL---------------ERVGlaDKAdaypAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1199 RVAIARAIVKDPKVLLLDEATSALDAEserVVQDALDrVMVN-----RTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGK 1272
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
....*.
gi 1063718281 1273 HETLIN 1278
Cdd:COG1126 220 PEEFFE 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
404-616 |
1.13e-38 |
|
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: 141.61 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGL 483
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 484 VSQepvlftssikeniaygkenatveeirkatelanaskfidklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRIL 563
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 564 LLDEATSALDAESERIVQEALDRIMV-NRTTVVVAHRLSTVRNA-DMIAVIHQGK 616
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1052-1265 |
1.25e-38 |
|
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: 143.38 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQ--IFQDLCLSIRAGKTIALVGESGSGKSTVI-ALLQRFyDPDSGQITLDGveiktlqlkwlrq 1128
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLsALLGEL-EKLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNETIRANIAYGKGGDATE-TEIVSAAELSNAhgfISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIV 1207
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEERyEKVIKACALEPD---LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1208 KDPKVLLLDEATSALDAES-----ERVVQDALdrvMVNRTTVVVAHRLSTIKNADVIAVVKNG 1265
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1052-1271 |
1.33e-38 |
|
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: 144.62 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTlQLKWLRQQTG 1131
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLF-NETIRANI-----AYGKGGDATETEIVSAAELSnahgfisGLQQGYDTMVGErgvqLSGGQKQRVAIARA 1205
Cdd:COG4555 78 VLPDERGLYdRLTVRENIryfaeLYGLFDEELKKRIEELIELL-------GLEEFLDRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQG 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
402-630 |
1.92e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 147.55 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 402 DIELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG---INLKEFQlkwiR 478
Cdd:COG3842 5 ALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvTGLPPEK----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 sKIGLVSQEPVLFTS-SIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPqgldtmvgehgTQLSGGQKQRIA 551
Cdd:COG3842 78 -NVGMVFQDYALFPHlTVAENVAFGLRMRGVpkAEIRArvaeLLELVGLEGLADRYP-----------HQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 552 VARAILKDPRILLLDEATSALDAESERIVQEALDRIM--VNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHSEL 626
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
....
gi 1063718281 627 LRDP 630
Cdd:COG3842 224 YERP 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1038-1291 |
2.17e-38 |
|
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: 144.67 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1038 SDESGRVLDNVKGDIELRHISFKYPS--RPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG 1115
Cdd:cd03288 6 SGSSNSGLVGLGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1116 VEIKTLQLKWLRQQTGLVSQEPVLFNETIRANI-AYGKGGDATETEIVSAAELSNahgFISGLQQGYDTMVGERGVQLSG 1194
Cdd:cd03288 83 IDISKLPLHTLRSRLSIILQDPILFSGSIRFNLdPECKCTDDRLWEALEIAQLKN---MVKSLPGGLDAVVTEGGENFSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHE 1274
Cdd:cd03288 160 GQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPE 239
|
250
....*....|....*..
gi 1063718281 1275 TLINIKDGVYASLVQLH 1291
Cdd:cd03288 240 NLLAQEDGVFASLVRTD 256
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1052-1284 |
2.64e-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: 144.03 E-value: 2.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVL-FNETIRANIAYG--------KGGDATETEIVSAA-ELSNAHGFIsglqqgydtmvgERGV-QLSGGQKQRV 1200
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfGRPSAEDREAVEEAlERTGLEHLA------------DRPVdELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALD----AESERVVQD-ALDRvmvNRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKGKHE 1274
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRlARER---GRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPE 223
|
250
....*....|...
gi 1063718281 1275 TLI---NIKDgVY 1284
Cdd:COG1120 224 EVLtpeLLEE-VY 235
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1052-1281 |
2.67e-38 |
|
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: 143.41 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLRQ 1128
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNE-TIRANIAY-----GKGGDATETEIVS----AAELSNAHgfisglqqgyDTMVGErgvqLSGGQKQ 1198
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFplrehTRLSEEEIREIVLekleAVGLRGAE----------DLYPAE----LSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1199 RVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGKHET 1275
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEE 223
|
....*.
gi 1063718281 1276 LINIKD 1281
Cdd:cd03261 224 LRASDD 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1052-1267 |
3.25e-38 |
|
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: 142.63 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPD-VQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRfydPDSGQITLDGVEIKTLQLKWL- 1126
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 ---RQQTGLVSQEPVLFNE-TIRANIAY-----GKGGDATETEIVSAAELSnahgfisGLQQGYDTMVGergvQLSGGQK 1197
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELLERV-------GLGDRLNHYPS----ELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1198 QRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLSTIKNADVIAVVKNGVI 1267
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
403-631 |
4.52e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 146.45 E-value: 4.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLI---ERfydPQSGEVRIDG----INL--KEfq 473
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGrdlfTNLppRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 474 lkwiRsKIGLVSQEPVLF-TSSIKENIAYG--KENATVEEIR-KATELA---NASKFIDKLPqgldtmvgehgTQLSGGQ 546
Cdd:COG1118 75 ----R-RVGFVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRaRVEELLelvQLEGLADRYP-----------SQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 547 KQRIAVARAILKDPRILLLDEATSALDA----ESERIVQEALDRImvNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKG 621
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|
gi 1063718281 622 SHSELLRDPE 631
Cdd:COG1118 217 TPDEVYDRPA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1052-1248 |
6.21e-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: 141.84 E-value: 6.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSR-PDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLqlkwlRQQT 1130
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLFN-ETIRANIAYG---KGGDATETEivsaaelSNAHGFISglqqgydtMVGERGV------QLSGGQKQRV 1200
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQGVPKAEAR-------ERAEELLE--------LVGLSGFenayphQLSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMV-NRTTVV-VAH 1248
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTH 190
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
403-625 |
1.13e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.34 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWIRS 479
Cdd:COG2884 2 IRFENVSKRYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQE-PVLFTSSIKENIAY-----GKENATVEE-IRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAV 552
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 553 ARAILKDPRILLLDEATSALDAE-SERIVqEALDRImvNR--TTVVVA-HRLSTVRNADM-IAVIHQGKIVEKGSHSE 625
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEI--NRrgTTVLIAtHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1052-1271 |
1.25e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.29 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRfydPDSGQITLDGVEIKTlQLKWLRQ 1128
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDLFT-NLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLF-NETIRANIAYG-KGGDATETEIVS-AAELSNAHGfISGLQQGYDTmvgergvQLSGGQKQRVAIARA 1205
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFGlRVRPPSKAEIRArVEELLELVQ-LEGLADRYPS-------QLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1206 IVKDPKVLLLDEATSALDA----ESERVVQDALDRvmVNRTTVVVAH------RLstiknADVIAVVKNGVIVEKG 1271
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
403-598 |
1.87e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.77 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfqlkwIRSKI 481
Cdd:COG1116 8 LELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLF---TssIKENIAYGKENATV------EEIRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAV 552
Cdd:COG1116 83 GVVFQEPALLpwlT--VLDNVALGLELRGVpkaerrERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063718281 553 ARAILKDPRILLLDEATSALDAESERIVQEALDRI-MVNRTTVV-VAH 598
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTH 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
403-617 |
2.18e-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: 138.68 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwIRSKIG 482
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFtssikeniaygkENATVEEIrkatelanaskfidklpqgLDtmvgehgtqLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03230 77 YLPEEPSLY------------ENLTVREN-------------------LK---------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKI 617
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
403-649 |
2.38e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 141.33 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYD--PQ---SGEVRIDGINL--KEFQLK 475
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 476 WIRSKIGLVSQEPVLFTSSIKENIAYG------KENATVEEI-----RKA---TELAnaskfiDKLpqgldtmvGEHGTQ 541
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIveeslRKAalwDEVK------DRL--------KKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 542 LSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEK 620
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEF 234
|
250 260
....*....|....*....|....*....
gi 1063718281 621 GSHSELLRDPEgaysqlirlqedTKQTED 649
Cdd:COG1117 235 GPTEQIFTNPK------------DKRTED 251
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
428-639 |
2.99e-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: 141.20 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 428 ISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKEnAT 507
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 508 VEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRI 587
Cdd:cd03288 123 DDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 588 MVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQLIR 639
Cdd:cd03288 203 FADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
128-639 |
3.08e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 153.36 E-value: 3.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 128 FVY--LGLGTLVAALLQvSGWMI-SGERQAGRIRSLYLQTILRQDIAFFdvETN-TGEVVGRMSGDTVLIQDAMGEKV-- 201
Cdd:PLN03130 957 LIYalLSFGQVLVTLLN-SYWLImSSLYAAKRLHDAMLGSILRAPMSFF--HTNpLGRIINRFAKDLGDIDRNVAVFVnm 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 202 --GKAIQLVSTFiggFVIAFTEgwllTLVMVSSIPLLVMSGAAL------AIVISKMASRGQTS-YAKAAVVVeQTVGSI 272
Cdd:PLN03130 1034 flGQIFQLLSTF---VLIGIVS----TISLWAIMPLLVLFYGAYlyyqstAREVKRLDSITRSPvYAQFGEAL-NGLSTI 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 273 RT------VASFTGeKQAISNYNKHLV--SAYRAgvfegasTGLGLGTLN-IVIFCTYALAVWYGGKMILEKGYTGGQVL 343
Cdd:PLN03130 1106 RAykaydrMAEING-RSMDNNIRFTLVnmSSNRW-------LAIRLETLGgLMIWLTASFAVMQNGRAENQAAFASTMGL 1177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 344 IIIFAV-LTGSMS--LGQASpclsafaagqaAAYKMFEAIKRKPE-IDASDTTGKVLDDIR--------GDIELNNVNFS 411
Cdd:PLN03130 1178 LLSYALnITSLLTavLRLAS-----------LAENSLNAVERVGTyIDLPSEAPLVIENNRpppgwpssGSIKFEDVVLR 1246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 412 YpaRPE-EQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVL 490
Cdd:PLN03130 1247 Y--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL 1324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 491 FTSSIKENIAYGKENATVeEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATS 570
Cdd:PLN03130 1325 FSGTVRFNLDPFNEHNDA-DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 571 ALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQLIR 639
Cdd:PLN03130 1404 AVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
100-364 |
3.43e-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: 141.93 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 100 LFGDVIDVFGQNQNSSDVSDkiakvaLKFVYLGLGTLVAALLQVSGWM--ISGERQAGRIRSLYLQTILRQDIAFFDvET 177
Cdd:cd18557 18 LIGRLIDTIIKGGDLDVLNE------LALILLAIYLLQSVFTFVRYYLfnIAGERIVARLRRDLFSSLLRQEIAFFD-KH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 178 NTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTS 257
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 258 YAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGY 337
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260
....*....|....*....|....*..
gi 1063718281 338 TGGQVLIIIFAVLTGSMSLGQASPCLS 364
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLA 277
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
403-661 |
3.62e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 141.69 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEP--VLFTSSIKENIAYGKEN------ATVEEIRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVAR 554
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigvpreEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAESErivQEALD--RIMVNRTTVVV---AHRLSTVRNADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1063718281 630 PEgaysQLIR----------LQEDTKQTEDSTDEQKLSMESM 661
Cdd:PRK13635 231 GH----MLQEigldvpfsvkLKELLKRNGILLPNTYLTMESL 268
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1052-1248 |
4.10e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.00 E-value: 4.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP-DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLqlkwlRQQT 1130
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLFN-ETIRANIAYG---KGGDATE-TEIVSAAelsnahgfisgLQqgydtMVGERGV------QLSGGQKQR 1199
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelRGVPKAErRERAREL-----------LE-----LVGLAGFedayphQLSGGMRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 1200 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTVV-VAH 1248
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTH 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
404-621 |
7.61e-37 |
|
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: 137.18 E-value: 7.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGL 483
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 484 VSQepvlftssikeniaygkenatveeirkATELANASKFIDKlpqgldtmvgeHGTQLSGGQKQRIAVARAILKDPRIL 563
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADR-----------PFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 564 LLDEATSALDAES-----ERIVQEALDRimvNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKG 621
Cdd:cd03214 120 LLDEPTSHLDIAHqiellELLRRLARER---GKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
403-630 |
7.81e-37 |
|
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: 142.11 E-value: 7.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQ---SGEVRIDGINLKEF---QLK 475
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 476 WIRSK-IGLVSQEPvlFTS-----SIKENIA--------YGKENAT--VEEIRKATELANASKFIDKLPqgldtmvgeHg 539
Cdd:COG0444 82 KIRGReIQMIFQDP--MTSlnpvmTVGDQIAeplrihggLSKAEARerAIELLERVGLPDPERRLDRYP---------H- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 540 tQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNR-TTVV-VAHRLSTVRN-ADMIAVIHQGK 616
Cdd:COG0444 150 -ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGR 228
|
250
....*....|....
gi 1063718281 617 IVEKGSHSELLRDP 630
Cdd:COG0444 229 IVEEGPVEELFENP 242
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
403-617 |
1.29e-36 |
|
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: 137.66 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--INLKEFQLKWIRSK 480
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENIAYGKenATVEEIRKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:cd03262 78 VGMVFQQFNLFPHlTVLENITLAP--IKVKGMSKAEAEERALELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 560 PRILLLDEATSALDAEserIVQEALDrIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKI 617
Cdd:cd03262 154 PKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
425-634 |
2.40e-36 |
|
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: 138.93 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG---INLKEFQLKWIRSK-IGLVSQEPVLFTS-SIKENI 499
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSRKELRELRRKkISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 500 AYGKENATV---EEIRKATE---LANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 573
Cdd:cd03294 124 AFGLEVQGVpraEREERAAEaleLVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 574 AESERIVQEALDRI--MVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELLRDPEGAY 634
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1053-1265 |
2.94e-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: 134.68 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGL 1132
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1133 VSQepvlfnetiraniaygkggdateteivsaaelsnahgfisglqqgydtmvgergvqLSGGQKQRVAIARAIVKDPKV 1212
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1213 LLLDEATSALDAESERVVQDALDRVMV-NRTTVVVAHRLSTIKNA-DVIAVVKNG 1265
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 ... |
731-987 |
3.38e-36 |
|
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: 139.23 E-value: 3.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 731 ILGSIAAVLNGVILP-IFGILISSVIKAffKPPEQLKSDTRFWAIIFMLLGVASMVvfpaQTIFFSIAGCKLVQRIRSMC 809
Cdd:cd18557 2 LLFLLISSAAQLLLPyLIGRLIDTIIKG--GDLDVLNELALILLAIYLLQSVFTFV----RYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNG 889
Cdd:cd18557 76 FSSLLRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 890 YIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSS 969
Cdd:cd18557 154 KIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLS 233
|
250
....*....|....*...
gi 1063718281 970 YAASFYAGARLVDDGKTT 987
Cdd:cd18557 234 LLLVLWYGGYLVLSGQLT 251
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
403-630 |
1.43e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.78 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWIR 478
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEPVLFTS-SIKENIAYgkenatveeirkATELANASK-FIDKLPQGLDTMVG--EHG----TQLSGGQKQRI 550
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVAL------------PLELAGTPKaEIKARVTELLELVGlsDKAdrypAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 551 AVARAILKDPRILLLDEATSALDAESERIVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSE 625
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSE 227
|
....*
gi 1063718281 626 LLRDP 630
Cdd:PRK11153 228 VFSHP 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1052-1268 |
1.43e-35 |
|
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: 135.77 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQ--- 1128
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNE-TIRANIAYGKGGDA----------TETEIVSAAELsnahgfisgLQQ-GYDTMVGERGVQLSGGQ 1196
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGRLGRRstwrslfglfPKEEKQRALAA---------LERvGLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLSTIK-NADVIAVVKNGVIV 1268
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
403-626 |
2.19e-35 |
|
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: 135.39 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPArpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGI---NLKEFQLKWIRS 479
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFT-SSIKENIAYGKENA-----------TVEEIRKATELanaskfIDKLpqGLDTMVGEHGTQLSGGQK 547
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRrstwrslfglfPKEEKQRALAA------LERV--GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 548 QRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLSTVR-NADMIAVIHQGKIVEKGSHS 624
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 1063718281 625 EL 626
Cdd:cd03256 231 EL 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1052-1267 |
2.26e-35 |
|
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: 132.91 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwLRQQTG 1131
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLfnetiraniaygkggdateteivsaaelsnahgfisglqqgYDTMVGERGVQLSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03230 77 YLPEEPSL-----------------------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTIKN-ADVIAVVKNGVI 1267
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1052-1268 |
2.39e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.18 E-value: 2.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLRQ 1128
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNE-TIRANIAYGKGGDA----------TETEIVSAAELsnahgfisgLQQgydtmVG------ERGVQ 1191
Cdd:COG3638 81 RIGMIFQQFNLVPRlSVLTNVLAGRLGRTstwrsllglfPPEDRERALEA---------LER-----VGladkayQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1192 LSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR----TTVVVAHRLSTIKN-ADVIAVVKNGV 1266
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRR--IARedgiTVVVNLHQVDLARRyADRIIGLRDGR 224
|
..
gi 1063718281 1267 IV 1268
Cdd:COG3638 225 VV 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
403-630 |
4.12e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.11 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYparpEEQIFRgFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKefQLKWIRSKIG 482
Cdd:COG3840 2 LRLDDLTYRY----GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAYG---------KENATVEEIRKATELANaskFIDKLPQgldtmvgehgtQLSGGQKQRIAV 552
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGlrpglkltaEQRAQVEQALERVGLAG---LLDRLPG-----------QLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 553 ARAILKDPRILLLDEATSALD----AESERIVQEALDRimVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELL 627
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
...
gi 1063718281 628 RDP 630
Cdd:COG3840 219 DGE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1052-1278 |
4.19e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 141.58 E-value: 4.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPD---SGQITLDGVEIKTLQLKWLRQ 1128
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEP--VLFNETIRANIAygkggDATETEIVSAAELSNAhgFISGLQQ-GYDTMVGERGVQLSGGQKQRVAIARA 1205
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIA-----EALENLGLSRAEARAR--VLELLEAvGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1053-1271 |
4.45e-35 |
|
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: 132.17 E-value: 4.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGL 1132
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1133 VSQepVLfnetiraniaygkggdatetEIVSAAELSNahgfisglqQGYDTmvgergvqLSGGQKQRVAIARAIVKDPKV 1212
Cdd:cd03214 78 VPQ--AL--------------------ELLGLAHLAD---------RPFNE--------LSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1213 LLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1052-1278 |
6.94e-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: 133.97 E-value: 6.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYP-SRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQT 1130
Cdd:cd03295 1 IEFENVTKRYGgGKKAVN---NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLF-NETIRANIA-------YGKggdatETEIVSAAELSNAHGF-ISGLQQGYDTmvgergvQLSGGQKQRVA 1201
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIAlvpkllkWPK-----EKIRERADELLALVGLdPAEFADRYPH-------ELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1202 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRL-STIKNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1052-1272 |
7.51e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.87 E-value: 7.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLRQ 1128
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQE-PVLFNETIRANIAY-----GKGGDATETEIVSAAELsnahgfiSGLQQGYDTMVgergVQLSGGQKQRVAI 1202
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDL-------VGLSDKAKALP----HELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1203 ARAIVKDPKVLLLDEATSALDAE-SERVVqDALDRvmVNR--TTVVVA-HRLSTIKNAD--VIaVVKNGVIVEKGK 1272
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEE--INRrgTTVLIAtHDLELVDRMPkrVL-ELEDGRLVRDEA 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
730-1000 |
1.36e-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: 134.60 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIkaffkpPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:cd07346 5 LLLLLLATALGLALPLLTKLLIDDVI------PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNG 889
Cdd:cd07346 79 FRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 890 YIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSS 969
Cdd:cd07346 157 RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALG 236
|
250 260 270
....*....|....*....|....*....|.
gi 1063718281 970 YAASFYAGARLVDDGKTTFDSVFRVFFALTM 1000
Cdd:cd07346 237 TALVLLYGGYLVLQGSLTIGELVAFLAYLGM 267
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
403-630 |
2.34e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfqlkwIRSKIG 482
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVL---FTSSIKENIA---YGKEN-------ATVEEIRKATELANASKFIDKLpqgldtmVGEhgtqLSGGQKQR 549
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLmgrYGRRGlfrrpsrADREAVDEALERVGLEDLADRP-------IGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 550 IAVARAILKDPRILLLDEATSALDAESERIVQEALDRI-MVNRTTVVVAHRLSTVR-NADMIAVIHQGKIVEkGSHSELL 627
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226
|
...
gi 1063718281 628 RDP 630
Cdd:COG1121 227 TPE 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1052-1276 |
2.94e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.14 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveiKTLQLKWLR---- 1127
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---KPPRRARRRigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 -QQTGLVSQEPVLFNETIRANIaYGKGG-----DATETEIVSAA-ELSNAHGFIsglqqgyDTMVGErgvqLSGGQKQRV 1200
Cdd:COG1121 81 pQRAEVDWDFPITVRDVVLMGR-YGRRGlfrrpSRADREAVDEAlERVGLEDLA-------DRPIGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDR-VMVNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGKHETL 1276
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLVAHGPPEEVL 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
422-630 |
5.11e-34 |
|
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: 130.92 E-value: 5.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfqLKWIRSKIGLVSQEPVLFTS-SIKENIA 500
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFPHmTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 501 YGKENATVEEIRKATELANASKFIdklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES-ERI 579
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 580 VQEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:cd03299 169 REELKKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1071-1278 |
7.72e-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: 131.61 E-value: 7.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQ----QTGLVSQEPVLF-NETIR 1145
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1146 ANIAYG---KGGDATETEIVSAAELSNAhgfisGLQQGYDTMVGErgvqLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1222
Cdd:cd03294 121 ENVAFGlevQGVPRAEREERAAEALELV-----GLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1223 DAESERVVQDALDRV--MVNRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:cd03294 192 DPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
403-629 |
8.25e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.78 E-value: 8.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYpaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEP--VLFTSSIKENIAYGKEN-----ATVEE-IRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVAR 554
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNmgldkDEVERrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
423-636 |
9.52e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 133.32 E-value: 9.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWIRSKIGLVSQEPvlFTS-----S 494
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDP--YASlnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 495 IKENIAYGKENATV----EEIRKATELanaskfidklpqgLDtMVG---EHGT----QLSGGQKQRIAVARAILKDPRIL 563
Cdd:COG4608 114 VGDIIAEPLRIHGLaskaERRERVAEL-------------LE-LVGlrpEHADryphEFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 564 LLDEATSALD----AEserIV------QEALdrimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEG 632
Cdd:COG4608 180 VCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARPLH 251
|
....
gi 1063718281 633 AYSQ 636
Cdd:COG4608 252 PYTQ 255
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-1250 |
3.33e-33 |
|
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: 140.05 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefqlkwirsK 480
Cdd:TIGR01271 425 GDDGLFFSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------R 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTSSIKENIAYGkenATVEEIRkATELANASKF---IDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAIL 557
Cdd:TIGR01271 489 ISFSPQTSWIMPGTIKDNIIFG---LSYDEYR-YTSVIKACQLeedIALFPEKDKTVLGEGGITLSGGQRARISLARAVY 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 558 KDPRILLLDEATSALDAESER-IVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSEL---------- 626
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqakrpdfssl 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 627 ----------------------LR-------DPEGAYSQLIR------------------------------------LQ 641
Cdd:TIGR01271 645 llgleafdnfsaerrnsiltetLRrvsidgdSTVFSGPETIKqsfkqpppefaekrkqsiilnpiasarkfsfvqmgpQK 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 642 EDTKQTEDSTDE---QKLSM----------------------------ESMKRSSLRKSSLSRSLSKRSSSFSMFgfpAG 690
Cdd:TIGR01271 725 AQATTIEDAVREpseRKFSLvpedeqgeeslprgnqyhhglqhqaqrrQSVLQLMTHSNRGENRREQLQTSFRKK---SS 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 691 IDTNNEAIPEKDI-----------KVSTPIKEKKV------------------SFFRVAALNKPEIPMLI------LGSI 735
Cdd:TIGR01271 802 ITQQNELASELDIysrrlskdsvyEISEEINEEDLkecfaderenvfetttwnTYLRYITTNRNLVFVLIfclvifLAEV 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 736 AAVLNGVIL----PIFGILISSVIKAFFKPPEQ---LKSDTRFWAIIFMLLGVASMVVfpAQTIFfsiAGCKLV------ 802
Cdd:TIGR01271 882 AASLLGLWLitdnPSAPNYVDQQHANASSPDVQkpvIITPTSAYYIFYIYVGTADSVL--ALGFF---RGLPLVhtlltv 956
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 803 -QRIRSMCFEKVVRMEVGWFDETEnsSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLviaFVASWQLAFIVLAM 881
Cdd:TIGR01271 957 sKRLHEQMLHSVLQAPMAVLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI---FVVSVLQPYIFIAA 1031
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 882 LPLIGLNGYIYMKFMVGfSADAKRMYEEA-SQVANDAVGSIR---TVASFCAEEKVMKMYKKKCEgpMRTGIRQGIVSGI 957
Cdd:TIGR01271 1032 IPVAVIFIMLRAYFLRT-SQQLKQLESEArSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALN--LHTANWFLYLSTL 1108
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 958 GFGVS----FFVLFSSyAASFYAGArlvddgkTTFDSVFRVFFALTMAAVAISQ---SSSLSPDSSKASNAAASIFAVID 1030
Cdd:TIGR01271 1109 RWFQMridiIFVFFFI-AVTFIAIG-------TNQDGEGEVGIILTLAMNILSTlqwAVNSSIDVDGLMRSVSRVFKFID 1180
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1031 RESkiDPSDESGRVLDNVKGD---IELRHISFKYPS--RPDVQ------------IFQDLCLSIRAGKTIALVGESGSGK 1093
Cdd:TIGR01271 1181 LPQ--EEPRPSGGGGKYQLSTvlvIENPHAQKCWPSggQMDVQgltakyteagraVLQDLSFSVEGGQRVGLLGRTGSGK 1258
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1094 STVIALLQRFYDPDsGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANI-AYGKGGDateTEIVSAAELSNAHG 1172
Cdd:TIGR01271 1259 STLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQWSD---EEIWKVAEEVGLKS 1334
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1173 FISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRL 1250
Cdd:TIGR01271 1335 VIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
401-630 |
7.16e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.35 E-value: 7.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwiRSK 480
Cdd:COG3839 2 ASLELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLF-TSSIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPqgldtmvgehgTQLSGGQKQRIAVA 553
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPLKLRKVpkAEIDRrvreAAELLGLEDLLDRKP-----------KQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 554 RAILKDPRILLLDEATSALDAE------SE--RIVQEaldrimVNRTTVVVAH------RLstvrnADMIAVIHQGKIVE 619
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKlrvemrAEikRLHRR------LGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQ 214
|
250
....*....|.
gi 1063718281 620 KGSHSELLRDP 630
Cdd:COG3839 215 VGTPEELYDRP 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1052-1271 |
1.49e-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: 126.58 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIktLQLKWLRQQTG 1131
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANIAYG---KGGDATE-----TEIVSAAELSN-AHGFISglqqgydtmvgergvQLSGGQKQRVA 1201
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlKKLPKAEikervAEALDLVQLEGyANRKPS---------------QLSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1202 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1052-1267 |
1.57e-32 |
|
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: 126.11 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI--KTLQLKWLRQQ 1129
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLF-NETIRANIAYG----KGGDATETEIVSAAEL------SNAHGFISglqqgydtmvgergvQLSGGQKQ 1198
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLApikvKGMSKAEAEERALELLekvglaDKADAYPA---------------QLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1199 RVAIARAIVKDPKVLLLDEATSALDAEserVVQDALDrVMVN-----RTTVVVAHRLSTIKN-ADVIAVVKNGVI 1267
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
735-985 |
2.50e-32 |
|
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: 128.04 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 735 IAAVLNgVILPIF-GILISSVIkaffkppeQLKSDTRFWAIIFML--LGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFE 811
Cdd:cd18572 7 VAALSE-LAIPHYtGAVIDAVV--------ADGSREAFYRAVLLLllLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 812 KVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYI 891
Cdd:cd18572 78 SLLRQDIAFFDAT--KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 892 YMKFMvgfSADAKRMYE---EASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFS 968
Cdd:cd18572 156 YGRYY---RKLSKEIQDalaEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNG 232
|
250
....*....|....*..
gi 1063718281 969 SYAASFYAGARLVDDGK 985
Cdd:cd18572 233 TQVLVLFYGGHLVLSGR 249
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1050-1271 |
3.01e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.42 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDIELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLqrfYDPDSGQITLDGVEIKTLQLKwl 1126
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGL---EDPTSGEILIGGRDVTDLPPK-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 RQQTGLVSQEPVLF-NETIRANIAYG---KGGDATETE--IVSAAELSNahgfISGLqqgYDTMVGergvQLSGGQKQRV 1200
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIAFPlklRKVPKAEIDrrVREAAELLG----LEDL---LDRKPK----QLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESeRV--------VQDALdrvmvNRTTVVVAHRLS---TIknADVIAVVKNGVIVE 1269
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQ 214
|
..
gi 1063718281 1270 KG 1271
Cdd:COG3839 215 VG 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1052-1261 |
3.12e-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: 124.90 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRfydPDSGQITLDGVEIKTLQLKWlRQ 1128
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllrILAGLLP---PSAGEVLWNGEPIRDAREDY-RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNE-TIRANIAY---GKGGDATETEIVSAAELSnahgfisGLQQGYDTMVGergvQLSGGQKQRVAIAR 1204
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFwaaLYGLRADREAIDEALEAV-------GLAGLADLPVR----QLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTIKNADVIAV 1261
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1052-1275 |
5.50e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.38 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYP-SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLR 1127
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 QQTGLVSQEpvlFN----ETIRANIAY-----GKGGDATET------EIVSAAELSNAhgfisglqqgYDTmvgergvQL 1192
Cdd:PRK11153 82 RQIGMIFQH---FNllssRTVFDNVALplelaGTPKAEIKArvtellELVGLSDKADR----------YPA-------QL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1193 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR----TTVVVAHRLSTIKN-ADVIAVVKNGVI 1267
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKD--INRelglTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
250
....*....|....*..
gi 1063718281 1268 VEKG---------KHET 1275
Cdd:PRK11153 220 VEQGtvsevfshpKHPL 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
403-631 |
5.99e-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: 125.04 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKefQLKWIRSKIG 482
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAYG------KENATVEEIRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVARA 555
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEEP 222
|
.
gi 1063718281 631 E 631
Cdd:cd03300 223 A 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
404-617 |
7.37e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.18 E-value: 7.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFqlkwiRSKIGL 483
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 484 VSQEPVL---FTSSIKENIA---YGK----ENATVEEIRKATE---LANASKFIDKlpqgldtmvgeHGTQLSGGQKQRI 550
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglYGHkglfRRLSKADKAKVDEaleRVGLSELADR-----------QIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 551 AVARAILKDPRILLLDEATSALDAESERIVQEALDRI-MVNRTTVVVAHRLSTV-RNADMIAVIHQGKI 617
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
403-626 |
1.73e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 125.23 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEP--VLFTSSIKENIAYGKENA------TVEEIRKATELANASKFIDKLPqgldtmvgehgTQLSGGQKQRIAVAR 554
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKgipheeMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 555 AILKDPRILLLDEATSALDAESE----RIVQEALDRimVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSEL 626
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
403-631 |
1.94e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.16 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSY-PARP-EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL--KEFQLKWIR 478
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEP--VLFTSSIKENIAYGKENATVEE------IRKATELANAS--KFIDKLPqgldtmvgehgTQLSGGQKQ 548
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEeeienrVKRAMNIVGLDyeDYKDKSP-----------FELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 549 RIAVARAILKDPRILLLDEATSALDAESErivQEALDRIM-----VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS 622
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
....*....
gi 1063718281 623 HSELLRDPE 631
Cdd:PRK13637 229 PREVFKEVE 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1052-1276 |
2.54e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.99 E-value: 2.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYD--PD---SGQITLDGVEI--KTLQLK 1124
Cdd:COG1117 12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQTGLVSQEPVLFNETIRANIAYG--KGGDATETEIVSAAELSnahgfisgLQQgydtmVG----------ERGVQL 1192
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrLHGIKSKSELDEIVEES--------LRK-----AAlwdevkdrlkKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1193 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAH------RLStiknaDVIAVVKNGV 1266
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGE 230
|
250
....*....|
gi 1063718281 1267 IVEKGKHETL 1276
Cdd:COG1117 231 LVEFGPTEQI 240
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
423-621 |
2.79e-31 |
|
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: 122.40 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSIS---SGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWI----RSKIGLVSQEPVLFTS-S 494
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqQRKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 495 IKENIAYGKENATVEEIRKATElanasKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDA 574
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD-----ELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063718281 575 ESERIVQEALDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKG 621
Cdd:cd03297 165 ALRLQLLPELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
733-987 |
3.19e-31 |
|
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: 125.05 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 733 GSIAAVLN---GVILPIF-GILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSM 808
Cdd:cd18780 1 GTIALLVSsgtNLALPYFfGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 809 CFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLN 888
Cdd:cd18780 81 LFSAIIAQEIAFFDVT--RTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 889 GYIYMKFMVGFSadaKRMYEE---ASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFV 965
Cdd:cd18780 159 AVIYGKYVRKLS---KKFQDAlaaASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAA 235
|
250 260
....*....|....*....|..
gi 1063718281 966 LFSSYAASFYAGARLVDDGKTT 987
Cdd:cd18780 236 AQLAIVLVLWYGGRLVIDGELT 257
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
403-642 |
3.61e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.89 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPArpeEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLK--EFQLKWIRSK 480
Cdd:PRK09493 2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENIAYGKENatVEEIRKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLR--VRGASKEEAEKQARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 560 PRILLLDEATSALDAEserIVQEALdRIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEga 633
Cdd:PRK09493 155 PKLMLFDEPTSALDPE---LRHEVL-KVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPP-- 228
|
....*....
gi 1063718281 634 ySQliRLQE 642
Cdd:PRK09493 229 -SQ--RLQE 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1052-1272 |
4.66e-31 |
|
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: 122.79 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQ---LKWLRQ 1128
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLF-NETIRANIAYGKGGdateteivsaaelsnAHGFISGL-----------------QQGYDTMVGERGV 1190
Cdd:TIGR02315 80 RIGMIFQHYNLIeRLTVLENVLHGRLG---------------YKPTWRSLlgrfseedkeralsaleRVGLADKAYQRAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1191 QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTVVVAHRLSTIKN-ADVIAVVKNGVI 1267
Cdd:TIGR02315 145 QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKyADRIVGLKAGEI 224
|
....*
gi 1063718281 1268 VEKGK 1272
Cdd:TIGR02315 225 VFDGA 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
403-634 |
1.05e-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: 121.68 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEeqiFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwiRSKIG 482
Cdd:cd03296 3 IEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAYGKEnatveeIRKATELANASKFIDKLPQ-----GLDTMVGEHGTQLSGGQKQRIAVARAI 556
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLR------VKPRSERPPEAEIRAKVHEllklvQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 557 LKDPRILLLDEATSALDA----ESERIVQEALDRIMVnrTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHV--TTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
...
gi 1063718281 632 GAY 634
Cdd:cd03296 230 SPF 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
403-648 |
1.22e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 122.79 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYP-ARPEeqiFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF-QLKWIRSK 480
Cdd:PRK13644 2 IRLENVSYSYPdGTPA---LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEP--VLFTSSIKENIAYGKENATVE--EIRKATELANASKfidklpqGLDTMVGEHGTQLSGGQKQRIAVARAI 556
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEI-------GLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 557 LKDPRILLLDEATSALDAESERIVQEALDRIMVN-RTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPEGAY- 634
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTl 231
|
250
....*....|....*...
gi 1063718281 635 ----SQLIRLQEDTKQTE 648
Cdd:PRK13644 232 gltpPSLIELAENLKMHG 249
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
403-597 |
1.59e-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: 120.21 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGI---NLKEFQLKWIRS 479
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQE-PVLFTSSIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAV 552
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVppREIRKrvpaALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063718281 553 ARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA 597
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
404-597 |
1.82e-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: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYPARPEeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLkwiRSKIGL 483
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 484 VSQEP--VLFTSSIKENIAYGKENAtveeirkATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 561
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKEL-------DAGNEQAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063718281 562 ILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA 597
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI 182
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
402-631 |
2.17e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.44 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 402 DIELNNVNFSYPAR-PEEQI-FRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL----KEFQLK 475
Cdd:PRK13634 2 DITFQKVEHRYQYKtPFERRaLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 476 WIRSKIGLVSQ--EPVLFTSSIKENIAYGKENATVEEirkATELANASKFIDKLpqGLDTMVGEHGT-QLSGGQKQRIAV 552
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE---EDAKQKAREMIELV--GLPEELLARSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 553 ARAILKDPRILLLDEATSALDAESERIVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
..
gi 1063718281 630 PE 631
Cdd:PRK13634 237 PD 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1052-1271 |
4.00e-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: 120.14 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwlRQQTG 1131
Cdd:cd03296 3 IEVRNVSKRFGDFVALD---DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANIAYG-----KGGDATETEIvsAAELSNAHGFI--SGLQQGYDTmvgergvQLSGGQKQRVAIA 1203
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlrvkpRSERPPEAEI--RAKVHELLKLVqlDWLADRYPA-------QLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 1204 RAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1052-1279 |
4.36e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.47 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqifqdLC--LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLqlkwlrqq 1129
Cdd:COG3840 2 LRLDDLTYRYGDFP-------LRfdLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 tgLVSQEPV--LFNE-------TIRANIAYG-----KGGDATETEIVSAAElsnahgfisglQQGYDTMVGERGVQLSGG 1195
Cdd:COG3840 67 --PPAERPVsmLFQEnnlfphlTVAQNIGLGlrpglKLTAEQRAQVEQALE-----------RVGLAGLLDRLPGQLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1196 QKQRVAIARAIVKDPKVLLLDEATSALD----AESERVVQDALDRvmVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEK 1270
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAAD 211
|
....*....
gi 1063718281 1271 GKHETLINI 1279
Cdd:COG3840 212 GPTAALLDG 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1072-1278 |
5.68e-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: 5.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1072 DLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwlRQQTGLVSQEPVLF-NETIRANIAY 1150
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1151 G---KGGDATETEivsaAELSNAHGFIsglqqGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE 1227
Cdd:cd03299 95 GlkkRKVDKKEIE----RKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1228 RVVQDALDRVM-VNRTTVV-VAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:cd03299 166 EKLREELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
746-984 |
6.36e-30 |
|
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: 121.08 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 746 IFGILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFpAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEte 825
Cdd:cd18573 18 AIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVGAAANF-GRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 826 NSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKR 905
Cdd:cd18573 95 NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 906 MYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDG 984
Cdd:cd18573 175 ALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASG 253
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1052-1272 |
7.07e-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: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLRQ 1128
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQE-PVLFNETIRANIAY-----GKGGDATETEIVSAAELSnahgfisGLQQGYDTMvgerGVQLSGGQKQRVAI 1202
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFalevtGVPPREIRKRVPAALELV-------GLSHKHRAL----PAELSGGEQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1203 ARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HrlstikNADVIAVVKNGVIV-EKGK 1272
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtH------AKELVDTTRHRVIAlERGK 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
403-621 |
9.36e-30 |
|
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: 118.13 E-value: 9.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwiRSKIG 482
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAYG------KENATVEEIRKATELANASKFIDKLPqgldtmvgehgTQLSGGQKQRIAVARA 555
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRIM--VNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKG 621
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
100-364 |
9.39e-30 |
|
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: 120.70 E-value: 9.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 100 LFGDVIDVFgqnqNSSDVSDKIAKVALKFVYLGLGTL-----VAALLQVSGWMISGERQAGRIRSLYLQTILRQDIAFFD 174
Cdd:cd18573 18 AIGKLIDVA----SKESGDIEIFGLSLKTFALALLGVfvvgaAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 175 VeTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRG 254
Cdd:cd18573 94 K-NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 255 QTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNIVIFCTYALAVWYGGKMILE 334
Cdd:cd18573 173 QDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVAS 252
|
250 260 270
....*....|....*....|....*....|.
gi 1063718281 335 KGYTGGQVL-IIIFAVLTGSmSLGQASPCLS 364
Cdd:cd18573 253 GELTVGDLTsFLMYAVYVGS-SVSGLSSFYS 282
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1052-1274 |
9.40e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 118.66 E-value: 9.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIA--YGKGGDATETEIvsaaelsnahgFISGLQQGY--DTMVGERGVQLSGGQKQRVAIARAIV 1207
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAI-----------FLDDLERFAlpDTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVV--VAHRLSTIKNAD-VIAVVKNGVIVEKGKHE 1274
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADkVITLQPHAGEMQEARYE 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
403-621 |
1.36e-29 |
|
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: 117.68 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTvALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfQLKWIRSKIG 482
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAY-----GKENATV-EEIRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVARA 555
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVkARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 556 ILKDPRILLLDEATSALDAEsERI-VQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 621
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPE-ERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
418-646 |
1.56e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 118.70 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 418 EQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVR-----IDG---INLKEFQLKWIRSKIGLVSQEPV 489
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTarsLSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 490 LFT-SSIKENIAYGKenATVEEIRKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:PRK11264 96 LFPhRTVLENIIEGP--VIVKGEPKEEATARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 569 TSALDAEserIVQEALDRIMV----NRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEgaysqlirlQED 643
Cdd:PRK11264 172 TSALDPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ---------QPR 239
|
...
gi 1063718281 644 TKQ 646
Cdd:PRK11264 240 TRQ 242
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1075-1276 |
2.02e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.61 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLRQQTGLVSQEP--VLfN--ETIRAN 1147
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPyaSL-NprMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1148 IA-----YGKGGDATETEIVsaAELsnahgfisgLQqgydtMVGERGV-------QLSGGQKQRVAIARAIVKDPKVLLL 1215
Cdd:COG4608 118 IAeplriHGLASKAERRERV--AEL---------LE-----LVGLRPEhadryphEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1216 DEATSALD----AEserVV------QDALdrvmvNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETL 1276
Cdd:COG4608 182 DEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1052-1272 |
2.15e-29 |
|
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: 118.69 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKW-LRQQT 1130
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEP--VLFNETIRANIAYG---KGGDATE--TEIVSAAELSNAHGFIsglqqgydtmvgERGVQ-LSGGQKQRVAI 1202
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGlenLGVPREEmrKRVDEALKLVGMEDFR------------DREPHlLSGGQKQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1203 ARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGK 1272
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
403-631 |
2.62e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.04 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEP--VLFTSSIKENIAYGKENATV---EEIRKATELANASKFIDklpqgldtMVGEHGTQLSGGQKQRIAVARAIL 557
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIpreEMIKRVDEALLAVNMLD--------FKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 558 KDPRILLLDEATSALD----AESERIVQEALDRIMVnrTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
425-630 |
3.09e-29 |
|
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: 120.60 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL----KEFQLKWIRSKIGLVSQEPVLFTS-SIKENI 499
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPHlSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 500 AYGKENATVEEIRkatelANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERI 579
Cdd:TIGR02142 97 RYGMKRARPSERR-----ISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 580 VQEALDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:TIGR02142 170 ILPYLERLHaeFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
403-631 |
3.82e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.36 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGE---VRIDGINLKEFQLKWIRS 479
Cdd:PRK13640 6 VEFKHVSFTYP-DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEP--VLFTSSIKENIAYGKENATVEE------IRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIA 551
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRpemikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 552 VARAILKDPRILLLDEATSALDAESERIVQEALDRIMV--NRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
..
gi 1063718281 630 PE 631
Cdd:PRK13640 234 VE 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1281 |
5.00e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.78 E-value: 5.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEP--VLFNETIRANIAYG---KGGDATE--TEIVSAAELSNAHGFISGLQQgydtmvgergvQLSGGQKQRVAIAR 1204
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGlenKKVPPKKmkDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESERVVQDALD--RVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIKD 1281
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1052-1278 |
5.24e-29 |
|
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: 119.00 E-value: 5.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP-DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDP---DSGQITLDGVEIKTL---QLK 1124
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLR-QQTGLVSQE------PVLfneTIRANIA------YGKGGDATETEIVSAAElsnahgfisglqqgydtMVG----E 1187
Cdd:COG0444 82 KIRgREIQMIFQDpmtslnPVM---TVGDQIAeplrihGGLSKAEARERAIELLE-----------------RVGlpdpE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1188 RGV-----QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAeserVVQ----DALDRVMVNR-TTVV-VAHRLSTIKN- 1255
Cdd:COG0444 142 RRLdryphELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaqilNLLKDLQRELgLAILfITHDLGVVAEi 217
|
250 260
....*....|....*....|...
gi 1063718281 1256 ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:COG0444 218 ADRVAVMYAGRIVEEGPVEELFE 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1052-1271 |
7.92e-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: 115.43 E-value: 7.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwlRQQTG 1131
Cdd:cd03301 1 VELENVTKRFGNVTALD---DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLF-NETIRANIAYG-KGGDATETEIV----SAAELSNahgfISGLQQGYDTmvgergvQLSGGQKQRVAIARA 1205
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlKLRKVPKDEIDervrEVAELLQ----IEHLLDRKPK-------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAH-RLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
403-646 |
1.02e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.19 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSY-PARP-EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL----KEFQLKW 476
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 IRSKIGLVSQ--EPVLFTSSIKENIAYGKEN--ATVEEIRkatelANASKFIDKLPQGLDTMvGEHGTQLSGGQKQRIAV 552
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVK-----NYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 553 ARAILKDPRILLLDEATSALDAESERIVQEALDRIMV--NRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
250 260
....*....|....*....|...
gi 1063718281 630 PEG------AYSQLIRLQEDTKQ 646
Cdd:PRK13646 237 KKKladwhiGLPEIVQLQYDFEQ 259
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
400-631 |
1.13e-28 |
|
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: 119.05 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 400 RGDIELNnVNFSYPARpeeqifrgfslsissGSTvALVGQSGSGKSTVVSLI---ERfydPQSGEVRIDG---------I 467
Cdd:COG4148 11 RGGFTLD-VDFTLPGR---------------GVT-ALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGevlqdsargI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 468 NLK-EfqlkwiRSKIGLVSQEPVLF-TSSIKENIAYGkenatveeIRKATELANASKF---IDKLpqGLDTMVGEHGTQL 542
Cdd:COG4148 71 FLPpH------RRRIGYVFQEARLFpHLSVRGNLLYG--------RKRAPRAERRISFdevVELL--GIGHLLDRRPATL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 543 SGGQKQRIAVARAILKDPRILLLDEATSALDAES--------ERIVQEAldRIMVnrttVVVAHRLSTV-RNADMIAVIH 613
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeilpylERLRDEL--DIPI----LYVSHSLDEVaRLADHVVLLE 208
|
250
....*....|....*...
gi 1063718281 614 QGKIVEKGSHSELLRDPE 631
Cdd:COG4148 209 QGRVVASGPLAEVLSRPD 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1052-1278 |
1.42e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.58 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIK--TLQLKWLRQQ 1129
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLFNE-TIRANIAYG----KGGDATETEIVSAAELSNAhgfisGLQQGYDTMVGErgvqLSGGQKQRVAIAR 1204
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGplrvRGASKEEAEKQARELLAKV-----GLAERAHHYPSE----LSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESE----RVVQDALDRVMvnrTTVVVAHRLS-TIKNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGM---TMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1052-1271 |
2.53e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.51 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKtlQLKWLRQQTG 1131
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLF-NETIRANIAYG----KGGDATETEIVSAAeLSNAHgfisgLQQgydtMVGERGVQLSGGQKQRVAIARAI 1206
Cdd:PRK09452 90 TVFQSYALFpHMTVFENVAFGlrmqKTPAAEITPRVMEA-LRMVQ-----LEE----FAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1207 VKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAH-RLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
77-355 |
2.83e-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: 116.04 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTigavGNGLGFPImtiLFGDVIDVFGQNQNSSDvsdkIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAGR 156
Cdd:cd18576 2 LILLLLSS----AIGLVFPL---LAGQLIDAALGGGDTAS----LNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 157 IRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLL 236
Cdd:cd18576 71 LRKDLYRHLQRLPLSFFH-ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 237 VMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNIV 316
Cdd:cd18576 150 VLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063718281 317 IFCTYALAVWYGGKMILEKGYTGGQ-VLIIIFAV-LTGSMS 355
Cdd:cd18576 230 LFGAIVAVLWYGGRLVLAGELTAGDlVAFLLYTLfIAGSIG 270
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
403-631 |
2.92e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.88 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwiRSKIG 482
Cdd:PRK10851 3 IEIANIKKSFGRT---QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAYG------KENATVEEIR-KATELANASKfidklpqgLDTMVGEHGTQLSGGQKQRIAVAR 554
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFGltvlprRERPNAAAIKaKVTQLLEMVQ--------LAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAEseriVQEALDRIM------VNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHSELL 627
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQ----VRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
....
gi 1063718281 628 RDPE 631
Cdd:PRK10851 226 REPA 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1072-1272 |
2.93e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.92 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1072 DLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI--KTLQLKWLRQQTGLVSQEP--VLFNETIRAN 1147
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1148 IAYGK-----GGDATETEIVSAAElsnahgfISGLQqgYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1222
Cdd:PRK13637 105 IAFGPinlglSEEEIENRVKRAMN-------IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1223 DAESErvvQDALDRVM-----VNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGK 1272
Cdd:PRK13637 176 DPKGR---DEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
102-341 |
3.35e-28 |
|
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: 116.10 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 102 GDVIDVFGQNQNSsdvsDKIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAGRIRSLYLQTILRQDIAFFDvETNTGE 181
Cdd:cd18572 20 GAVIDAVVADGSR----EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD-ATKTGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 182 VVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKA 261
Cdd:cd18572 95 LTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 262 AVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQ 341
Cdd:cd18572 175 NQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
403-624 |
3.39e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 114.34 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPArpeEQIFRGFSLSISSGSTVALVGQSGSGKST---VVSLIERfydPQSGEVRIDGINL------KEFQ 473
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGNHFdfsktpSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 474 LKWIRSKIGLVSQEPVLFTS-SIKENI--AYGKenatVEEIRKATELANASKFIDKLPqgLDTMVGEHGTQLSGGQKQRI 550
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPHlTVQQNLieAPCR----VLGLSKDQALARAEKLLERLR--LKPYADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 551 AVARAILKDPRILLLDEATSALDAE-SERIVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHS 624
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
417-642 |
3.55e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.07 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN----------LKEF---QLKWIRSKIGL 483
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVAdknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 484 VSQEPVLFTS-SIKENIAygKENATVEEIRKATELANASKFIDKLpqGLDTMV-GEHGTQLSGGQKQRIAVARAILKDPR 561
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVM--EAPIQVLGLSKQEARERAVKYLAKV--GIDERAqGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 562 ILLLDEATSALDAEserIVQEALdRIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEGAys 635
Cdd:PRK10619 173 VLLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQSP-- 246
|
....*..
gi 1063718281 636 qliRLQE 642
Cdd:PRK10619 247 ---RLQQ 250
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
403-631 |
5.27e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 115.31 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSY-PARP-EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG----INLKEFQLKW 476
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 IRSKIGLVSQ--EPVLFTSSIKENIAYGKENATVEEiRKATElaNASKFIDKLpqGLDTMVGEHGT-QLSGGQKQRIAVA 553
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKE--KALKWLKKV--GLSEDLISKSPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 554 RAILKDPRILLLDEATSALDAES-ERIVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
419-631 |
5.91e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.24 E-value: 5.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 419 QIFRGFSLSISSGSTVALVGQSGSGKSTVVS----LIERFYDPQ-SGEVRIDGINLKEFQLKWIRSKIGLVSQEP-VLFT 492
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 493 SSIKENIAYG-KENATV-------EEIRKATELAnasKFIDKLPQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILL 564
Cdd:PRK14247 97 LSIFENVALGlKLNRLVkskkelqERVRWALEKA---QLWDEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 565 LDEATSALDAESERIVQEALDRIMVNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1053-1267 |
6.49e-28 |
|
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: 112.63 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLK--WLRQQT 1130
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLFNETIRANIAYGKGG----------DATET-EIVSAAELSNAHgfISglqqgydtmvgergvQLSGGQKQR 1199
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLYGHKGLfrrlskadkaKVDEAlERVGLSELADRQ--IG---------------ELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1200 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTVVVAHRLSTI-KNADVIAVVKNGVI 1267
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1052-1265 |
8.51e-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: 8.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQIfQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTlQLKWLRQQTG 1131
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANIA-YG--KGGDATETEIVSAAELSnahgfISGLQQGYDTMVGergvQLSGGQKQRVAIARAIV 1207
Cdd:cd03263 79 YCPQFDALFDElTVREHLRfYArlKGLPKSEIKEEVELLLR-----VLGLTDKANKRAR----TLSGGMKRKLSLAIALI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKN-ADVIAVVKNG 1265
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDG 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
425-630 |
9.22e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.36 E-value: 9.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwiRSKIGLVSQEPVLFTS-SIKENIAYG- 502
Cdd:PRK11432 26 NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHmSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 503 -KENATVEEIRK----ATELANASKFIDKLpqgLDtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 577
Cdd:PRK11432 104 kMLGVPKEERKQrvkeALELVDLAGFEDRY---VD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 578 RIVQEALDRIM--VNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK11432 173 RSMREKIRELQqqFNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1052-1268 |
2.38e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.44 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveiktlqlkwlrqqtg 1131
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 lvsqEPVLFNETIRANiaygkggdateteivsaaelsnAHGfISglqqgydtMVgergVQLSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03216 62 ----KEVSFASPRDAR----------------------RAG-IA--------MV----YQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1212 VLLLDEATSAL-DAESERVVqDALDRVMVNRTTVV-VAHRLSTIKN-ADVIAVVKNGVIV 1268
Cdd:cd03216 103 LLILDEPTAALtPAEVERLF-KVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
414-611 |
2.46e-27 |
|
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: 110.65 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 414 ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWiRSKIGLVSQEPVLFTS 493
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 -SIKENIAY----GKENATVEEIRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:COG4133 90 lTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063718281 569 TSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTVRNADMIAV 611
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1052-1271 |
2.65e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.19 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYP--SRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIkTLQLKW-LRQ 1128
Cdd:PRK13635 6 IRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVWdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEP--VLFNETIRANIAYGkggdateteivsaaeLSNahgfiSGLQQgyDTMVgER--------GVQ------- 1191
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAFG---------------LEN-----IGVPR--EEMV-ERvdqalrqvGMEdflnrep 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1192 --LSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALdRVMVNRTTVVV---AHRLSTIKNADVIAVVKNGV 1266
Cdd:PRK13635 139 hrLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETV-RQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGE 217
|
....*
gi 1063718281 1267 IVEKG 1271
Cdd:PRK13635 218 ILEEG 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
401-629 |
3.17e-27 |
|
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: 112.64 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYpARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQsGEVRIDGINLKEFQLKWIRSK 480
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTSSIKENI-AYGKENAtvEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1080-1271 |
3.20e-27 |
|
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: 110.85 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1080 GKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI----KTLQLKWLRQQTGLVSQEPVLF-NETIRANIAYGKGG 1154
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1155 DATETEIVSAAELSNAHGfISGLQQGYDTmvgergvQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDAL 1234
Cdd:cd03297 103 KRNREDRISVDELLDLLG-LDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063718281 1235 DRVM--VNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKG 1271
Cdd:cd03297 175 KQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
403-643 |
3.72e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 111.71 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSG-EVRIDGINLKEFQLKWIRSKI 481
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVS---QEPVLFTSSIKENIAYGK-------ENATVEEIRKATELANASkfidklpqGLDTMVGEHGTQLSGGQKQRIA 551
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFfdsiglyREPTDEQRERARELLELL--------GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 552 VARAILKDPRILLLDEATSALDAESERIVQEALDRIMVN--RTTVVVAHRLStvrnaDMIAVIH------QGKIVEKGSH 623
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVE-----EIPPGIThvlllkDGRVVAAGPK 227
|
250 260
....*....|....*....|..
gi 1063718281 624 SELLRDP--EGAYSQLIRLQED 643
Cdd:COG1119 228 EEVLTSEnlSEAFGLPVEVERR 249
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
403-629 |
4.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.53 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPA-RP-EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL----KEFQLKW 476
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 IRSKIGLVSQ--EPVLFTSSIKENIAYGKENATVEEIrKATELANaskfiDKLpqgldTMVG-------EHGTQLSGGQK 547
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQE-EAEALAR-----EKL-----ALVGiseslfeKNPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 548 QRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKGSHSE 625
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKD 231
|
....
gi 1063718281 626 LLRD 629
Cdd:PRK13649 232 IFQD 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
383-630 |
4.99e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.66 E-value: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 383 KPEIDASDTTGKVLddirgdIELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEV 462
Cdd:PRK09452 1 SKKLNKQPSSLSPL------VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 463 RIDGINLKefQLKWIRSKIGLVSQEPVLFTS-SIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPQgldtmv 535
Cdd:PRK09452 72 MLDGQDIT--HVPAENRHVNTVFQSYALFPHmTVFENVAFGLRMQKTpaAEITPrvmeALRMVQLEEFAQRKPH------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 536 gehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIM--VNRTTVVVAH----RLSTvrnADMI 609
Cdd:PRK09452 144 -----QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHdqeeALTM---SDRI 215
|
250 260
....*....|....*....|.
gi 1063718281 610 AVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK09452 216 VVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
403-629 |
5.30e-27 |
|
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: 110.22 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG---INLKEFQLkwIRS 479
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrdiTGLPPHER--ARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFTS-SIKENIAYGKENATVEEIRKATElanasKFIDKLPQgLDTMVGEHGTQLSGGQKQRIAVARAILK 558
Cdd:cd03224 76 GIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLE-----RVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 559 DPRILLLDEATSALdaeSERIVQEALDRIM-VNR---TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:cd03224 150 RPKLLLLDEPSEGL---APKIVEEIFEAIReLRDegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
403-636 |
5.58e-27 |
|
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: 117.09 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeEQIFR----------GFSLSISSGSTVALVGQSGSGKST----VVSLIerfydPQSGEVRIDGIN 468
Cdd:COG4172 276 LEARDLKVWFPIK--RGLFRrtvghvkavdGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 469 ---LKEFQLKWIRSKIGLVSQEPvlFTS-----SIKENIAYG----KENATVEEIRKATelanaskfIDKLPQ-GLD-TM 534
Cdd:COG4172 349 ldgLSRRALRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARV--------AEALEEvGLDpAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 535 VGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDaeseRIVQ----EALDRIMVNR--TTVVVAHRLSTVRN-AD 607
Cdd:COG4172 419 RHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqilDLLRDLQREHglAYLFISHDLAVVRAlAH 494
|
250 260
....*....|....*....|....*....
gi 1063718281 608 MIAVIHQGKIVEKGSHSELLRDPEGAYSQ 636
Cdd:COG4172 495 RVMVMKDGKVVEQGPTEQVFDAPQHPYTR 523
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
733-1002 |
6.57e-27 |
|
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: 112.19 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 733 GSIAAVLNGVILPIFGILISSVIKAFF--KPPEQLKSDTRFWAIIFMLLGVASMVvfpaQTIFFSIAGCKLVQRIRSMCF 810
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALggGDTASLNQIALLLLGLFLLQAVFSFF----RIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 811 EKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGY 890
Cdd:cd18576 77 RHLQRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 891 IYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSY 970
Cdd:cd18576 155 LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
|
250 260 270
....*....|....*....|....*....|...
gi 1063718281 971 AASFYAGARLVDDGKTTFDSVFR-VFFALTMAA 1002
Cdd:cd18576 235 VAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG 267
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
398-642 |
7.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.02 E-value: 7.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 398 DIRGDIELNNVNFSYPAR-PEEqiFRGF---SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG----INL 469
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKtPFE--FKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 470 KEF-QLKWIRSKIGLVSQEP--VLFTSSIKENIAYGKEN--ATVEEIRKatelanaskfidKLPQGLDTM------VGEH 538
Cdd:PRK13645 80 KKIkEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNlgENKQEAYK------------KVPELLKLVqlpedyVKRS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 539 GTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVN--RTTVVVAHRLSTV-RNADMIAVIHQG 615
Cdd:PRK13645 148 PFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEG 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063718281 616 KIVEKG------SHSELLR----DPEGAYSQLIRLQE 642
Cdd:PRK13645 228 KVISIGspfeifSNQELLTkieiDPPKLYQLMYKLKN 264
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
423-636 |
8.06e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 112.75 E-value: 8.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTV---VSLIERfydPQSGEVRIDGINLKEF---QLKWIRSKIGLVSQEPvlftssik 496
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNP-------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 497 eniaYGKEN------ATVEE-IRKATELANAskfiDKLPQGLDTM--VG---EHGTQ----LSGGQKQRIAVARAILKDP 560
Cdd:PRK11308 102 ----YGSLNprkkvgQILEEpLLINTSLSAA----ERREKALAMMakVGlrpEHYDRyphmFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 561 RILLLDEATSALDAEserIVQEALDRIM-----VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEGAY 634
Cdd:PRK11308 174 DVVVADEPVSALDVS---VQAQVLNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
|
..
gi 1063718281 635 SQ 636
Cdd:PRK11308 251 TQ 252
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1075-1276 |
1.18e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 110.22 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL--------QLKWLRQQTGLVSQEPVLF-NETIR 1145
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkgLIRQLRQHVGFVFQNFNLFpHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1146 ANIAYGK---GGDATETEIVSAAELSNAHGfISGLQQGYDTmvgergvQLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1222
Cdd:PRK11264 104 ENIIEGPvivKGEPKEEATARARELLAKVG-LAGKETSYPR-------RLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1223 DAEserVVQDALDRVMV----NRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETL 1276
Cdd:PRK11264 176 DPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
403-618 |
1.28e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.56 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVN--FsYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQlkw 476
Cdd:COG1101 2 LELKNLSktF-NPGTVNEkRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 iRSK-IGLVSQEPVLFTS---SIKEN--IAY--GKENAtveeIRKATELANASKFIDKLPQ---GL----DTMVGehgtQ 541
Cdd:COG1101 78 -RAKyIGRVFQDPMMGTApsmTIEENlaLAYrrGKRRG----LRRGLTKKRRELFRELLATlglGLenrlDTKVG----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 542 LSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRImVNR---TTVVVAHRLS-TVRNADMIAVIHQGKI 617
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
.
gi 1063718281 618 V 618
Cdd:COG1101 228 I 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
414-627 |
1.40e-26 |
|
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: 110.67 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 414 ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF---QLKWIRSKIGLVSQE--- 487
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 488 PVLFTSSIKENIAYGKENAT----VEEIRKATELANA----SKFIDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKD 559
Cdd:TIGR02769 100 AVNPRMTVRQIIGEPLRHLTsldeSEQKARIAELLDMvglrSEDADKLPR-----------QLSGGQLQRINIARALAVK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRIMVNRTT--VVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELL 627
Cdd:TIGR02769 169 PKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1052-1271 |
1.45e-26 |
|
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: 108.82 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTiALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTlQLKWLRQQTG 1131
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLF-NETIRANIAYG---KGGDATET--EIVSAAELSNahgfisgLQQGYDTMVGergvQLSGGQKQRVAIARA 1205
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYIawlKGIPSKEVkaRVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
414-628 |
1.89e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.16 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 414 ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF---QLKWIRSKIGLVSQEP-- 488
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 489 -VLFTSSIKENIAY----------GKENATVEEIRKATELANAskFIDKLPQgldtmvgehgtQLSGGQKQRIAVARAIL 557
Cdd:PRK10419 101 aVNPRKTVREIIREplrhllsldkAERLARASEMLRAVDLDDS--VLDKRPP-----------QLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 558 KDPRILLLDEATSALDAESERIVQEALDRIMVNRTT--VVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELLR 628
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
407-636 |
2.12e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.75 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 407 NVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL----KEFQLKWI--RSK 480
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkDIFQIDAIklRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQ 636
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1052-1269 |
2.81e-26 |
|
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: 108.68 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP-DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL----QLKWL 1126
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedaRARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 RQQTGLVSQ-EPVLFNETIRANIAY-----GKgGDATETeivsAAELSNAHGfisglqqgydtmVGERG----VQLSGGQ 1196
Cdd:COG4181 89 ARHVGFVFQsFQLLPTLTALENVMLplelaGR-RDARAR----ARALLERVG------------LGHRLdhypAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR---TT-VVVAHRLSTIKNADVIAVVKNGVIVE 1269
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE--LNRergTTlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
422-626 |
2.88e-26 |
|
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: 108.36 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfQLKWIRSKIGLVSQEPVLFtssikeniay 501
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 502 gkENATVEE----------IRKATELANASKFIDK--LPQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEAT 569
Cdd:cd03263 88 --DELTVREhlrfyarlkgLPKSEIKEEVELLLRVlgLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 570 SALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSEL 626
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
403-632 |
2.92e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.84 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPArPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEV-----RIDGINLKEfqlkwI 477
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEK-----L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 478 RSKIGLVSQEP--VLFTSSIKENIAYGKENATV------EEIRKATELANASKFIDKLPQGLdtmvgehgtqlSGGQKQR 549
Cdd:PRK13648 82 RKHIGIVFQNPdnQFVGSIVKYDVAFGLENHAVpydemhRRVSEALKQVDMLERADYEPNAL-----------SGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 550 IAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELL 627
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIF 230
|
....*
gi 1063718281 628 RDPEG 632
Cdd:PRK13648 231 DHAEE 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1036-1278 |
4.49e-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: 114.40 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1036 DPSDESGRVLdnvkgdIELRHISFKYPSR--------PDVQIFQDLCLSIRAGKTIALVGESGSGKSTV-IALLQrfYDP 1106
Cdd:COG4172 266 RPVPPDAPPL------LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLR--LIP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1107 DSGQITLDGVEIKTL---QLKWLRQQTGLVSQEPvlFNE-----TIRANIA-----YGKGGDATE-TEIVSAAelsnahg 1172
Cdd:COG4172 338 SEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDP--FGSlsprmTVGQIIAeglrvHGPGLSAAErRARVAEA------- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1173 fisgLQQ-GYDTMVGERGV-QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDaeseRVVQ----DALDRVMVNR--TTV 1244
Cdd:COG4172 409 ----LEEvGLDPAARHRYPhEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqilDLLRDLQREHglAYL 480
|
250 260 270
....*....|....*....|....*....|....*
gi 1063718281 1245 VVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:COG4172 481 FISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
403-631 |
6.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.02 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQ---IFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKW-IR 478
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEP--VLFTSSIKENIAYGKENATV--EEIRKATELA----NASKFIDKLPQgldtmvgehgtQLSGGQKQRI 550
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLGIppEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 551 AVARAILKDPRILLLDEATSALDAESERivqEALDRIM-VNR----TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSE 625
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRR---EVVNTIKeLNKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
....*.
gi 1063718281 626 LLRDPE 631
Cdd:PRK13633 231 IFKEVE 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1052-1271 |
7.31e-26 |
|
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: 106.81 E-value: 7.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqifQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwlRQQTG 1131
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANIAYGKGGDATETEIVSAAELSNAHgfisglQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDP 1210
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVALA------RVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1211 KVLLLDEATSALDAESERVVQDALDRVMVNR--TTVVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1278 |
7.70e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 7.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEP--VLFNETIRANIAYGK-----GGDATETEIVSAAELSNAHGFISglQQGYdtmvgergvQLSGGQKQRVAIAR 1204
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPvnmglDKDEVERRVEEALKAVRMWDFRD--KPPY---------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLS-TIKNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
705-1294 |
8.52e-26 |
|
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: 116.20 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 705 VSTPIKEKKVSFFRVaaLNKPEIPMLILGSIAAVLNGVILPIFGILISSVIKaFFKPPEQLKSDTRFWAIifmLLGVASM 784
Cdd:TIGR00957 296 VKSPHKPRKPSLFKV--LYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIR-FVNDPMAPDWQGYFYTG---LLFVCAC 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 785 VVFPAQTIFFSIAGCKLVqRIRSMCFEKVVRMEVGWFDETENSS--GAIGARLSADAATVRGLvgdalAQTVQNLASVTA 862
Cdd:TIGR00957 370 LQTLILHQYFHICFVSGM-RIKTAVMGAVYRKALVITNSARKSStvGEIVNLMSVDAQRFMDL-----ATYINMIWSAPL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 863 GLVIAFVASWQ-LAFIVLA----MLPLIGLNGYIYMKfmvgfsadaKRMYEEASQVANDAvgSIRTVASFCAEEKVMKMY 937
Cdd:TIGR00957 444 QVILALYFLWLnLGPSVLAgvavMVLMVPLNAVMAMK---------TKTYQVAHMKSKDN--RIKLMNEILNGIKVLKLY 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 938 ------KKKCEGpmrtgIRQG---------IVSGIG----FGVSFFVLFSSYAASFYAGARLVDDGKTTFDSV--FRVF- 995
Cdd:TIGR00957 513 awelafLDKVEG-----IRQEelkvlkksaYLHAVGtftwVCTPFLVALITFAVYVTVDENNILDAEKAFVSLalFNILr 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 996 FALTMAAVAISQSSSLSPDSSKASnaaasIFAvidRESKIDP-SDESGRVLDNVKGDIELRHISFKYpSRPDVQIFQDLC 1074
Cdd:TIGR00957 588 FPLNILPMVISSIVQASVSLKRLR-----IFL---SHEELEPdSIERRTIKPGEGNSITVHNATFTW-ARDLPPTLNGIT 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRqqtglvsqepvlfNETIRANIAYGKGG 1154
Cdd:TIGR00957 659 FSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQ-------------NDSLRENILFGKAL 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1155 DAT--ETEIVSAAELSNAHGFISGLQqgydTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQD 1232
Cdd:TIGR00957 726 NEKyyQQVLEACALLPDLEILPSGDR----TEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1233 AL---DRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINiKDGVYASLVQLHLSA 1294
Cdd:TIGR00957 802 HVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ-RDGAFAEFLRTYAPD 865
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
425-652 |
8.69e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.66 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF---QLKWIR-SKIGLVSQEPVLFTS-SIKENI 499
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRrKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 500 AYGKENATVEEIRKAtelanaSKFIDKLPQ-GLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 578
Cdd:PRK10070 128 AFGMELAGINAEERR------EKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 579 IVQEALDRIMV--NRTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQLIRLQEDTKQTEDSTD 652
Cdd:PRK10070 202 EMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKD 278
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
403-621 |
8.70e-26 |
|
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: 106.42 E-value: 8.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYparpEEQIFRgFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwiRSKIG 482
Cdd:cd03298 1 VRLDKIRFSY----GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAYGKENAT--VEEIRKATELANASkfidklpQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSPGLklTAEDRQAIEVALAR-------VGLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 621
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1027-1274 |
1.03e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.70 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1027 AVIDReskidPSDESGRVLDNVkgdIELRHISFKYPSRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDP 1106
Cdd:PRK11607 3 DAIPR-----PQAKTRKALTPL---LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1107 DSGQITLDGVEIKtlQLKWLRQQTGLVSQEPVLF-NETIRANIAYG-KGGDATETEIVSAAE--LSNAHgfisgLQQgyd 1182
Cdd:PRK11607 72 TAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQNIAFGlKQDKLPKAEIASRVNemLGLVH-----MQE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1183 tMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAE-SERV---VQDALDRVMVnrTTVVVAH-RLSTIKNAD 1257
Cdd:PRK11607 142 -FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMqleVVDILERVGV--TCVMVTHdQEEAMTMAG 218
|
250
....*....|....*..
gi 1063718281 1258 VIAVVKNGVIVEKGKHE 1274
Cdd:PRK11607 219 RIAIMNRGKFVQIGEPE 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
403-627 |
1.77e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.20 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSY---PARpeeqifrgFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwiRS 479
Cdd:PRK10771 2 LKLTDITWLYhhlPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFTS-SIKENIAYG---------KENATVEEIRKATELANaskFIDKLPqgldtmvgehgTQLSGGQKQR 549
Cdd:PRK10771 72 PVSMLFQENNLFSHlTVAQNIGLGlnpglklnaAQREKLHAIARQMGIED---LLARLP-----------GQLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 550 IAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSEL 626
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDEL 217
|
.
gi 1063718281 627 L 627
Cdd:PRK10771 218 L 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
403-630 |
1.80e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.04 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPArpeEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQsGEVRIDG--------INLKEFQL 474
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 475 KWIRSKIGLVSQEPVLFTSSIKENIAYGKE----------NATVEEIRKATELANASKfidklpqgldTMVGEHGTQLSG 544
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpkleiDDIVESALKDADLWDEIK----------HKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 545 GQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALD--RIMVNRTTVVVAHRLSTV-RNADMIAVIHQ-----GK 616
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQ 233
|
250
....*....|....
gi 1063718281 617 IVEKGSHSELLRDP 630
Cdd:PRK14258 234 LVEFGLTKKIFNSP 247
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
422-631 |
1.84e-25 |
|
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: 106.37 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG---INLKEFQlkwiRSKIGLVS--QEPVLFTS-SI 495
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGediTGLPPHE----IARLGIGRtfQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 496 KENIAYGKENAT---------VEEIRKATELANAskFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLD 566
Cdd:cd03219 93 LENVMVAAQARTgsglllaraRREEREARERAEE--LLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 567 EATSAL-DAESERIVqEALDRIMV-NRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:cd03219 169 EPAAGLnPEETEELA-ELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1052-1224 |
2.00e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYP-SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIktlqlkwlrqqT 1130
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----------T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLFNE-------TIRANIAYG---KGGDATETEIVSAAELSnahgfISGLQQgydtmVGERGV-QLSGGQKQR 1199
Cdd:COG4525 73 GPGADRGVVFQKdallpwlNVLDNVAFGlrlRGVPKAERRARAEELLA-----LVGLAD-----FARRRIwQLSGGMRQR 142
|
170 180
....*....|....*....|....*
gi 1063718281 1200 VAIARAIVKDPKVLLLDEATSALDA 1224
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDA 167
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1051-1271 |
2.10e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.80 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1051 DIELRHISFKY-PSRPdvqiFQ-----DLCLSIRAGKTIALVGESGSGKSTVI----ALLQrfydPDSGQITLDGVEI-- 1118
Cdd:PRK13634 2 DITFQKVEHRYqYKTP----FErralyDVNVSIPSGSYVAIIGHTGSGKSTLLqhlnGLLQ----PTSGTVTIGERVIta 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1119 --KTLQLKWLRQQTGLVSQ--EPVLFNETIRANIAYG-KGGDATETEivsAAELSNAHGFISGLqqgyDTMVGERG-VQL 1192
Cdd:PRK13634 74 gkKNKKLKPLRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEED---AKQKAREMIELVGL----PEELLARSpFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1193 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVE 1269
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
..
gi 1063718281 1270 KG 1271
Cdd:PRK13634 227 QG 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
401-626 |
2.44e-25 |
|
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: 107.25 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefqlkwirsK 480
Cdd:cd03291 36 DDNNLFFSNLCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------R 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTSSIKENIAYGkenATVEEIR-----KATELanaSKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARA 555
Cdd:cd03291 100 ISFSSQFSWIMPGTIKENIIFG---VSYDEYRyksvvKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 556 ILKDPRILLLDEATSALDAESER-IVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSEL 626
Cdd:cd03291 174 VYKDADLYLLDSPFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1053-1268 |
2.50e-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: 105.03 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSRPDvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKtlqLKWLRQQTGL 1132
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1133 VSQEP--VLFNETIRANIAYGKGGDATETEIVSA-------AELSNAHGFIsglqqgydtmvgergvqLSGGQKQRVAIA 1203
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKELDAGNEQAETvlkdldlYALKERHPLS-----------------LSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1204 RAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTIKN-ADVIAVVKNGVIV 1268
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVItHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1052-1278 |
2.67e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG--------VEIKTLQL 1123
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1124 kwLRQQTGLVSQE----PVLfneTIRANIaygkggdaTETEI-----VSAAELSNAHGFISGLQqgYDTMVGERGVQLSG 1194
Cdd:COG4161 80 --LRQKVGMVFQQynlwPHL---TVMENL--------IEAPCkvlglSKEQAREKAMKLLARLR--LTDKADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSALDAE-SERVVQDALDRVMVNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGK 1272
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGD 224
|
....*.
gi 1063718281 1273 HETLIN 1278
Cdd:COG4161 225 ASHFTQ 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1052-1265 |
3.87e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.74 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIkTLQLKW-LRQQT 1130
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENVWdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEP--VLFNETIRANIAYG---KGGDATE--TEIVSAAELSNAHGFISglqqgydtmvgERGVQLSGGQKQRVAIA 1203
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGlenKGIPHEEmkERVNEALELVGMQDFKE-----------REPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1204 RAIVKDPKVLLLDEATSALDAESE----RVVQDALDRvmVNRTTVVVAHRLSTIKNADVIAVVKNG 1265
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
403-621 |
4.43e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.78 E-value: 4.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARP---EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLI--ERFYDPQSGEVRIDGINLKefqLKWI 477
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 478 RSKIGLVSQEPVLFtssikeniaygkENATVEEirkatelanASKFIDKLpQGLdtmvgehgtqlSGGQKQRIAVARAIL 557
Cdd:cd03213 81 RKIIGYVPQDDILH------------PTLTVRE---------TLMFAAKL-RGL-----------SGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 558 KDPRILLLDEATSALDAESERIVQEALdRIMV--NRTTVVVAHRLST--VRNADMIAVIHQGKIVEKG 621
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLL-RRLAdtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
404-589 |
5.64e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.10 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQ---SGEVRIDGINLKEFQLKwiRSK 480
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENIAYGKENATVEEIRKAT---ELANAskfidklpqGLDTMVGEHGTQLSGGQKQRIAVARAI 556
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLAFALPPTIGRAQRRARveqALEEA---------GLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063718281 557 LKDPRILLLDEATSALDAES---------ERIVQEALDRIMV 589
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALraqfrefvfEQIRQRGIPALLV 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
403-631 |
7.04e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.31 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQ-----SGEVRIDGINLKEFQLKWI 477
Cdd:PRK14267 5 IETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 478 --RSKIGLVSQEPVLFTS-SIKENIAYG-KENATV---EEIRKATELA-NASKFIDKLPQGLDtmvgEHGTQLSGGQKQR 549
Cdd:PRK14267 82 evRREVGMVFQYPNPFPHlTIYDNVAIGvKLNGLVkskKELDERVEWAlKKAALWDEVKDRLN----DYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 550 IAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHR-LSTVRNADMIAVIHQGKIVEKGSHSELLR 628
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
...
gi 1063718281 629 DPE 631
Cdd:PRK14267 238 NPE 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
425-635 |
1.00e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKefQLKWIRSKIGLVSQEPVLFTS-SIKENIAYGK 503
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 504 E---------NATVEEIrkaTELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDA 574
Cdd:PRK11607 117 KqdklpkaeiASRVNEM---LGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 575 E-SERIVQEALDRI-MVNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHSELLRDPEGAYS 635
Cdd:PRK11607 183 KlRDRMQLEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
422-649 |
1.01e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYD--PQ---SGEVRIDGINLKEFQLKW--IRSKIGLVSQEPVLFTSS 494
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 495 IKENIAYG--------KE--NATVEEIRKATELANASKfiDKLPqglDTMVGehgtqLSGGQKQRIAVARAILKDPRILL 564
Cdd:PRK14239 102 IYENVVYGlrlkgikdKQvlDEAVEKSLKGASIWDEVK--DRLH---DSALG-----LSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 565 LDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELLRDPEgaysqlirlqed 643
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMFMNPK------------ 239
|
....*.
gi 1063718281 644 TKQTED 649
Cdd:PRK14239 240 HKETED 245
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
403-659 |
1.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.16 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--INLKEFQLKWIRSK 480
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEP--VLFTSSIKENIAYGKENATV--EEIRK----ATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAV 552
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLGLskEEVEKrvkeALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 553 ARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
250 260
....*....|....*....|....*....
gi 1063718281 631 EGAYSQLIRLQEDTKQTEDSTDEQKLSME 659
Cdd:PRK13639 229 ETIRKANLRLPRVAHLIEILNKEDNLPIK 257
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
419-636 |
1.23e-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: 109.77 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 419 QIFRGFSLSISSGSTVALVGQSGSGKS----TVVSLIERFYDPQSGEVRIDGINL---KEFQLKWIR-SKIGLVSQEPV- 489
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRgNRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 490 ----LFT--SSIKENIAY-----GKE-NATVEEIRKATELANASKFIDKLPqgldtmvgeHgtQLSGGQKQRIAVARAIL 557
Cdd:COG4172 104 slnpLHTigKQIAEVLRLhrglsGAAaRARALELLERVGIPDPERRLDAYP---------H--QLSGGQRQRVMIAMALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 558 KDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVV--AHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEGAY 634
Cdd:COG4172 173 NEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLliTHDLGVVRRfADRVAVMRQGEIVEQGPTAELFAAPQHPY 252
|
..
gi 1063718281 635 SQ 636
Cdd:COG4172 253 TR 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1053-1225 |
1.65e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.95 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPD---SGQITLDGVEIKTLQLkwLRQQ 1129
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLF-NETIRANIAYG----KGGDATETEIVSAAELSNAHGFisglqqgydtmvGERGV-QLSGGQKQRVAIA 1203
Cdd:COG4136 78 IGILFQDDLLFpHLSVGENLAFAlpptIGRAQRRARVEQALEEAGLAGF------------ADRDPaTLSGGQRARVALL 145
|
170 180
....*....|....*....|..
gi 1063718281 1204 RAIVKDPKVLLLDEATSALDAE 1225
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAA 167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1052-1269 |
1.93e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.95 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKtlqlkwLR---- 1127
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR------FRsprd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 -QQTG--LVSQEPVLFNE-TIRANIAYG----KGG----DATETEivsAAELSNAHGF-ISGlqqgyDTMVGErgvqLSG 1194
Cdd:COG1129 76 aQAAGiaIIHQELNLVPNlSVAENIFLGreprRGGlidwRAMRRR---ARELLARLGLdIDP-----DTPVGD----LSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSAL-DAESER---VVQDALDRvmvNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVE 1269
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLtEREVERlfrIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
425-650 |
2.04e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 104.15 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--INLKEFQLkwiRSK-IGLVSQEPvlfTSSIKENIAY 501
Cdd:COG4167 33 SFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkLEYGDYKY---RCKhIRMIFQDP---NTSLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 502 GKenaTVEE-IRKATELaNASKFIDKLPQGLdTMVG---EHGT----QLSGGQKQRIAVARAILKDPRILLLDEATSALD 573
Cdd:COG4167 107 GQ---ILEEpLRLNTDL-TAEEREERIFATL-RLVGllpEHANfyphMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 574 AeSER--IV------QEALdrimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEGAYSQ-LIRLQED 643
Cdd:COG4167 182 M-SVRsqIInlmlelQEKL-----GISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANPQHEVTKrLIESHFG 255
|
....*..
gi 1063718281 644 TKQTEDS 650
Cdd:COG4167 256 EALTADA 262
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1027-1249 |
2.66e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1027 AVIDR--------ESKIDPSDESGRVLDNVKGDIELRHISFKypsRPDVQ-IFQDLCLSIRAGKTIALVGESGSGKST-- 1095
Cdd:COG4178 330 ATVDRlagfeealEAADALPEAASRIETSEDGALALEDLTLR---TPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTll 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1096 -VIALLQRFYdpdSGQITLDGVEiKTLqlkwlrqqtgLVSQEPVLFNETIRANIAYGKGGDA-TETEIVSAAELSNAHGF 1173
Cdd:COG4178 407 rAIAGLWPYG---SGRIARPAGA-RVL----------FLPQRPYLPLGTLREALLYPATAEAfSDAELREALEAVGLGHL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1174 ISGLQQGYDtmvgeRGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHR 1249
Cdd:COG4178 473 AERLDEEAD-----WDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1052-1278 |
3.17e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG------VEIKTLQLKW 1125
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 LRQQTGLVSQE----PVLfneTIRANIaygkggdaTETEI----VSAAE-LSNAHGFISGLQQgydTMVGER-GVQLSGG 1195
Cdd:PRK11124 80 LRRNVGMVFQQynlwPHL---TVQQNL--------IEAPCrvlgLSKDQaLARAEKLLERLRL---KPYADRfPLHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1196 QKQRVAIARAIVKDPKVLLLDEATSALDAE-SERVVQDALDRVMVNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGKH 1273
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDA 225
|
....*
gi 1063718281 1274 ETLIN 1278
Cdd:PRK11124 226 SCFTQ 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
425-615 |
4.38e-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: 102.02 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSK----IGLVSQEPVLFTSSIKENIA 500
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENIT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 501 YGKEnATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE-SERI 579
Cdd:cd03290 101 FGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063718281 580 VQEALDRIMVN--RTTVVVAHRLSTVRNADMIAVIHQG 615
Cdd:cd03290 180 MQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1283 |
4.87e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.29 E-value: 4.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQIfQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEP--VLFNETIRANIAYGkggdaTETEIVSAAELsnaHGFISGLQQGYDtMVGERGVQ---LSGGQKQRVAIARAI 1206
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFG-----LENHAVPYDEM---HRRVSEALKQVD-MLERADYEpnaLSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1207 VKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIKDGV 1283
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
386-599 |
5.00e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 386 IDASDTTGKVLDDIR----GDIELNNVNFSYPArpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGE 461
Cdd:COG4178 342 LEAADALPEAASRIEtsedGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 462 VRI-DGinlkefqlkwirSKIGLVSQEPVLFTSSIKENIAYGKENATV--EEIRKATELANASKFIDKLPQGLDTmvgeh 538
Cdd:COG4178 420 IARpAG------------ARVLFLPQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGHLAERLDEEADW----- 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 539 GTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHR 599
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
422-640 |
5.14e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.41 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLKWIR----SKIGLVSQEPVLFTS-SIK 496
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRdaqaAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 497 ENIAYGKENATVEEIRKATELANASKFIDKLpqGLD----TMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSAL 572
Cdd:COG1129 98 ENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 573 -DAESER---IVQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDpegaysQLIRL 640
Cdd:COG1129 172 tEREVERlfrIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTED------ELVRL 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-629 |
6.35e-24 |
|
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: 110.00 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYpARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQsGEVRIDGINLKEFQLKWIRSK 480
Cdd:TIGR01271 1216 GQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTSSIKENIAyGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 560
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 561 RILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
403-613 |
6.83e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTSSIKENIAYGKEnatveeIRKATelANASKFIDKLPQ-GL-DTMVGEHGTQLSGGQKQRIAVARAILKDP 560
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQ------IRNQQ--PDPAIFLDDLERfALpDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 561 RILLLDEATSALDAESERIVQEALDRIMVNRTTVV--VAHRLSTVRNADmiAVIH 613
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHAD--KVIT 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1052-1272 |
9.59e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDS---GQITLDGVEIKTLQLKWLRQ 1128
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEP--VLFNETIRANIAYGkggdaTETEIVSAAE-LSNAHGFISglQQGYDTMVGERGVQLSGGQKQRVAIARA 1205
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFG-----LENRAVPRPEmIKIVRDVLA--DVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESERVVQDALDRVMV--NRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGK 1272
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
404-631 |
1.21e-23 |
|
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: 101.21 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG---INLKEFQLkwIRSK 480
Cdd:COG0410 5 EVENLHAGYGGI---HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGediTGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENI---AY-----GKENATVEEIrkaTELanaskFidklPQgLDTMVGEHGTQLSGGQKQRIA 551
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLllgAYarrdrAEVRADLERV---YEL-----F----PR-LKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 552 VARAILKDPRILLLDEATSALdaeSERIVQEALDRIM-VNR--TTVVV----AHRLSTVrnADMIAVIHQGKIVEKGSHS 624
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRrLNRegVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAA 221
|
....*..
gi 1063718281 625 ELLRDPE 631
Cdd:COG0410 222 ELLADPE 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
422-622 |
1.29e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.78 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGeVRIDG--------INLKEFQLKWIRSKIGLVSQEPVLFTS 493
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGkvtfhgknLYAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 SIKENIAYGKE--------NATVEEIRKATELANASKfiDKLPQGldtmvgehGTQLSGGQKQRIAVARAILKDPRILLL 565
Cdd:PRK14243 106 SIYDNIAYGARingykgdmDELVERSLRQAALWDEVK--DKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 566 DEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQgKIVEKGS 622
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFNV-ELTEGGG 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
403-618 |
1.61e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 98.27 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPArpeEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefqlkwirskig 482
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 lvsqEPVLFTSsikeniaygkenatveeIRKATELanaskfidklpqGLdTMVgehgTQLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03216 62 ----KEVSFAS-----------------PRDARRA------------GI-AMV----YQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIV 618
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
403-629 |
1.74e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.39 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQlKWIRSKI- 481
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELARRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVL-FTSSIKENIAYGK-----ENATVEEI-RKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVAR 554
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGRaphglSRAEDDALvAAALAQVDLAHLAGRDYP-----------QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AIL------KDPRILLLDEATSALD-AESERIVQEALDRIMVNRTTV-VVAHRLS-TVRNADMIAVIHQGKIVEKGSHSE 625
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAViVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
....
gi 1063718281 626 LLRD 629
Cdd:PRK13548 228 VLTP 231
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
77-329 |
2.06e-23 |
|
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: 101.74 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGnGLGFPIMTilfGDVIDVFGQNQNSSdvsdkiAKVALkfvyLGLGTLVAALLQ-VSGWMIS--GERQ 153
Cdd:cd18551 2 ILALLLSLLGTAA-SLAQPLLV---KNLIDALSAGGSSG------GLLAL----LVALFLLQAVLSaLSSYLLGrtGERV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 154 AGRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSI 233
Cdd:cd18551 68 VLDLRRRLWRRLLRLPVSFFD-RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 234 PLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTL 313
Cdd:cd18551 147 PLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLM 226
|
250
....*....|....*.
gi 1063718281 314 NIVIFCTYALAVWYGG 329
Cdd:cd18551 227 GLAVQLALLVVLGVGG 242
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1027-1274 |
2.23e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 108.33 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1027 AVIDRESKIDPS------DESGRVLDNVKGDIELRhiSFKYPSRPDVQIFQ--------DLCLSIRAGKTIALVGESGSG 1092
Cdd:PTZ00243 621 VVVEDTDYGSPSsasrhiVEGGTGGGHEATPTSER--SAKTPKMKTDDFFElepkvllrDVSVSVPRGKLTVVLGATGSG 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1093 KSTVIALLQRFYDPDSGQItldgveiktlqlkWLRQQTGLVSQEPVLFNETIRANIAYGKGGDATEteIVSAAELSNAHG 1172
Cdd:PTZ00243 699 KSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNILFFDEEDAAR--LADAVRVSQLEA 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1173 FISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAE-SERVVQDALDRVMVNRTTVVVAHRLS 1251
Cdd:PTZ00243 764 DLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVH 843
|
250 260
....*....|....*....|...
gi 1063718281 1252 TIKNADVIAVVKNGVIVEKGKHE 1274
Cdd:PTZ00243 844 VVPRADYVVALGDGRVEFSGSSA 866
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1052-1276 |
2.47e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.26 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG--VEIKTLQlkwlRQQ 1129
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHRSIQ----QRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLF-NETIRANIAYG---KGGDATE--TEIVSAAELSNAHGFisglqqgydtmvGERGV-QLSGGQKQRVAI 1202
Cdd:PRK11432 80 ICMVFQSYALFpHMSLGENVGYGlkmLGVPKEErkQRVKEALELVDLAGF------------EDRYVdQISGGQQQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1203 ARAIVKDPKVLLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKGKHETL 1276
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQqqFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
403-587 |
2.64e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQ-IFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefqlKWIR--- 478
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG--------VPVTgpg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEPVLFT-SSIKENIAYGKENATVEeirKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAIL 557
Cdd:COG4525 76 ADRGVVFQKDALLPwLNVLDNVAFGLRLRGVP---KAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190
....*....|....*....|....*....|
gi 1063718281 558 KDPRILLLDEATSALDAESERIVQEALDRI 587
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
403-629 |
3.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.35 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSY-PARP-EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL----KEFQLKW 476
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 IRSKIGLVSQEP--VLFTSSIKENIAYGKENATV--EEIRKAT----ELANASK-FIDKLPqgldtmvgehgTQLSGGQK 547
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIpkEKAEKIAaeklEMVGLADeFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 548 QRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRI-MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSE 625
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....
gi 1063718281 626 LLRD 629
Cdd:PRK13643 231 VFQE 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
403-619 |
3.07e-23 |
|
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: 99.82 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLI---ERfydPQSGEVRIDGINLkeFQL---- 474
Cdd:COG4181 9 IELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDL--FALdeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 475 --KWIRSKIGLVSQ-EPVLFTSSIKENIAYGKENATVEEIRkatelANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIA 551
Cdd:COG4181 84 raRLRARHVGFVFQsFQLLPTLTALENVMLPLELAGRRDAR-----ARARALLERV--GLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 552 VARAILKDPRILLLDEATSALDAESERIVQEALDRimVNR---TT-VVVAHRLSTVRNADMIAVIHQGKIVE 619
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFE--LNRergTTlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1052-1291 |
3.77e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVL-FNETIRANIAYG----KGGDATETEIVSAA-ELSNAHGFisglqqgydtmvGERGV-QLSGGQKQRVAIAR 1204
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGraphGLSRAEDDALVAAAlAQVDLAHL------------AGRDYpQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1205 AIV------KDPKVLLLDEATSALD-AESERVVQDALDRVMVNRTTV-VVAHRLstikN-----ADVIAVVKNGVIVEKG 1271
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAViVVLHDL----NlaaryADRIVLLHQGRLVADG 223
|
250 260
....*....|....*....|....*
gi 1063718281 1272 KHETLI---NIKDgVY--ASLVQLH 1291
Cdd:PRK13548 224 TPAEVLtpeTLRR-VYgaDVLVQPH 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1052-1272 |
5.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.59 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQ---IFqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI----KTLQLK 1124
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgraLF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQTGLVSQ--EPVLFNETIRANIAYGK---GGDATETEIVSAAELSnahgfISGLQqgyDTMVGERGVQLSGGQKQR 1199
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPqnfGVSQEEAEALAREKLA-----LVGIS---ESLFEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1200 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVV-VAHRLSTIKN-ADVIAVVKNGVIVEKGK 1272
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
405-576 |
5.75e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 405 LNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefqlkwiRSKIGLV 484
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 485 SQEPVLFTS-SIKENI----------------AYGKENATVEEIRKATEL-------------ANASKFIDKL---PQGL 531
Cdd:COG0488 67 PQEPPLDDDlTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELqeefealggweaeARAEEILSGLgfpEEDL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063718281 532 DTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 576
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1052-1276 |
5.81e-23 |
|
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: 99.39 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQ-ITLDGVEIKTLQLKWLRQQT 1130
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVS---QEPVLFNETIRaniaygkggdatetEIVsaaeLSNAHGFIsGLQQGYDTMVGER--------GV--------- 1190
Cdd:COG1119 81 GLVSpalQLRFPRDETVL--------------DVV----LSGFFDSI-GLYREPTDEQRERarellellGLahladrpfg 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1191 QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN--RTTVVVAHRLStiknaDVIAVV------ 1262
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVE-----EIPPGIthvlll 216
|
250
....*....|....*
gi 1063718281 1263 KNGVIVEKG-KHETL 1276
Cdd:COG1119 217 KDGRVVAAGpKEEVL 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
422-631 |
7.56e-23 |
|
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: 99.34 E-value: 7.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQlkwiRSKIGLVS--QEPVLFTS-SI 495
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPHR----IARLGIARtfQNPRLFPElTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 496 KENI-----AYGKEN---------ATVEEIRKATELANAskFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 561
Cdd:COG0411 97 LENVlvaahARLGRGllaallrlpRARREEREARERAEE--LLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 562 ILLLDEATSAL-DAESERIVqEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:COG0411 173 LLLLDEPAAGLnPEETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
402-627 |
8.09e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 8.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 402 DIELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKI 481
Cdd:PRK11231 2 TLRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFTS-SIKENIAYG-------------KENATVEEIRKATElanaskfidklpqgLDTMVGEHGTQLSGGQK 547
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRELVAYGrspwlslwgrlsaEDNARVNQAMEQTR--------------INHLADRRLTDLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 548 QRIAVARAILKDPRILLLDEATSALD----AESERIVQEALDRimvNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS 622
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDinhqVELMRLMRELNTQ---GKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGT 221
|
....*
gi 1063718281 623 HSELL 627
Cdd:PRK11231 222 PEEVM 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1069-1271 |
8.25e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 8.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1069 IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPvLFNE--TIRA 1146
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHH-LTPEgiTVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1147 NIAYGKG---------GDATETEIVSAAElsnahgfisglQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDE 1217
Cdd:PRK11231 96 LVAYGRSpwlslwgrlSAEDNARVNQAME-----------QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1218 ATSALDAeSERVVQDALDRVMVN--RTTVVVAHRLS-TIKNADVIAVVKNGVIVEKG 1271
Cdd:PRK11231 165 PTTYLDI-NHQVELMRLMRELNTqgKTVVTVLHDLNqASRYCDHLVVLANGHVMAQG 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
394-631 |
1.10e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.70 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 394 KVLDDIRGDI--ELNNVNFSYPARPEEQI--FRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGI-- 467
Cdd:PRK13631 11 KVPNPLSDDIilRVKNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 468 ----------------NLKEFqlKWIRSKIGLVSQEP--VLFTSSIKENIAYGKENATVEEIRkATELAnaSKFIDKLpq 529
Cdd:PRK13631 91 gdkknnhelitnpyskKIKNF--KELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLA--KFYLNKM-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 530 GLD-TMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER-IVQEALDRIMVNRTTVVVAHRLSTVRN-A 606
Cdd:PRK13631 164 GLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvA 243
|
250 260
....*....|....*....|....*
gi 1063718281 607 DMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
130-360 |
1.34e-22 |
|
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: 99.48 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 130 YLGLGTLVAALLQVSG----WMIS--GERQAGRIRSLYLQTILRQDIAFFDVeTNTGEVVGRMSGDTVLIQDAMGEKVGK 203
Cdd:cd18575 38 AFLLLLAVALVLALASalrfYLVSwlGERVVADLRKAVFAHLLRLSPSFFET-TRTGEVLSRLTTDTTLIQTVVGSSLSI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 204 AIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQ 283
Cdd:cd18575 117 ALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 284 AISNYNKHLVSAYRAGVFEGASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQVL-IIIFAVLTGSmSLGQAS 360
Cdd:cd18575 197 ERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSqFVFYAVLAAG-SVGALS 273
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1068-1292 |
1.39e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.47 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1068 QIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI----KTLQLKWLRQQTGLVSQ--EPVLFN 1141
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1142 ETIRANIAYGKGGDATETEIVSaaelSNAHGFIsgLQQGYDTMVGERG-VQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1220
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDEVK----NYAHRLL--MDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1221 ALDAESERVVQDALDRVMV--NRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGKHETLINIKDgvyaSLVQLHL 1292
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDKK----KLADWHI 245
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
77-341 |
1.42e-22 |
|
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: 99.55 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGNGLGFPIMTilfGDVIDVFGQNQNSSDVsdkiakvalkfVYLGLGTLVAALLQ-----VSGWMIS-- 149
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLT---KLLIDDVIPAGDLSLL-----------LWIALLLLLLALLRallsyLRRYLAArl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 150 GERQAGRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVM 229
Cdd:cd07346 67 GQRVVFDLRRDLFRHLQRLSLSFFD-RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 230 VSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLG 309
Cdd:cd07346 146 LLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALF 225
|
250 260 270
....*....|....*....|....*....|..
gi 1063718281 310 LGTLNIVIFCTYALAVWYGGKMILEKGYTGGQ 341
Cdd:cd07346 226 SPLIGLLTALGTALVLLYGGYLVLQGSLTIGE 257
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1055-1269 |
1.56e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.99 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1055 RHISFKYPS------RPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKW 1125
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 LRQQTGLVSQEPV-LFN--ETIRANIA----YGKGGDATETEiVSAAELSNAHGFISGLQQgydtmvgERGVQLSGGQKQ 1198
Cdd:PRK10419 87 FRRDIQMVFQDSIsAVNprKTVREIIReplrHLLSLDKAERL-ARASEMLRAVDLDDSVLD-------KRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1199 RVAIARAIVKDPKVLLLDEATSALDaeseRVVQ----DALDRVMVNRTT--VVVAHRLSTIKN-ADVIAVVKNGVIVE 1269
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLD----LVLQagviRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1052-1271 |
1.84e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.54 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISfKYPSRpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwlRQQTG 1131
Cdd:PRK10851 3 IEIANIK-KSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANIAYGkggdateTEIVSAAELSNAHGFISGLQQGYDtMV-----GER-GVQLSGGQKQRVAIAR 1204
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFG-------LTVLPRRERPNAAAIKAKVTQLLE-MVqlahlADRyPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAEservVQDALDRVM------VNRTTVVVAH-RLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQ----VRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1052-1278 |
1.98e-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: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL-------QLK 1124
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpsrelakRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQTGLVSQepvLfneTIRANIAYGK----GGDATE--TEIVSAA----ELSN-AHGFISglqqgydtmvgergvQLS 1193
Cdd:COG4604 79 ILRQENHINSR---L---TVRELVAFGRfpysKGRLTAedREIIDEAiaylDLEDlADRYLD---------------ELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1194 GGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvMV---NRTTVVVAHRLstikN-----ADVIAVVKNG 1265
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRR-LAdelGKTVVIVLHDI----NfascyADHIVAMKDG 212
|
250
....*....|...
gi 1063718281 1266 VIVEKGKHETLIN 1278
Cdd:COG4604 213 RVVAQGTPEEIIT 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1070-1245 |
2.37e-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: 97.12 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1070 FQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLD----GVEIKTL---QLKWLRQQT-GLVSQ------ 1135
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQAsprEILALRRRTiGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1136 ---------EPVLfnetiraniaygKGGDATETEIVSAAELsnahgfISGLQqgydtmVGERGVQL-----SGGQKQRVA 1201
Cdd:COG4778 107 rvsaldvvaEPLL------------ERGVDREEARARAREL------LARLN------LPERLWDLppatfSGGEQQRVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063718281 1202 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVV 1245
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
403-621 |
3.43e-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: 96.28 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSY-PARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwIRSKI 481
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFTS-SIKENIAYgkeNATVEEIRKATELANASKFIDKLPQG--LDTMVGEhgtqLSGGQKQRIAVARAILK 558
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEY---FAGLYGLKGDELTARLEELADRLGMEelLDRRVGG----FSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 559 DPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKG 621
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1052-1271 |
3.72e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 95.70 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP---DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALL--QRFYDPDSGQITLDGveiKTLQLKWL 1126
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 RQQTGLVSQEPVLF-NETIRANIAYgkggdateteivsAAELsnahgfisglqqgydtmvgeRGvqLSGGQKQRVAIARA 1205
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTVRETLMF-------------AAKL--------------------RG--LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESERVVQDALDR-VMVNRTTVVVAHRLST--IKNADVIAVVKNGVIVEKG 1271
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1052-1271 |
3.92e-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: 96.28 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKY-PSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwLRQQT 1130
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLFNE-TIRANIAY-----GKGGDATETEIVSAAELSNAHGFISglqqgydtmvgERGVQLSGGQKQRVAIAR 1204
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfaglyGLKGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1054-1226 |
4.35e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1054 LRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLD-GVEIktlqlkwlrqqtGL 1132
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRI------------GY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1133 VSQEPVLF-NETIRANIAYGKGG---------------DATETEIVSAAEL-------------SNAHGFISGL---QQG 1180
Cdd:COG0488 66 LPQEPPLDdDLTVLDTVLDGDAElraleaeleeleaklAEPDEDLERLAELqeefealggweaeARAEEILSGLgfpEED 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063718281 1181 YDTMVGErgvqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES 1226
Cdd:COG0488 146 LDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1072-1286 |
4.64e-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: 99.42 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1072 DLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI----KTLQLKWLRQQTGLVSQEPVLFNE-TIRA 1146
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1147 NIAYG-KGGDATETEIVSAAelsnahgFISGLqqGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAE 1225
Cdd:TIGR02142 95 NLRYGmKRARPSERRISFER-------VIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1226 SERVVQDALDRVM--VNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLINIKDGVYAS 1286
Cdd:TIGR02142 166 RKYEILPYLERLHaeFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1050-1271 |
4.87e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.77 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDIELRHISFKYPSRP--DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI-----KTLQ 1122
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 LKWLRQQTGLVSQEP--VLFNETIRANIAYGK---GGDATET-----EIVSAAELSNAHgfisglqqgydtmVGERGVQL 1192
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPvnlGENKQEAykkvpELLKLVQLPEDY-------------VKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1193 SGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN--RTTVVVAHRLSTI-KNADVIAVVKNGVIVE 1269
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
|
..
gi 1063718281 1270 KG 1271
Cdd:PRK13645 232 IG 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1056-1276 |
4.90e-22 |
|
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: 101.68 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1056 HISFKYPSRpDVQIFQDLCLSIRAGKTIALVGESGSGKS----TVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQ--- 1128
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 -QTGLVSQEPV-----LFneTIRANIA------YGKGGDATETEIVsaaELsnahgfisgLQQgydtmVG----ERGV-- 1190
Cdd:COG4172 92 nRIAMIFQEPMtslnpLH--TIGKQIAevlrlhRGLSGAAARARAL---EL---------LER-----VGipdpERRLda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1191 ---QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAeserVVQ----DALDRvMVNRTTVVVA---HRLSTIKN-ADVI 1259
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKD-LQRELGMALLlitHDLGVVRRfADRV 227
|
250
....*....|....*..
gi 1063718281 1260 AVVKNGVIVEKGKHETL 1276
Cdd:COG4172 228 AVMRQGEIVEQGPTAEL 244
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
766-987 |
5.86e-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: 97.77 E-value: 5.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 766 KSDTRF-WAIIFM-LLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETEnsSGAIGARLSADAATVR 843
Cdd:cd18784 30 KSQDKFsRAIIIMgLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVK--TGDITSRLTSDTTTMS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 844 GLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRT 923
Cdd:cd18784 108 DTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRT 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 924 VASFCAEEKVMKMYKKKCEGPMRTGIRQGIV-SGIGFGVSFFVLfSSYAASFYAGARLVDDGKTT 987
Cdd:cd18784 188 VRSFANEDGEANRYSEKLKDTYKLKIKEALAyGGYVWSNELTEL-ALTVSTLYYGGHLVITGQIS 251
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1084-1226 |
6.19e-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: 99.02 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1084 ALVGESGSGKSTV---IALLQRfydPDSGQITLDGveiKTLQ----LKWL---RQQTGLVSQEPVLFNE-TIRANIAYG- 1151
Cdd:COG4148 29 ALFGPSGSGKTTLlraIAGLER---PDSGRIRLGG---EVLQdsarGIFLpphRRRIGYVFQEARLFPHlSVRGNLLYGr 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1152 --KGGDATETEIVSAAELSNahgfISGLQqgydtmvgERGV-QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES 1226
Cdd:COG4148 103 krAPRAERRISFDEVVELLG----IGHLL--------DRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
405-617 |
6.37e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.67 E-value: 6.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 405 LNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfqlkwIRSKIGLV 484
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 485 SQEPVLFT-SSIKENIAYGKENATVEEIRKATELAnaskfidklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRIL 563
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 564 LLDEATSALDAESeRI-VQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKI 617
Cdd:PRK11247 156 LLDEPLGALDALT-RIeMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1071-1278 |
6.76e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 6.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQ----QTGLVSQEPVLF-NETIR 1145
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1146 ANIAYGkggdateTEIVSAAELSNAHGFISGLQQ-GYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDA 1224
Cdd:PRK10070 125 DNTAFG-------MELAGINAEERREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1225 ESERVVQDALDRVMV--NRTTVVVAHRL-STIKNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK10070 198 LIRTEMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
403-587 |
7.26e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGInlkefQLKWIRSKIG 482
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQ-EPVLFTSSIKENIAYGKENATVEeirKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 561
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQLAGVE---KMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180
....*....|....*....|....*.
gi 1063718281 562 ILLLDEATSALDAESERIVQEALDRI 587
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1052-1278 |
9.21e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.42 E-value: 9.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKY---PSRPDvqifqdlcLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEiktlqlkwlrQ 1128
Cdd:PRK10771 2 LKLTDITWLYhhlPMRFD--------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----------H 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPV--LFNE-------TIRANIAYG-----KGGDATETEIVSAAElsnahgfisglQQGYDTMVGERGVQLSG 1194
Cdd:PRK10771 64 TTTPPSRRPVsmLFQEnnlfshlTVAQNIGLGlnpglKLNAAQREKLHAIAR-----------QMGIEDLLARLPGQLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTVVVAHRLStikNADVIA----VVKNGVIV 1268
Cdd:PRK10771 133 GQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLE---DAARIAprslVVADGRIA 209
|
250
....*....|
gi 1063718281 1269 EKGKHETLIN 1278
Cdd:PRK10771 210 WDGPTDELLS 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1065-1265 |
9.82e-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: 95.09 E-value: 9.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1065 PDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQI----TLDGVEIKTLQLKWLRQQTGLVSQEPVLF 1140
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1141 NETIRANIAYGKGGDATETEIVSAAelSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1220
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDA--CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063718281 1221 ALDAE-SERVVQDALDRVMVN--RTTVVVAHRLSTIKNADVIAVVKNG 1265
Cdd:cd03290 170 ALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1052-1237 |
9.85e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.31 E-value: 9.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQlkwlrQQTG 1131
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQ-EPVLFNETIRANIAYGK--GGDATETEIVSAAELSNAHGFisglqQGYdtmvGERGV-QLSGGQKQRVAIARAIV 1207
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLqlAGVEKMQRLEIAHQMLKKVGL-----EGA----EKRYIwQLSGGQRQRVGIARALA 144
|
170 180 190
....*....|....*....|....*....|
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRV 1237
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
102-359 |
1.07e-21 |
|
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: 97.00 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 102 GDVIDVFGQNQNSsdvsDKIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAGRIRSLYLQTILRQDIAFFDvETNTGE 181
Cdd:cd18784 20 GQVIDGIVIEKSQ----DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD-TVKTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 182 VVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKA 261
Cdd:cd18784 95 ITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 262 AVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYR-----AGVFEGASTGLGLGTLNIVIfctyaLAVWYGGKMILEKG 336
Cdd:cd18784 175 NEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKlkikeALAYGGYVWSNELTELALTV-----STLYYGGHLVITGQ 249
|
250 260
....*....|....*....|....
gi 1063718281 337 YTGGQ-VLIIIFavltgSMSLGQA 359
Cdd:cd18784 250 ISGGNlISFILY-----QLELGSC 268
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
403-621 |
1.08e-21 |
|
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: 94.59 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfqLKWIRSKIG 482
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFtssikeniaygkENATVEE--IRKATELANASKFIDKLpqgLDtMVGEHGT------QLSGGQKQRIAVAR 554
Cdd:cd03268 76 ALIEAPGFY------------PNLTAREnlRLLARLLGIRKKRIDEV---LD-VVGLKDSakkkvkGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKG 621
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1052-1269 |
1.23e-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: 96.03 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPS------RPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---Q 1122
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 LKWLRQQTGLVSQE-PVLFN--ETIRANIA----YGKGGDATETEiVSAAELSNAHGFISGLQQGYDTmvgergvQLSGG 1195
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNprMTVRQIIGeplrHLTSLDESEQK-ARIAELLDMVGLRSEDADKLPR-------QLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1196 QKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTT--VVVAHRLSTIKN-ADVIAVVKNGVIVE 1269
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
730-1001 |
1.61e-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: 96.34 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIKAFF--KPPEQLKsdtrFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRS 807
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFveKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 808 MCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGL 887
Cdd:cd18552 77 DLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 888 NGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEG----PMRTGIRQGIVSGI-----G 958
Cdd:cd18552 155 PIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERlrrlSMKIARARALSSPLmellgA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063718281 959 FGVSFFVLFssyaasfyaGARLVDDGKTTFDSVFRVFFALTMA 1001
Cdd:cd18552 235 IAIALVLWY---------GGYQVISGELTPGEFISFITALLLL 268
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1034-1269 |
1.72e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1034 KIDPSDESGRVLdnvkgdIELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITL 1113
Cdd:COG0488 304 RFPPPERLGKKV------LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1114 -DGVEIktlqlkwlrqqtGLVSQEPVLFNE--TIRANIAYGkGGDATETEIVSAAElsnAHGFiSGLQQgyDTMVGErgv 1190
Cdd:COG0488 375 gETVKI------------GYFDQHQEELDPdkTVLDELRDG-APGGTEQEVRGYLG---RFLF-SGDDA--FKPVGV--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1191 qLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDR----VmvnrttVVVAH-R--LSTIknADVIAVVK 1263
Cdd:COG0488 433 -LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV--ATRILEFE 503
|
....*.
gi 1063718281 1264 NGVIVE 1269
Cdd:COG0488 504 DGGVRE 509
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
411-607 |
1.86e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 411 SYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefqlkwiRSKIGLVSQ---E 487
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 488 PVLFTSSIKENIAYGK-------------ENATVEEIRKA---TELANASkfidklpqgLDTmvgehgtqLSGGQKQRIA 551
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwarrglwrrltrdDRAAVDDALERvglADLAGRQ---------LGE--------LSGGQRQRAL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 552 VARAILKDPRILLLDEATSALDAESERIVQEALDRIMV-NRTTVVVAHRLSTVRNAD 607
Cdd:NF040873 130 LAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRAD 186
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
403-618 |
1.95e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.57 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF------QLK 475
Cdd:PRK10535 5 LELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalaQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 476 wiRSKIGLVSQEPVLFTS-SIKENIAYGKENATVEeirKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVAR 554
Cdd:PRK10535 85 --REHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRIMVN-RTTVVVAHRLSTVRNADMIAVIHQGKIV 618
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1052-1271 |
1.98e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:COG4559 2 LEAENLSVRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVL-FNETIRANIAYGK----GGDATETEIVSAA-ELSNAHGFisglqqgydtmvGERGVQ-LSGGQKQRVAIAR 1204
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVALGRaphgSSAAQDRQIVREAlALVGLAHL------------AGRSYQtLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1205 AIV-------KDPKVLLLDEATSALD-AESERVVQdaLDRVMVNRTTVVVA--HRLstikN-----ADVIAVVKNGVIVE 1269
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDlAHQHAVLR--LARQLARRGGGVVAvlHDL----NlaaqyADRILLLHQGRLVA 220
|
..
gi 1063718281 1270 KG 1271
Cdd:COG4559 221 QG 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1052-1279 |
2.14e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.05 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKY-PSRP-DVQIFQDLCLSIRAGKTIALVGESGSGKSTviaLLQRF---YDPDSGQITLDGVEIkTLQ---- 1122
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKST---LMQHFnalLKPSSGTITIAGYHI-TPEtgnk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 -LKWLRQQTGLVSQ--EPVLFNETIRANIAYG-KGGDATETEIVSAAelsnahgfISGLQQ-GYDTMVGERG-VQLSGGQ 1196
Cdd:PRK13641 79 nLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDEAKEKA--------LKWLKKvGLSEDLISKSpFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSALDAES-ERVVQDALDRVMVNRTTVVVAHRLSTI-KNADVIAVVKNGVIVekgKHE 1274
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLI---KHA 227
|
....*
gi 1063718281 1275 TLINI 1279
Cdd:PRK13641 228 SPKEI 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
417-636 |
3.03e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKS-TVVSLIERFYDPQ----SGEVRIDGINL---KEFQLKWIR-SKIGLVSQE 487
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 488 PVLFTS---SIKENIA--------YGKENATVEEIR--KATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVAR 554
Cdd:PRK15134 101 PMVSLNplhTLEKQLYevlslhrgMRREAARGEILNclDRVGIRQAAKRLTDYPH-----------QLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAESE-RIVQ--EALDRIMvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQaQILQllRELQQEL-NMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAP 248
|
....*.
gi 1063718281 631 EGAYSQ 636
Cdd:PRK15134 249 THPYTQ 254
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
421-595 |
3.75e-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: 93.65 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRID----GINL---KEFQLKWIRSK-IGLVSQ------ 486
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLaqaSPREILALRRRtIGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 487 ---------EPVLftssikeniAYGKENATVEEirKATELanaskfidklpqgLDTM-VGEHGTQL-----SGGQKQRIA 551
Cdd:COG4778 107 rvsaldvvaEPLL---------ERGVDREEARA--RAREL-------------LARLnLPERLWDLppatfSGGEQQRVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063718281 552 VARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVV 595
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
403-621 |
4.03e-21 |
|
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: 93.11 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLKwIRSKIG 482
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIA-ARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAYGKE--NATVEEIRK-ATELANASKFIDKLPQGLDtmvgehgtQLSGGQKQRIAVARAILK 558
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYLAQlkGLKKEEARRrIDEWLERLELSEYANKRVE--------ELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 559 DPRILLLDEATSALDAESERIVQEALDRIMVNRTTVV-VAHRLSTV-RNADMIAVIHQGKIVEKG 621
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
735-1005 |
4.26e-21 |
|
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: 95.24 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 735 IAAVLNGVILPIFGILISSVIKAFFKPPEQLKSDTRFWAIIFM--LLGVASmvvfPAQTIFFSIAGCKLVQRIRSMCFEK 812
Cdd:cd18575 3 IALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAValVLALAS----ALRFYLVSWLGERVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 813 VVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYIY 892
Cdd:cd18575 79 LLRLSPSFFETT--RTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 893 MKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAA 972
Cdd:cd18575 157 GRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260 270
....*....|....*....|....*....|....*
gi 1063718281 973 SFYAGARLVDDGKTTFD--SVFrVFFALtMAAVAI 1005
Cdd:cd18575 237 VLWLGAHDVLAGRMSAGelSQF-VFYAV-LAAGSV 269
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
403-640 |
6.86e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEqiFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--INLKEFQLKWIRSK 480
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEP--VLFTSSIKENIAYGKENATV--EEIRKATELANASKfidklpqGLDTMVGEHGTQLSGGQKQRIAVARAI 556
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRT-------GIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 557 LKDPRILLLDEATSALD----AESERIVQEALDRIMVnrTTVVVAHRLSTVR-NADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGL--TIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
....*....
gi 1063718281 632 GAYSQLIRL 640
Cdd:PRK13636 235 MLRKVNLRL 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
375-629 |
7.87e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 375 KMFEAIKR--------KPEID--ASDTTGKVLddirgdIELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGK 444
Cdd:COG0488 284 KALEKLEReepprrdkTVEIRfpPPERLGKKV------LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 445 STVVSLIERFYDPQSGEVRIdGINLkefqlkwirsKIGLVSQEPVLFTS--SIKENIAYGKENATVEEIRKAteLAN--- 519
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGY--LGRflf 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 520 ----ASKFIDKlpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRImvNRTTVV 595
Cdd:COG0488 422 sgddAFKPVGV---------------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLL 484
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063718281 596 VAH-R--LSTVrnADMIAVIHQGKIVEK-GSHSELLRD 629
Cdd:COG0488 485 VSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
403-630 |
8.15e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.22 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVlFTS--SIKENIAYG-----KENATVEE---IRKA------TELANasKFIDklpqgldtmvgehgtQLSGGQ 546
Cdd:COG4604 79 ILRQENH-INSrlTVRELVAFGrfpysKGRLTAEDreiIDEAiayldlEDLAD--RYLD---------------ELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 547 KQRIAVARAILKDPRILLLDEATSALDAESERIVQEALdRIMV---NRTTVVVAHRLstvrN-----ADMIAVIHQGKIV 618
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLL-RRLAdelGKTVVIVLHDI----NfascyADHIVAMKDGRVV 215
|
250
....*....|..
gi 1063718281 619 EKGSHSELLRDP 630
Cdd:COG4604 216 AQGTPEEIITPE 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1071-1269 |
1.06e-20 |
|
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: 92.50 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwLRQQTGLVS--QEPVLFNE-TIRAN 1147
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1148 I---AYGKGGDAT--------ETEIVSAAElsNAHGFIsGLQQGYDTMVGErgvqLSGGQKQRVAIARAIVKDPKVLLLD 1216
Cdd:cd03219 96 VmvaAQARTGSGLllararreEREARERAE--ELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1217 EATSAL-DAESERVVqDALDRVMV-NRTTVVVAHRLSTIKN-ADVIAVVKNG-VIVE 1269
Cdd:cd03219 169 EPAAGLnPEETEELA-ELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGrVIAE 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1050-1280 |
1.32e-20 |
|
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: 93.38 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDIELRHISFKYPSRPDVqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDsGQITLDGVEIKTLQLKWLRQQ 1129
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLFNETIRANI-AYGKGGDateTEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVK 1208
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1209 DPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIK 1280
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
398-636 |
1.48e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.62 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 398 DIRGDIELNNVNFSY-PARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG---------- 466
Cdd:PRK10261 8 DARDVLAVENLNIAFmQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 467 INLKEF---QLKWIR-SKIGLVSQEPVlftSSIKENIAYGKENAtvEEIR------KATELANASKFID--KLPQGlDTM 534
Cdd:PRK10261 88 IELSEQsaaQMRHVRgADMAMIFQEPM---TSLNPVFTVGEQIA--ESIRlhqgasREEAMVEAKRMLDqvRIPEA-QTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 535 VGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE-RIVQ--EALDRIMvNRTTVVVAHRLSTVRN-ADMIA 610
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQliKVLQKEM-SMGVIFITHDMGVVAEiADRVL 240
|
250 260
....*....|....*....|....*.
gi 1063718281 611 VIHQGKIVEKGSHSELLRDPEGAYSQ 636
Cdd:PRK10261 241 VMYQGEAVETGSVEQIFHAPQHPYTR 266
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1052-1278 |
1.54e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.51 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTlQLKWLRQQTG 1131
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRAN-IAYGK--GGDATETEIVSAAELSNAHgfisgLQQGYDTMVGErgvqLSGGQKQRVAIARAIV 1207
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENlLVFGRyfGMSTREIEAVIPSLLEFAR-----LESKADARVSD----LSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVV-------AHRLstiknADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
99-360 |
1.96e-20 |
|
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: 93.38 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 99 ILFGDVIDVFGQNQNSSDVS--DKIAKVALK--FVYLGLGTLVAALLqvsgWMIS--GERQAGRIRSLYLQTILRQDIAF 172
Cdd:cd18574 17 LLLGDLVNVISRSLKETNGDfiEDLKKPALKllGLYLLQSLLTFAYI----SLLSvvGERVAARLRNDLFSSLLRQDIAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 173 FDvETNTGEVVGRMSGDtvlIQD--------------AMGEKVGKAIQLvstfiggFVIAFTegwlLTLVMVSSIPLLVM 238
Cdd:cd18574 93 FD-THRTGELVNRLTAD---VQEfkssfkqcvsqglrSVTQTVGCVVSL-------YLISPK----LTLLLLVIVPVVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 239 SGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHL--------VSAYRAGVFEGAST---- 306
Cdd:cd18574 158 VGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVekaaklneKLGLGIGIFQGLSNlaln 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 307 GLGLGTLnivifctyalavWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQAS 360
Cdd:cd18574 238 GIVLGVL------------YYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLS 279
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1071-1265 |
2.28e-20 |
|
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: 91.37 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIktlqlkwlrQQTG----LVSQEPVLFN-ETIR 1145
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---------TEPGpdrmVVFQNYSLLPwLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1146 ANIAYGKGG---DATETEivsAAELSNAHGFISGLQQGYDtmvgERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSAL 1222
Cdd:TIGR01184 73 ENIALAVDRvlpDLSKSE---RRAIVEEHIALVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063718281 1223 DAESERVVQDALDRVMV-NRTTVV-VAHRL-STIKNADVIAVVKNG 1265
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEeHRVTVLmVTHDVdEALLLSDRVVMLTNG 191
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1052-1291 |
2.36e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.21 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKY------PSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKW 1125
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 LRQQTGLVSQEPvlfNETIRANIAYGKGGDA-----TEteiVSAAE-------------LSNAHGFIsglqqgYDTMvge 1187
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGQILEEplrlnTD---LTAEEreerifatlrlvgLLPEHANF------YPHM--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1188 rgvqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAeSERvVQdaldrvMVNR----------TTVVVAHRLSTIKN-A 1256
Cdd:COG4167 150 ----LSSGQKQRVALARALILQPKIIIADEALAALDM-SVR-SQ------IINLmlelqeklgiSYIYVSQHLGIVKHiS 217
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063718281 1257 DVIAVVKNGVIVEKGK-HETLINIKDGVYASLVQLH 1291
Cdd:COG4167 218 DKVLVMHQGEVVEYGKtAEVFANPQHEVTKRLIESH 253
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
422-626 |
2.56e-20 |
|
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: 90.89 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN-LKEfqLKWIRSKIGLVSQEPVL---FTSsiKE 497
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVRE--PREVRRRIGIVFQDLSVddeLTG--WE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 498 NIA-----YGKENAT----VEEIRKATELANASkfidklpqglDTMVGEHgtqlSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:cd03265 93 NLYiharlYGVPGAErrerIDELLDFVGLLEAA----------DRLVKTY----SGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 569 TSALDAESERIVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSEL 626
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
421-637 |
2.63e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.91 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--------INLKEFQLKWI-RSKIGLVSQEP--- 488
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlYALSEAERRRLlRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 489 VLFTSSIKENIA----------YGKENATVEEIRKATELANASkfIDKLPqgldtmvgehgTQLSGGQKQRIAVARAILK 558
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYGDIRATAGDWLERVEIDAAR--IDDLP-----------TTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 559 DPRILLLDEATSALDAEseriVQ-EALD--RIMVNR---TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVS----VQaRLLDllRGLVRElglAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
....*.
gi 1063718281 632 GAYSQL 637
Cdd:PRK11701 245 HPYTQL 250
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
429-641 |
2.75e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.17 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 429 SSGSTvALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL----KEFQLKWIRSKIGLVSQEPVLFTS-SIKENIAYGK 503
Cdd:PRK11144 23 AQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 504 ENATVEEIRKATELANASKFIDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEA 583
Cdd:PRK11144 102 AKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 584 LDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS-----HSELLRD--PEGAYSQLIRLQ 641
Cdd:PRK11144 171 LERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPleevwASSAMRPwlPKEEQSSILKVT 238
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
731-987 |
3.70e-20 |
|
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: 92.49 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 731 ILGSIAAVLNGVILP-IFGILISSVIKAFFKppeqlksdTRFWAIIFMLLGVA---SMVVFpAQTIFFSIAGCKLVQRIR 806
Cdd:cd18542 5 ILALLLATALNLLIPlLIRRIIDSVIGGGLR--------ELLWLLALLILGVAllrGVFRY-LQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 807 SMCFEKVVRMEVGWFDETEnsSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIG 886
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKAR--TGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 887 LNGYIYMKFMvgfsadaKRMYEEASQ-------VANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGF 959
Cdd:cd18542 154 LFSYVFFKKV-------RPAFEEIREqegelntVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYW 226
|
250 260
....*....|....*....|....*...
gi 1063718281 960 GVSFFVLFSSYAASFYAGARLVDDGKTT 987
Cdd:cd18542 227 PLMDFLSGLQIVLVLWVGGYLVINGEIT 254
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
403-623 |
3.82e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfQLKWIRSKIG 482
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVL---FTssIKEN-IAYGK----ENATVEE-IRKATELAnaskfidKLPQGLDTMVGEhgtqLSGGQKQRIAVA 553
Cdd:PRK13536 118 VVPQFDNLdleFT--VRENlLVFGRyfgmSTREIEAvIPSLLEFA-------RLESKADARVSD----LSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 554 RAILKDPRILLLDEATSALDAESERIVQEALDRIMV-NRTTVVVAHRLSTV-RNADMIAVIHQG-KIVEKGSH 623
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPH 257
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
400-631 |
3.93e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.17 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 400 RGDIE-LNNVNFSYPARpeeqifrgfslsissgSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIR 478
Cdd:PRK13652 14 SGSKEaLNNINFIAPRN----------------SRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEP--VLFTSSIKENIAYGKENATVEEIRKATELANASKFIdklpqGLDTMVGEHGTQLSGGQKQRIAVARAI 556
Cdd:PRK13652 78 KFVGLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 557 LKDPRILLLDEATSALDAESERIVQEALDRIMVN--RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
405-630 |
3.98e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.77 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 405 LNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLV 484
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 485 SQE-PVLFTSSIKENIAYGK----------ENATVEEIRKATELANASKFIDKLpqgLDTmvgehgtqLSGGQKQRIAVA 553
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 554 RAILKDPRILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1052-1271 |
4.40e-20 |
|
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: 89.97 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWlrQQTG 1131
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANI-AYGKGGDATETEIVSAAElsnahgfISGLQQGYDTMVGergvQLSGGQKQRVAIARAIVKD 1209
Cdd:cd03268 76 ALIEAPGFYPNlTARENLrLLARLLGIRKKRIDEVLD-------VVGLKDSAKKKVK----GFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1210 PKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTI-KNADVIAVVKNGVIVEKG 1271
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1052-1278 |
5.15e-20 |
|
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: 90.19 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQL-KWLRQQT 1130
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLFNE-TIRANI---AYGKGGDATETEIVSAAELsnahgFiSGLQQGYDTMVGergvQLSGGQKQRVAIARAI 1206
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLllgAYARRRAKRKARLERVYEL-----F-PRLKERRKQLAG----TLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1207 VKDPKVLLLDEATSALdaeSERVVQDALDRVM-VNR--TTVVV----AHRLSTIknADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:cd03224 148 MSRPKLLLLDEPSEGL---APKIVEEIFEAIReLRDegVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
425-618 |
5.23e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLK----WIRSKIGLVSQEPVLFTS-SIKENI 499
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRsprdAIALGIGMVHQHFMLVPNlTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 500 AYGKENATV------EEIRKATELANASKF-IDklpqgLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSAL 572
Cdd:COG3845 102 VLGLEPTKGgrldrkAARARIRELSERYGLdVD-----PDAKVE----DLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063718281 573 -DAESERiVQEALDRIMVNRTTVV-VAHRLSTVR-NADMIAVIHQGKIV 618
Cdd:COG3845 173 tPQEADE-LFEILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
404-629 |
5.41e-20 |
|
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: 90.28 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLkwIRSK 480
Cdd:TIGR03410 2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHER--ARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENIAYGKENatveeirkateLANASKFIDK----LPQGLDTMVGEHGTQLSGGQKQRIAVARA 555
Cdd:TIGR03410 77 IAYVPQGREIFPRlTVEENLLTGLAA-----------LPRRSRKIPDeiyeLFPVLKEMLGRRGGDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 556 ILKDPRILLLDEATSALDAEserIVQE---ALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPS---IIKDigrVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDED 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1069-1266 |
6.22e-20 |
|
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: 96.90 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1069 IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveiktlqlkwlrqQTGLVSQEPVLFNETIRANI 1148
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1149 AYGKGGDATE-TEIVSAAELSNAhgfISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE 1227
Cdd:TIGR01271 508 IFGLSYDEYRyTSVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063718281 1228 R-VVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGV 1266
Cdd:TIGR01271 585 KeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1052-1271 |
6.77e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.31 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEP--VLFNETIRANIAYG--KGGDATETEIVSAAELSNAHGFISglqqgYDTMVGERgvqLSGGQKQRVAIARAIV 1207
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGmeNQGIPREEMIKRVDEALLAVNMLD-----FKTREPAR---LSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1208 KDPKVLLLDEATSALD----AESERVVQDALDRVMVnrTTVVVAHRLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1061-1257 |
8.27e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 8.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1061 YPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveikTLQLKWLRQQTGLVSQEPVlf 1140
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1141 neTIRANIAYGKGG--------DATETEIVSAAelsnahgfisgLQQ-GYDTMVGERGVQLSGGQKQRVAIARAIVKDPK 1211
Cdd:NF040873 73 --TVRDLVAMGRWArrglwrrlTRDDRAAVDDA-----------LERvGLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDR-VMVNRTTVVVAHRLSTIKNAD 1257
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRAD 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1056-1271 |
8.42e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1056 HISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGV------EIKTLQLKWLRQQ 1129
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLFNE-TIRANIAY--GKGGDATETEIVSAAELSNAHgfiSGLQQGYDTMVGERGVQLSGGQKQRVAIARAI 1206
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYplKSHGIKEKREIKKIVEECLRK---VGLWKEVYDRLNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1207 VKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKG 1271
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWG 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1052-1278 |
8.96e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 8.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL-QLKWLRQQT 1130
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEP--VLFNETIRANIAYGKggdatETEIVSAAELsnahgfisglQQGYDTMVGERGVQ---------LSGGQKQR 1199
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGP-----ENLCLPPIEI----------RKRVDRALAEIGLEkyrhrspktLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1200 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN-RTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1076-1278 |
1.07e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.95 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1076 SIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIK---TLQLKWLRQQTGLVSQEPvlfnetiraniaYG- 1151
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP------------YGs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1152 -----KGGDATE------TEIVSAAELSNAHGFIS--GLQ----QGYDTMvgergvqLSGGQKQRVAIARAIVKDPKVLL 1214
Cdd:PRK11308 105 lnprkKVGQILEepllinTSLSAAERREKALAMMAkvGLRpehyDRYPHM-------FSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1215 LDEATSALDAESERVVqdaLDRVM-----VNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK11308 178 ADEPVSALDVSVQAQV---LNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
422-598 |
1.10e-19 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 89.45 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKE--------FQ----LKWIRskiglVSQEPV 489
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrmvvFQnyslLPWLT-----VRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 490 LFTSSIKENIAYGKENATVEEirkATELANASKFIDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDEAT 569
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEE---HIALVGLTEAADKRP-----------GQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190
....*....|....*....|....*....|.
gi 1063718281 570 SALDAESERIVQEALDRIMV-NRTTVV-VAH 598
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEeHRVTVLmVTH 173
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
401-633 |
1.19e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.54 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDIELNNVNFSYPARpeeqifrgfslsissgSTVALVGQSGSGKSTVVSLIERFYDP-----QSGEVRIDGINLKEFQ-L 474
Cdd:PRK14271 33 GKTVLDQVSMGFPAR----------------AVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 475 KWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVAR 554
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELLRDPEGA 633
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1063-1274 |
1.23e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1063 SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVL-FN 1141
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1142 ETIRANIAYGK--------GGDATETEIVSAAelsnahgfisgLQQGYDTMVGERGV-QLSGGQKQRVAIARAIVKDPKV 1212
Cdd:PRK09536 92 FDVRQVVEMGRtphrsrfdTWTETDRAAVERA-----------MERTGVAQFADRPVtSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1213 LLLDEATSALDAESE-RVVQDALDRVMVNRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKGKHE 1274
Cdd:PRK09536 161 LLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPA 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1084-1272 |
1.30e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.83 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1084 ALVGESGSGKSTVIALLQRFYD--PD---SGQITLDGVEI-----KTLQLkwlRQQTGLVSQEPVLFNETIRANIAYG-- 1151
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysprtDTVDL---RKEIGMVFQQPNPFPMSIYENVVYGlr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1152 -KG-------GDATETEIVSAAELSNAHGFIsglqqgYDTMVGergvqLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:PRK14239 112 lKGikdkqvlDEAVEKSLKGASIWDEVKDRL------HDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1224 AESERVVQDALDRVMVNRTTVVVAHRL---STIknADVIAVVKNGVIVEKGK 1272
Cdd:PRK14239 181 PISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYND 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1069-1265 |
1.55e-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: 90.30 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1069 IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLrqqtglvsqepvlFNETIRANI 1148
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWI-------------MPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1149 AYGKGGDATE-TEIVSAAELSNAhgfISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE 1227
Cdd:cd03291 119 IFGVSYDEYRyKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063718281 1228 R-VVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNG 1265
Cdd:cd03291 196 KeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
403-640 |
1.87e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARP--------EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQsGEVRIDGINLKEF-- 472
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLnr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 473 -QLKWIRSKIGLVSQEPvlfTSS------IKENIAYGKE------NATVEEIRKATELANAskfidklpqGLD-TMVGEH 538
Cdd:PRK15134 355 rQLLPVRHRIQVVFQDP---NSSlnprlnVLQIIEEGLRvhqptlSAAQREQQVIAVMEEV---------GLDpETRHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 539 GTQLSGGQKQRIAVARAILKDPRILLLDEATSALDaeseRIVQE---ALDRIMVNR---TTVVVAHRLSTVRN-ADMIAV 611
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIV 498
|
250 260 270
....*....|....*....|....*....|
gi 1063718281 612 IHQGKIVEKGSHSELLRDPEGAYS-QLIRL 640
Cdd:PRK15134 499 LRQGEVVEQGDCERVFAAPQQEYTrQLLAL 528
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
403-631 |
2.42e-19 |
|
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: 88.37 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQL-KWIRSKI 481
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFTS-SIKENIAYGKENATVEEIRKATELANaskFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 560
Cdd:cd03218 78 GYLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEE---LLEEF--HITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 561 RILLLDEATSALD----AESERIVQEALDR---IMVN----RTTVVVAHRlstvrnadmIAVIHQGKIVEKGSHSELLRD 629
Cdd:cd03218 153 KFLLLDEPFAGVDpiavQDIQKIIKILKDRgigVLITdhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAAN 223
|
..
gi 1063718281 630 PE 631
Cdd:cd03218 224 EL 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1052-1293 |
2.83e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.99 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFkYPSRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPD----SGQITLDGVEIKTLQLKwlR 1127
Cdd:PRK10418 5 IELRNIAL-QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALR--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 QQTGLVSQEP-VLFN--ETIRAN-----IAYGK-GGDATETEIVSAAELSNAHgfisglqqgydTMVGERGVQLSGGQKQ 1198
Cdd:PRK10418 79 RKIATIMQNPrSAFNplHTMHTHaretcLALGKpADDATLTAALEAVGLENAA-----------RVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1199 RVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRT--TVVVAHRLSTI-KNADVIAVVKNGVIVEKGKHET 1275
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVET 227
|
250
....*....|....*....
gi 1063718281 1276 LINI-KDGVYASLVQLHLS 1293
Cdd:PRK10418 228 LFNApKHAVTRSLVSAHLA 246
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
403-616 |
3.06e-19 |
|
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: 85.58 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefqlkwiRSKIG 482
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQepvlftssikeniaygkenatveeirkatelanaskfidklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 562
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 563 LLLDEATSALDAESERIVQEALDRImvNRTTVVVAH-R--LSTVrnADMIAVIHQGK 616
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
403-629 |
3.16e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.78 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLKwIRSKIG 482
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPE-DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS-SIKENIAY-----GkenatveeIRKATELANASKFIDKLpqGLdtmvGEHGT----QLSGGQKQRIAV 552
Cdd:COG4152 75 YLPEERGLYPKmKVGEQLVYlarlkG--------LSKAEAKRRADEWLERL--GL----GDRANkkveELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 553 ARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1064-1224 |
3.35e-19 |
|
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: 88.10 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1064 RPDVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRFYDPDSGQITLDGVEIKTLQLK----WLRQQTGLVS-- 1134
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRKPDQFQkcvaYVRQDDILLPgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1135 --QEPVLFNETIRANIAYGKGGDATETEIVsaaelsnahgfisGLQQGYDTMVGERGVQ-LSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03234 97 tvRETLTYTAILRLPRKSSDAIRKKRVEDV-------------LLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPK 163
|
170
....*....|...
gi 1063718281 1212 VLLLDEATSALDA 1224
Cdd:cd03234 164 VLILDEPTSGLDS 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1052-1271 |
3.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKY-PSRP-DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI----KTLQLKW 1125
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 LRQQTGLVSQEP--VLFNETIRANIAYGK---GGDATETEIVSAAELSnahgfISGLQQGYdtmVGERGVQLSGGQKQRV 1200
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPqnfGIPKEKAEKIAAEKLE-----MVGLADEF---WEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRV-MVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1052-1278 |
3.76e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDS-----GQITLDGVEI--KTLQLK 1124
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1125 WLRQQTGLVSQEPVLFNETIRANIAYGKG--GDATETEIVSAAE--LSNAHgfisgLQQGYDTMVGERGVQLSGGQKQRV 1200
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKivGWRPKLEIDDIVEsaLKDAD-----LWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESERVVQDALD--RVMVNRTTVVVAHRLSTIKN-ADVIAVVKN-----GVIVEKGK 1272
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGL 239
|
....*.
gi 1063718281 1273 HETLIN 1278
Cdd:PRK14258 240 TKKIFN 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1052-1250 |
5.75e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHIS--FKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQlKWLRQQ 1129
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 T-GLVSQEPVL---FNETIRAN--IAYGKGG--------DATETEIVSA--AELSNahgfisGLQQGYDTMVGergvQLS 1193
Cdd:COG1101 81 YiGRVFQDPMMgtaPSMTIEENlaLAYRRGKrrglrrglTKKRRELFREllATLGL------GLENRLDTKVG----LLS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1194 GGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVmVNR---TTVVVAHRL 1250
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNM 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1054-1272 |
7.15e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.81 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1054 LRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQItLDGveikTLQLKWLRQQTGLV 1133
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1134 SQEPVLFN-ETIRANIAYGKGGD--ATETEIVSAAELSNahgfisglqqgydtMVGERGVQLSGGQKQRVAIARAIVKDP 1210
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKGQwrDAALQALAAVGLAD--------------RANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1211 KVLLLDEATSALDAESERVVQDALDRVMVNR--TTVVVAHRLStiknaDVIAVVKNGVIVEKGK 1272
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVS-----EAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
417-627 |
7.80e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--INLKEFQLKWIRSKIGLVSQEP--VLFT 492
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 493 SSIKENIAYGKENATVEEIRKATELANASKFIDklpqgldtmvGEHGTQ-----LSGGQKQRIAVARAILKDPRILLLDE 567
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD----------AQHFRHqpiqcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 568 ATSALDAESERIVQEALDRIMVNRTTVVV-AHRLSTVRN-ADMIAVIHQGKIVEKGSHSELL 627
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1068-1278 |
9.03e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 87.72 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1068 QIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL-------------QLKWLRQQTGLVS 1134
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1135 QEPVLFNE-TIRANI--AYGKGGDATETEIVSAAELSNAHGFISGLQQGydtmvgERGVQLSGGQKQRVAIARAIVKDPK 1211
Cdd:PRK10619 99 QHFNLWSHmTVLENVmeAPIQVLGLSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1212 VLLLDEATSALDAEserVVQDALdRVMVN-----RTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK10619 173 VLLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1066-1271 |
1.14e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1066 DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYD--PD---SGQITLDGVEIKTLQLKWLRQQTGLVSQEP-VL 1139
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1140 FNETIRANIAYG-------KGGDATETEIVSAAELSNahgfisgLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKV 1212
Cdd:PRK14247 95 PNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1213 LLLDEATSALDAESERVVQDALDRVMVNRTTVVVAH------RLStiknaDVIAVVKNGVIVEKG 1271
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1280 |
1.14e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.22 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRP--DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQI------------------ 1111
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1112 TLDGVEI------KTLQLKWLRQQTGLVSQ--EPVLFNETIRANIAYGKGGDATETEivSAAELSNAHGFISGLQQGYdt 1183
Cdd:PRK13651 83 VLEKLVIqktrfkKIKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE--EAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1184 mVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN-RTTVVVAHRL-STIKNADVIAV 1261
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRTIF 237
|
250 260
....*....|....*....|
gi 1063718281 1262 VKNGVIVEKGK-HETLINIK 1280
Cdd:PRK13651 238 FKDGKIIKDGDtYDILSDNK 257
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
403-659 |
1.18e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL------KEFQLkw 476
Cdd:PRK15439 12 LCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpaKAHQL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 irsKIGLVSQEPVLFTS-SIKENIAYGKENATVEEIRKATELANASKFIDklpqgLDTMVGehgtQLSGGQKQRIAVARA 555
Cdd:PRK15439 87 ---GIYLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQLLAALGCQLD-----LDSSAG----SLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 556 ILKDPRILLLDEATSALD-AESERI---VQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDp 630
Cdd:PRK15439 155 LMRDSRILILDEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTD- 230
|
250 260
....*....|....*....|....*....
gi 1063718281 631 egaysQLIRLQEDTKQTEDSTDEQKLSME 659
Cdd:PRK15439 231 -----DIIQAITPAAREKSLSASQKLWLE 254
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
424-630 |
1.41e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.53 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 424 FSLSISSGSTVALVGQSGSGKSTVVSLIERFYdPQSGEVRIDGINLKEFQL-KWIRSKIGLVSQEPVLFTSSIKENIA-Y 501
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaELARHRAYLSQQQTPPFAMPVFQYLTlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 502 GKENATVEEIRKA-TELANASKFIDKLPQGLdtmvgehgTQLSGGQKQRIAVARAILK-DPRI------LLLDEATSALD 573
Cdd:PRK03695 94 QPDKTRTEAVASAlNEVAEALGLDDKLGRSV--------NQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 574 aeserIVQE-ALDRIMV-----NRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK03695 166 -----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1271 |
1.55e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYpsRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTG 1131
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEP--VLFNETIRANIAYGKGGDATETEIVsaaelsnAHGFISGLQQ-GYDTMVGERGVQLSGGQKQRVAIARAIVK 1208
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETV-------AHRVSSALHMlGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1209 DPKVLLLDEATSALDAESERVVQDALDRVMVN--RTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYG 220
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
77-350 |
1.70e-18 |
|
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: 87.48 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGNGLGFPIMTIlfgDVIDVFGQNQNSSdvsdkiakvalKFVYLGLGTLVAALLQ-----VSGWMIS-- 149
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLK---PLLDDIFVEKDLE-----------ALLLVPLAIIGLFLLRglasyLQTYLMAyv 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 150 GERQAGRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVM 229
Cdd:cd18552 67 GQRVVRDLRNDLFDKLLRLPLSFFD-RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 230 VSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLG 309
Cdd:cd18552 146 LVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALS 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063718281 310 LGTLNIVIFCTYALAVWYGGKMILEKGYTGGQVLIIIFAVL 350
Cdd:cd18552 226 SPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALL 266
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1075-1294 |
1.80e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLqrfydpdSGQITLDG-----VEI--KTLQ--------LKWLRQQTGLVSQEPVL 1139
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKsagshIELlgRTVQregrlardIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1140 FNE-TIRANIAYGKGGDAT--ETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLD 1216
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1217 EATSALDAESERVVQDALDRVMVNR--TTVVVAHRLS-TIKNADVIAVVKNGVIVEKGKHETLINIK-DGVYASLVQLHL 1292
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHLYRSINRVEE 257
|
..
gi 1063718281 1293 SA 1294
Cdd:PRK09984 258 NA 259
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1071-1250 |
1.98e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.76 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYD-----PDSGQITLDGVEIKTLQLK--WLRQQTGLVSQEPVLFNET 1143
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1144 IRANIAYG---KGGDATETEIVSAAeLSNAhgfisGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1220
Cdd:PRK14243 107 IYDNIAYGariNGYKGDMDELVERS-LRQA-----ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190
....*....|....*....|....*....|
gi 1063718281 1221 ALDAESERVVQDALDRVMVNRTTVVVAHRL 1250
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1054-1262 |
2.23e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1054 LRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLK-WLRQQTGL 1132
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1133 VSQEPVLFNETIRANIAYGK----GG----DATETEIVSAAelsnahgfisglqqgyDTMVG-----ERGV-QLSGGQKQ 1198
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRypwhGAlgrfGAADREKVEEA----------------ISLVGlkplaHRLVdSLSGGERQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1199 RVAIARAIVKDPKVLLLDEATSALDAESERVVqdaldrvmvnrttVVVAHRLSTIKNADVIAVV 1262
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV-------------LALVHRLSQERGLTVIAVL 205
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
403-638 |
2.28e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSypaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWIRS 479
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipaMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQEPVLFTS-SIKENIAYgkenatveEIRKATELANA---SKFIDKLPQ-GLDTMVGEHGTQLSGGQKQRIAVAR 554
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAY--------PLREHTQLPAPllhSTVMMKLEAvGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPD 236
|
....*..
gi 1063718281 632 GAYSQLI 638
Cdd:PRK11831 237 PRVRQFL 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1052-1268 |
2.32e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPS-RPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLR 1127
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 --------QQTGLVSQEPVLFNETIRANIAyGKGgdateteivSAAELSNAHGFISGLqqGYDTMVGERGVQLSGGQKQR 1199
Cdd:PRK10535 85 rehfgfifQRYHLLSHLTAAQNVEVPAVYA-GLE---------RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1200 VAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN-RTTVVVAHRLSTIKNADVIAVVKNGVIV 1268
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
402-631 |
2.41e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.55 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 402 DIELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKwiRSKI 481
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFTS-SIKENIAYGKENATVE--EIRK----ATELANASKFIDKLPQGLdtmvgehgtqlSGGQKQRIAVAR 554
Cdd:PRK11000 78 GMVFQSYALYPHlSVAENMSFGLKLAGAKkeEINQrvnqVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 555 AILKDPRILLLDEATSALDAE---SERIVQEALDRiMVNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAAlrvQMRIEISRLHK-RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
.
gi 1063718281 631 E 631
Cdd:PRK11000 226 A 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1071-1269 |
2.79e-18 |
|
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: 85.86 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLkWLRQQTGLVS--QEPVLFNE-TIRAN 1147
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1148 IA----------------YGKGGDATETEIVSAAE--LSnahgfISGLQQGYDTMVGErgvqLSGGQKQRVAIARAIVKD 1209
Cdd:COG0411 100 VLvaaharlgrgllaallRLPRARREEREARERAEelLE-----RVGLADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1210 PKVLLLDEATSAL-DAESERVVqDALDRV--MVNRTTVVVAHRLSTIKN-ADVIAVVKNG-VIVE 1269
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
423-629 |
3.24e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.86 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRI----DGINLKE--FQLKWiRSK--IGLVSQEPVLFT-S 493
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKpgPDGRG-RAKryIGILHQEYDLYPhR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 SIKENI--AYGKENATVEEIRKATELANASKFIDKLPQG-LDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATS 570
Cdd:TIGR03269 381 TVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKAEEiLDKYPDE----LSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 571 ALDAESERIVQEAL--DRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:TIGR03269 457 TMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1066-1271 |
3.40e-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: 84.64 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1066 DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQlkwlRQQTGLVSQEPVLF-NETI 1144
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1145 RANIAY-GKGGDATETEIVSAAE--LSNAHgfISGLQQgydtmvgERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSA 1221
Cdd:cd03269 88 IDQLVYlAQLKGLKKEEARRRIDewLERLE--LSEYAN-------KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1222 LDAESERVVQDALDRVMVNRTTVV-VAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
424-627 |
3.68e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.81 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 424 FSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTS-SIKENIAYG 502
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 503 K--ENATVEEIRKATELANASKFidkLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIV 580
Cdd:PRK10253 106 RypHQPLFTRWRKEDEEAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 581 QEALDRImvNR----TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELL 627
Cdd:PRK10253 183 LELLSEL--NRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
403-629 |
3.88e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.68 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPAR-PEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRI---------------- 464
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 465 --DGINLKEF------QLKWIRSKIGLVSQ--EPVLFTSSIKENIAYGKENATVEeirKATELANASKFIDKLpqGLDTM 534
Cdd:PRK13651 83 vlEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVS---KEEAKKRAAKYIELV--GLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 535 VGEHGT-QLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVN-RTTVVVAHRLSTV-RNADMIAV 611
Cdd:PRK13651 158 YLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKRTIF 237
|
250
....*....|....*...
gi 1063718281 612 IHQGKIVEKGSHSELLRD 629
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
403-574 |
4.66e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.59 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--INlkefQLKWIRSK 480
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVN----ELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTS-SIKENIAYGKENATV--EEIR----KATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVA 553
Cdd:PRK11650 78 IAMVFQNYALYPHmSVRENMAYGLKIRGMpkAEIEervaEAARILELEPLLDRKPR-----------ELSGGQRQRVAMG 146
|
170 180
....*....|....*....|.
gi 1063718281 554 RAILKDPRILLLDEATSALDA 574
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1223 |
5.17e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.90 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIK--TLQLKWLRQQ 1129
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEP--VLFNETIRANIAYGK-----GGDATETEIVSAAELSNAHGFisglqqgydtmvgERGV--QLSGGQKQRV 1200
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPlnlglSKEEVEKRVKEALKAVGMEGF-------------ENKPphHLSGGQKKRV 146
|
170 180
....*....|....*....|...
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALD 1223
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLD 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1068-1278 |
5.42e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.99 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1068 QIFQDLCLSIRAGKTIALVGESGSGKS-TVIALLQRFYDPD----SGQITLDGVEIKTLQLKWLRQ----QTGLVSQEP- 1137
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1138 VLFN--ETIRANIA------YGKGGDATETEIVSAAE---LSNAHGFISGLQQgydtmvgergvQLSGGQKQRVAIARAI 1206
Cdd:PRK15134 103 VSLNplHTLEKQLYevlslhRGMRREAARGEILNCLDrvgIRQAAKRLTDYPH-----------QLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1207 VKDPKVLLLDEATSALDAESERVVQDALD--RVMVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
729-988 |
6.06e-18 |
|
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: 85.90 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 729 MLILGSIAAVLngviLPIfgiLISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSM 808
Cdd:cd18544 7 LLLLATALELL----GPL---LIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 809 CFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLN 888
Cdd:cd18544 80 LFSHIQRLPLSFFDRT--PVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 889 GYIYMKFMvgfsadaKRMYEEA-SQVA------NDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGV 961
Cdd:cd18544 158 TYLFRKKS-------RKAYREVrEKLSrlnaflQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPL 230
|
250 260
....*....|....*....|....*..
gi 1063718281 962 SFFVLFSSYAASFYAGARLVDDGKTTF 988
Cdd:cd18544 231 VELLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
414-585 |
7.85e-18 |
|
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: 83.18 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 414 ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTS 493
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 SIKENIAY-----GKENATVEEirkATELANASKFIDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:TIGR01189 89 SALENLHFwaaihGGAQRTIED---ALAAVGLTGFED-LPAA----------QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170
....*....|....*..
gi 1063718281 569 TSALDAESERIVQEALD 585
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR 171
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
77-567 |
8.10e-18 |
|
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: 88.70 E-value: 8.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGN-GLgfpIMTIlfgdvidvfgqNQNSSDVSDKIAKVALKFVYLGLGTLVAALlqVSGWMIS--GERQ 153
Cdd:COG4615 16 LLALLLGLLSGLANaGL---IALI-----------NQALNATGAALARLLLLFAGLLVLLLLSRL--ASQLLLTrlGQHA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 154 AGRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAmgekvgkAIQLVSTFIGGFVIAFTEGWLLTLvmvsSI 233
Cdd:COG4615 80 VARLRLRLSRRILAAPLERLE-RIGAARLLAALTEDVRTISQA-------FVRLPELLQSVALVLGCLAYLAWL----SP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 234 PLLVMSGAALAIVIS---KMASRGQTSYAKAAVVVEQTVGSIRTV--------------ASFTGE--KQAISNYNKHLVs 294
Cdd:COG4615 148 PLFLLTLVLLGLGVAgyrLLVRRARRHLRRAREAEDRLFKHFRALlegfkelklnrrrrRAFFDEdlQPTAERYRDLRI- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 295 ayRAGVFEGASTGLGLGTLNIVIFCTYALAVWYGgkmILEKGYTGGQVLIIIFavLTGSMS-LGQASPCLSAFAAGQAAA 373
Cdd:COG4615 227 --RADTIFALANNWGNLLFFALIGLILFLLPALG---WADPAVLSGFVLVLLF--LRGPLSqLVGALPTLSRANVALRKI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 374 YKMFEAIKRKPEIDASDTTGKVLDDIRGdIELNNVNFSYPARPEEQIFR-G-FSLSISSGSTVALVGQSGSGKSTVVSLI 451
Cdd:COG4615 300 EELELALAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDGDEGFTlGpIDLTIRRGELVFIVGGNGSGKSTLAKLL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 452 ERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSsikeniAYGKENATVEEirKATELanaskfIDKLpqGL 531
Cdd:COG4615 379 TGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPA--RAREL------LERL--EL 442
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1063718281 532 DTMVG-EHG----TQLSGGQKQRIAVARAILKDPRILLLDE 567
Cdd:COG4615 443 DHKVSvEDGrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1071-1278 |
8.62e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTV-IALLQRFydPDSGQITLDGVEIKTL---QLKWLRQQTGLVSQEPvlfNETI-- 1144
Cdd:PRK15134 303 KNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDP---NSSLnp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1145 RAN----IAYGKggdATETEIVSAAELSNAhgFISGLQQ-GYDTMVGER-GVQLSGGQKQRVAIARAIVKDPKVLLLDEA 1218
Cdd:PRK15134 378 RLNvlqiIEEGL---RVHQPTLSAAQREQQ--VIAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1219 TSALDaeseRVVQD---ALDRVMVNR---TTVVVAHRLSTIKNA--DVIaVVKNGVIVEKGKHETLIN 1278
Cdd:PRK15134 453 TSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRALchQVI-VLRQGEVVEQGDCERVFA 515
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1047-1271 |
9.49e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 9.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1047 NVKGDIELR--HISFKYPSRPDVQI--FQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI---- 1118
Cdd:PRK13631 15 PLSDDIILRvkNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1119 ------------KTLQLKWLRQQTGLVSQEP--VLFNETIRANIAYGKggDATETEIVSAAELSNAHgfISGLQQGYDTM 1184
Cdd:PRK13631 95 nnhelitnpyskKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGP--VALGVKKSEAKKLAKFY--LNKMGLDDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1185 vgERG-VQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESER-VVQDALDRVMVNRTTVVVAHRLSTI-KNADVIAV 1261
Cdd:PRK13631 171 --ERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIV 248
|
250
....*....|
gi 1063718281 1262 VKNGVIVEKG 1271
Cdd:PRK13631 249 MDKGKILKTG 258
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1068-1253 |
1.27e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.39 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1068 QIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI---KTLQLKWLRQQTGLVSQEP-VLFNET 1143
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1144 IRANIAY-----GKGGDATETEIVSAAE----LSNAHGFisglqqgydtmvgerGVQLSGGQKQRVAIARAIVKDPKVLL 1214
Cdd:PRK10908 96 VYDNVAIpliiaGASGDDIRRRVSAALDkvglLDKAKNF---------------PIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063718281 1215 LDEATSALD-AESERVVQ--DALDRVMVnrTTVVVAHRLSTI 1253
Cdd:PRK10908 161 ADEPTGNLDdALSEGILRlfEEFNRVGV--TVLMATHDIGLI 200
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
403-636 |
1.62e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.60 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFsYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDP----QSGEVRIDGINLKEFQLKWIr 478
Cdd:PRK10418 5 IELRNIAL-QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 sKIGLVSQEP--------VLFTSSIKENIAYGKE--NATVEEIRKATELANASKFIDKLPqgldtmvgehgTQLSGGQKQ 548
Cdd:PRK10418 80 -KIATIMQNPrsafnplhTMHTHARETCLALGKPadDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 549 RIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRT--TVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSE 625
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVET 227
|
250
....*....|.
gi 1063718281 626 LLRDPEGAYSQ 636
Cdd:PRK10418 228 LFNAPKHAVTR 238
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
731-987 |
2.12e-17 |
|
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: 84.13 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 731 ILGSI-AAVLNGVILPIFGILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:cd18574 2 VLSALaAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNG 889
Cdd:cd18574 82 FSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 890 YIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIvsGIGF--GVSFFVLF 967
Cdd:cd18574 160 TLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGL--GIGIfqGLSNLALN 237
|
250 260
....*....|....*....|
gi 1063718281 968 SSYAASFYAGARLVDDGKTT 987
Cdd:cd18574 238 GIVLGVLYYGGSLVSRGELT 257
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
403-634 |
2.16e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSypaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG 482
Cdd:PRK09536 4 IDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVL-FTSSIKENIAYGK----------ENATVEEIRKATELANASKFIDKlpqgldtmvgeHGTQLSGGQKQRIA 551
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFADR-----------PVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 552 VARAILKDPRILLLDEATSALDAESE-RIVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELL-- 627
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLta 229
|
250
....*....|
gi 1063718281 628 ---RDPEGAY 634
Cdd:PRK09536 230 dtlRAAFDAR 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1052-1277 |
2.23e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.47 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTlQLKWLRQQTG 1131
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQ----EPvlfNETIRANI-AYGK--GGDATETEIVSAAELSNAHgfisgLQQGYDTMVGErgvqLSGGQKQRVAIAR 1204
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLlVFGRyfGLSAAAARALVPPLLEFAK-----LENKADAKVGE----LSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVV-------AHRLstiknADVIAVVKNGVIVEKGKHETLI 1277
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
419-625 |
2.35e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 419 QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN---LKEFQLKWIRSKIGLVSQEP-VLFTSS 494
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 495 IKENIAYGK--ENATVEEIRKATELAnaskfIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL 572
Cdd:PRK10908 96 VYDNVAIPLiiAGASGDDIRRRVSAA-----LDKV--GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 573 D-AESERIVQ--EALDRIMVnrTTVVVAHRLSTV-RNADMIAVIHQGKIVEkGSHSE 625
Cdd:PRK10908 169 DdALSEGILRlfEEFNRVGV--TVLMATHDIGLIsRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
420-601 |
3.02e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.56 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 420 IFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF----QLKWIRSKIGLVSQEPVL---FT 492
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLlpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 493 SSikENIAY-----GKENATVEEirKATELANASkfidklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDE 567
Cdd:PRK11629 104 AL--ENVAMplligKKKPAEINS--RALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063718281 568 ATSALDAESERIVQEALDRIMVNRTT--VVVAHRLS 601
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
404-621 |
3.15e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNfsypARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLI---ERfYDPQSGEVRIDGINLkefqLKW--- 476
Cdd:COG0396 2 EIKNLH----VSVEGkEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDI----LELspd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 IRSK--IGLVSQEPV--------LFTSSIKENIAYGKENAT--VEEIR-KATELANASKFIDKlpqGLDtmVGehgtqLS 543
Cdd:COG0396 73 ERARagIFLAFQYPVeipgvsvsNFLRTALNARRGEELSARefLKLLKeKMKELGLDEDFLDR---YVN--EG-----FS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 544 GGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMV-NRTTVVVAH--RLSTVRNADMIAVIHQGKIVEK 620
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKS 222
|
.
gi 1063718281 621 G 621
Cdd:COG0396 223 G 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1271 |
3.85e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.36 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG--VEIKTLQLKWLRQQ 1129
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEP--VLFNETIRANIAYGKGG-DATETEIVSAAELSNAHGFISGLQQgydtmvgERGVQLSGGQKQRVAIARAI 1206
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNlKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1207 VKDPKVLLLDEATSALD----AESERVVQDALDRVMVnrTTVVVAHRLSTIK-NADVIAVVKNGVIVEKG 1271
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGL--TIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
730-979 |
4.35e-17 |
|
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: 83.25 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLnGVILPIFgilISSVIKAFFKppeqlKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:cd18551 5 LLLSLLGTAA-SLAQPLL---VKNLIDALSA-----GGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNG 889
Cdd:cd18551 76 WRRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 890 YIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSS 969
Cdd:cd18551 154 LPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLA 233
|
250
....*....|.
gi 1063718281 970 YAASF-YAGAR 979
Cdd:cd18551 234 LLVVLgVGGAR 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1052-1268 |
4.83e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG--VEIKT----LQLKw 1125
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaIALG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 lrqqTGLVSQEPVLFNE-TIRANIAYG----KGG----DATETEIvsaAELSNAHGFISGLqqgyDTMVGergvQLSGGQ 1196
Cdd:COG3845 82 ----IGMVHQHFMLVPNlTVAENIVLGleptKGGrldrKAARARI---RELSERYGLDVDP----DAKVE----DLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSAL-DAESERVVqDALdRVMVNR-TTVV-VAHRLSTIK-NADVIAVVKNGVIV 1268
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLtPQEADELF-EIL-RRLAAEgKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
421-617 |
6.41e-17 |
|
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: 80.17 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQ-LKWIRSKIGLVSQEP----VLFTSSI 495
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 496 KENIAygkenatveeirkatelanaskfidkLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE 575
Cdd:cd03215 96 AENIA--------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063718281 576 SERIVQEALDRIMVNRTTVVVahrLST-----VRNADMIAVIHQGKI 617
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
423-636 |
7.27e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.60 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL---KEFQLKWIRSKIGLVSQEPVLFTS---SIK 496
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLASLNprmTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 497 ENIA-----YgKENATVEEIRKatELANASKFIDKLPQgldtMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSA 571
Cdd:PRK15079 119 EIIAeplrtY-HPKLSRQEVKD--RVKAMMLKVGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 572 LD----AESERIVQEaLDRIMvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEGAYSQ 636
Cdd:PRK15079 192 LDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
403-627 |
7.53e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.93 E-value: 7.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfQLKWIRSKIG 482
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVL---FTssIKENIA-----YGKENATVEE-IRKATELAnaskfidKLPQGLDTMVGEhgtqLSGGQKQRIAVA 553
Cdd:PRK13537 84 VVPQFDNLdpdFT--VRENLLvfgryFGLSAAAARAlVPPLLEFA-------KLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 554 RAILKDPRILLLDEATSALDAESERIVQEALDRIMVN-RTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELL 627
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1052-1276 |
7.55e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQlKWLRQQTG 1131
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 --LVSQEPVLF-NETIRANIAYGKGGDATETEIVSA--AELsnahgfisGLQQGYDTMVGergvQLSGGQKQRVAIARAI 1206
Cdd:PRK15439 88 iyLVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQllAAL--------GCQLDLDSSAG----SLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1207 VKDPKVLLLDEATSALD-AESERVVQ--DALDRVMVNrtTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETL 1276
Cdd:PRK15439 156 MRDSRILILDEPTASLTpAETERLFSriRELLAQGVG--IVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
793-991 |
9.76e-17 |
|
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: 82.39 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 793 FFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETEnsSGAIGARLSADAAtvrgLVGDALAQTV----QNLASVTAGLVIAF 868
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTK--TGDLTSRLSTDTT----LMSRSVALNAnvllRSLVKTLGMLGFML 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 869 VASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTG 948
Cdd:cd18590 133 SLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLK 212
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063718281 949 IRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTTFDSV 991
Cdd:cd18590 213 DRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSL 255
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1073-1272 |
1.21e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1073 LCLSIRAGKTIALVGESGSGKSTVIALLQRFYdPDSGQITLDGVEIKTLQLK-------WLRQQTGLVSQEPV-----LF 1140
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFAMPVfqylaLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1141 netiraniaYGKGGDATETEIVsAAELSNAhgfiSGLQQGYDTMVGergvQLSGGQKQRVAIARAIVK-------DPKVL 1213
Cdd:COG4138 94 ---------QPAGASSEAVEQL-LAQLAEA----LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptinpEGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1214 LLDEATSALDaeserVVQD-ALDRVMVN-----RTTVVVAHRLS-TIKNADVIAVVKNGVIVEKGK 1272
Cdd:COG4138 156 LLDEPMNSLD-----VAQQaALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1052-1276 |
1.52e-16 |
|
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: 80.11 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIkTLQLKWLRQQTG 1131
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANIA-----YGKGGDATETEIVSAAELSnahgfisGLQQGYDTMVGergvQLSGGQKQRVAIARA 1205
Cdd:cd03265 77 IVFQDLSVDDElTGWENLYiharlYGVPGAERRERIDELLDFV-------GLLEAADRLVK----TYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1206 IVKDPKVLLLDEATSALDAESE----RVVQDALDRvmVNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGKHETL 1276
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRahvwEYIEKLKEE--FGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
421-618 |
1.53e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLK----WIRSKIGLVS----QEPVLFT 492
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRsprdAIRAGIAYVPedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 493 SSIKENIAYgkenATVEE------IRKATELANASKFIDKL---PQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRIL 563
Cdd:COG1129 345 LSIRENITL----ASLDRlsrgglLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 564 LLDEATSALD--AESE--RIVQEALDR----IMVnrttvvvahrlST-----VRNADMIAVIHQGKIV 618
Cdd:COG1129 417 ILDEPTRGIDvgAKAEiyRLIRELAAEgkavIVI-----------SSelpelLGLSDRILVMREGRIV 473
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
420-580 |
1.53e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.21 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 420 IFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINL---KEFQLKWIRSK-IGLVSQEPVLF-TSS 494
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRAKhVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 495 IKENIAY------GKENATVEEIRKATELANASKFIDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:PRK10584 105 ALENVELpallrgESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170
....*....|...
gi 1063718281 569 TSALDAES-ERIV 580
Cdd:PRK10584 174 TGNLDRQTgDKIA 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
414-584 |
1.96e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 79.07 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 414 ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTS 493
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 SIKENIAYGKENATVEEIRKATELANASKFIDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 573
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGFED-RPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|.
gi 1063718281 574 AESERIVQEAL 584
Cdd:cd03231 158 KAGVARFAEAM 168
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
422-621 |
2.51e-16 |
|
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: 79.68 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRsKIGLV--SQEPVLFTSSIKENI 499
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 500 AYGKENATVEEIRKATELANASKFIDkLPQGLDTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERI 579
Cdd:cd03267 117 YLLAAIYDLPPARFKKRLDELSELLD-LEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063718281 580 VQEALDRIMVNRTTVVV--AHRLSTV-RNADMIAVIHQGKIVEKG 621
Cdd:cd03267 192 IRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1059-1289 |
2.53e-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: 85.07 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1059 FKYPSRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTlQLKWLRQQTGLVSQEPV 1138
Cdd:TIGR01257 938 FEPSGRPAVD---RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 LFNE-TIRANI---AYGKGGDATETEIVSAAELSNahgfiSGLQQGYDtmvgERGVQLSGGQKQRVAIARAIVKDPKVLL 1214
Cdd:TIGR01257 1014 LFHHlTVAEHIlfyAQLKGRSWEEAQLEMEAMLED-----TGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1215 LDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLIN-IKDGVYASLVQ 1289
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNcFGTGFYLTLVR 1161
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1068-1276 |
2.88e-16 |
|
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: 79.49 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1068 QIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWlRQQTGL--VSQEPVLFNE-TI 1144
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFPRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1145 RANIAYGKGG-DATETEIVSaaelsnahgFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:TIGR03410 93 EENLLTGLAAlPRRSRKIPD---------EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1224 ----AESERVVQDALDRvmVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETL 1276
Cdd:TIGR03410 164 psiiKDIGRVIRRLRAE--GGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
417-645 |
3.86e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.06 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVV----SLIERFYDPQSgEVRIDGINLKEF-----QLKWIRSKIGLVSQE 487
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGS-HIELLGRTVQREgrlarDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 488 PVLFTS-SIKENIAYGKENAT---------VEEIRKATELANASKFidklpqGLDTMVGEHGTQLSGGQKQRIAVARAIL 557
Cdd:PRK09984 95 FNLVNRlSVLENVLIGALGSTpfwrtcfswFTREQKQRALQALTRV------GMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 558 KDPRILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELLRDP-EGA 633
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHL 248
|
250
....*....|..
gi 1063718281 634 YSQLIRLQEDTK 645
Cdd:PRK09984 249 YRSINRVEENAK 260
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1053-1278 |
4.83e-16 |
|
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: 78.87 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIktlqlkwLRQQT-- 1130
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-------TGLPPhr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 ------GLVSQEPVLFNE-TIRANI---AYGKGGDATETEIVSAAelsnahgfisglqqgYDT------MVGERGVQLSG 1194
Cdd:COG0410 75 iarlgiGYVPEGRRIFPSlTVEENLllgAYARRDRAEVRADLERV---------------YELfprlkeRRRQRAGTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSALdaeSERVVQDALDRVM-VNR--TTVVV----AHRLSTIknADVIAVVKNGVI 1267
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRrLNRegVTILLveqnARFALEI--ADRAYVLERGRI 214
|
250
....*....|.
gi 1063718281 1268 VEKGKHETLIN 1278
Cdd:COG0410 215 VLEGTAAELLA 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
403-631 |
5.77e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.92 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKST----VVSLIErfydPQSGEVRIDGINLKEFQLkWIR 478
Cdd:COG1137 4 LEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPM-HKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SK--IGLVSQEPVLFtssikeniaygkENATVEE-IRKATELANASKfiDKLPQGLDTMVGE----H-----GTQLSGGQ 546
Cdd:COG1137 76 ARlgIGYLPQEASIF------------RKLTVEDnILAVLELRKLSK--KEREERLEELLEEfgitHlrkskAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 547 KQRIAVARAILKDPRILLLDEATSALD----AESERIVQEALDR-IMV-----N-RTTvvvahrLSTVRNAdmiAVIHQG 615
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKERgIGVlitdhNvRET------LGICDRA---YIISEG 212
|
250
....*....|....*.
gi 1063718281 616 KIVEKGSHSELLRDPE 631
Cdd:COG1137 213 KVLAEGTPEEILNNPL 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
415-627 |
5.85e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 415 RPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIErFYDPQ----SGEVRIDG--INLKEFQLkwiRSK-------- 480
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGmpIDAKEMRA---ISAyvqqddlf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IG-LVSQEPVLFTSSIK--ENIAYGKENATVEEIRKATELANASkfidklpqglDTMVGEHGTQ--LSGGQKQRIAVARA 555
Cdd:TIGR00955 111 IPtLTVREHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCA----------NTRIGVPGRVkgLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLST--VRNADMIAVIHQGKIVEKGSHSELL 627
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
417-629 |
6.30e-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: 77.57 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERF--YDPQSGEVRIDGINLKEFQLKwIRSK--IGLVSQEPVlft 492
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 493 ssikeniaygkenaTVEEIRKATELANaskfidklpqgldtmVGEhgtQLSGGQKQRIAVARAILKDPRILLLDEATSAL 572
Cdd:cd03217 88 --------------EIPGVKNADFLRY---------------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 573 DAESERIVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGShSELLRD 629
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1052-1265 |
6.71e-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: 75.95 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveiktlqlkwlrqqtg 1131
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 lvsqepvlfnetiRANIAYgkggdateteivsaaelsnahgfisglqqgYDtmvgergvQLSGGQKQRVAIARAIVKDPK 1211
Cdd:cd03221 62 -------------TVKIGY------------------------------FE--------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDRvmVNRTTVVVAHRLSTIKN-ADVIAVVKNG 1265
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
405-582 |
7.66e-16 |
|
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: 82.29 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 405 LNNVNFSYParPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRI-DGInlkefqlkwirsKIGL 483
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI------------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 484 VSQEPVL-FTSSIKENIAYG-----------------------------KENATVEEIRKATELANASKFID------KL 527
Cdd:TIGR03719 73 LPQEPQLdPTKTVRENVEEGvaeikdaldrfneisakyaepdadfdklaAEQAELQEIIDAADAWDLDSQLEiamdalRC 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 528 PQGlDTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES----ERIVQE 582
Cdd:TIGR03719 153 PPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1069-1251 |
8.26e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1069 IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL-----------QLKWLRQQTGLVSQEP 1137
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaelrnqKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1138 VLFNETIRANIAYGKGGDATETeivsAAELSNAHGFisglqqgyDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDE 1217
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSR----ALEMLAAVGL--------EHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063718281 1218 ATSALDAESERVVQDALDRVMVNRTT--VVVAHRLS 1251
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
403-642 |
8.43e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.58 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYP------------------ARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVR 463
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrTRREEfWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 464 IDGInlkefqlkwIRSKIGL-VSQEPVLftsSIKENI-----AYG---KE-NATVEEIRKATELanaSKFIDkLPqgldt 533
Cdd:COG1134 85 VNGR---------VSALLELgAGFHPEL---TGRENIylngrLLGlsrKEiDEKFDEIVEFAEL---GDFID-QP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 534 mVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE----SERIVQEALDRimvNRTTVVVAHRLSTVRN-ADM 608
Cdd:COG1134 144 -VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlCDR 215
|
250 260 270
....*....|....*....|....*....|....
gi 1063718281 609 IAVIHQGKIVEKGSHSELLRdpegAYSQLIRLQE 642
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIA----AYEALLAGRE 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1067-1248 |
9.03e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1067 VQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLR-QQTGLVSQEPVLFnE 1142
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRaKHVGFVFQSFMLI-P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1143 TIRA--NI---AYGKGGDATETEIVSAAELSNAhgfisGLQQGYDTMVGergvQLSGGQKQRVAIARAIVKDPKVLLLDE 1217
Cdd:PRK10584 102 TLNAleNVelpALLRGESSRQSRNGAKALLEQL-----GLGKRLDHLPA----QLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1063718281 1218 ATSALDAESERVVQDALdrVMVNR----TTVVVAH 1248
Cdd:PRK10584 173 PTGNLDRQTGDKIADLL--FSLNRehgtTLILVTH 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1052-1223 |
9.58e-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: 77.97 E-value: 9.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwLRQQTG 1131
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 L--VSQEPVLFNE-TIRANIAYgkggdATETEIVSAAELSN-AHGFISGLQqgYDTMVGERGVQLSGGQKQRVAIARAIV 1207
Cdd:cd03218 77 IgyLPQEASIFRKlTVEENILA-----VLEIRGLSKKEREEkLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALA 149
|
170
....*....|....*.
gi 1063718281 1208 KDPKVLLLDEATSALD 1223
Cdd:cd03218 150 TNPKFLLLDEPFAGVD 165
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1050-1271 |
1.06e-15 |
|
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: 77.57 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDIELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveiktlQLKW-LRQ 1128
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSlLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLvsqEPVLfneTIRANIAY--------GKGGDATETEIVSAAELSNAhgfisglqqgYDTMVGErgvqLSGGQKQRV 1200
Cdd:cd03220 92 GGGF---NPEL---TGRENIYLngrllglsRKEIDEKIDEIIEFSELGDF----------IDLPVKT----YSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESERVVQDAL-DRVMVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
425-630 |
1.26e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.68 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPvlfTSSIKENIAYGKe 504
Cdd:PRK15112 33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQRISQ- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 505 naTVE-EIRKATEL---ANASKFIDKLPQ-GLdtmVGEHGT----QLSGGQKQRIAVARAILKDPRILLLDEATSALDAE 575
Cdd:PRK15112 109 --ILDfPLRLNTDLepeQREKQIIETLRQvGL---LPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 576 seriVQEALDRIMVNR------TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK15112 184 ----MRSQLINLMLELqekqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1069-1278 |
1.47e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1069 IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDP-----DSGQITLDGVEIKTLQ-LKWLRQQTGLVSQEPVLFNE 1142
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1143 TIRANIAYG----KGGDATETEIVSAAELSNAhgfisGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEA 1218
Cdd:PRK14271 116 SIMDNVLAGvrahKLVPRKEFRGVAQARLTEV-----GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 1219 TSALDAESERVVQDALDRVMVNRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
403-599 |
1.49e-15 |
|
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: 75.65 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFsypARPEEQIF-RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefqlkwiRSKI 481
Cdd:cd03223 1 IELENLSL---ATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFTSSIKENIAYgkenatveeirkatelanaskfidklPQGldtmvgehgTQLSGGQKQRIAVARAILKDPR 561
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIY--------------------------PWD---------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063718281 562 ILLLDEATSALDAESE----RIVQEALdrimvnrTTVV-VAHR 599
Cdd:cd03223 112 FVFLDEATSALDEESEdrlyQLLKELG-------ITVIsVGHR 147
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1053-1269 |
1.58e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIK-TLQLKWLRQQTG 1131
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNE-TIRANIAYG----KGGDATETEIVSAAELSNAHgfiSGLQQGYDTMVGErgvqLSGGQKQRVAIARAI 1206
Cdd:PRK11288 83 IIYQELHLVPEmTVAENLYLGqlphKGGIVNRRLLNYEAREQLEH---LGVDIDPDTPLKY----LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1207 VKDPKVLLLDEATSALDA-ESE---RVVQDALDRvmvNRTTVVVAHRLSTI-KNADVIAVVKNGVIVE 1269
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1047-1271 |
1.78e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1047 NVKGDIELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWL 1126
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 RQQ-TGLVSQEPVLFNE-TIRANIAYGKGG----------DATETEIVSAAELsnahgFISGLQQGYDTMVGErgvqLSG 1194
Cdd:PRK09700 78 AQLgIGIIYQELSVIDElTVLENLYIGRHLtkkvcgvniiDWREMRVRAAMML-----LRVGLKVDLDEKVAN----LSI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSAL-DAESERVVQdALDRVMVNRTTVV-VAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1052-1272 |
2.19e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQlkwlRQQTG 1131
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLF-NETIRANIAY-G--KGGDATETEIvSAAELSNAHGfisgLQQGYDTMVGErgvqLSGGQKQRVAIARAIV 1207
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlArlKGLSKAEAKR-RADEWLERLG----LGDRANKKVEE----LSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTI-KNADVIAVVKNGVIVEKGK 1272
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
403-621 |
2.25e-15 |
|
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: 76.80 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYP-------------------ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVR 463
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 464 IDGinlkefQLKWIrskIGL-VSQEPVLftsSIKENIAY--------GKENATV-EEIRKATELAnasKFIDkLPqgldt 533
Cdd:cd03220 81 VRG------RVSSL---LGLgGGFNPEL---TGRENIYLngrllglsRKEIDEKiDEIIEFSELG---DFID-LP----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 534 mVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAeseRIVQEALDRI--MVN--RTTVVVAHRLSTVRN-ADM 608
Cdd:cd03220 140 -VKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDA---AFQEKCQRRLreLLKqgKTVILVSHDPSSIKRlCDR 211
|
250
....*....|...
gi 1063718281 609 IAVIHQGKIVEKG 621
Cdd:cd03220 212 ALVLEKGKIRFDG 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1052-1249 |
2.38e-15 |
|
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: 74.88 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRFYdpdSGQITLDGVEiktlqlkwlrq 1128
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSlfrALAGLWPWG---SGRIGMPEGE----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNETIRANIAY--GKggdateteivsaaelsnahgfisglqqgydtmvgergvQLSGGQKQRVAIARAI 1206
Cdd:cd03223 65 DLLFLPQRPYLPLGTLREQLIYpwDD--------------------------------------VLSGGEQQRLAFARLL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063718281 1207 VKDPKVLLLDEATSALDAESERVVQDALDRVMvnrTTVV-VAHR 1249
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1051-1272 |
2.49e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.30 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1051 DIELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKwlRQQT 1130
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPVLF-NETIRANIAYG-KGGDATETEIVS----AAELsnahgfisgLQQGYdtMVGERGVQLSGGQKQRVAIAR 1204
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFGlKLAGAKKEEINQrvnqVAEV---------LQLAH--LLDRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAeSERV---VQDALDRVMVNRTTVVVAH-RLSTIKNADVIAVVKNGVIVEKGK 1272
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1072-1274 |
3.58e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.76 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1072 DLCLSIRA-----GKTiALVGESGSGKSTVIALLQRFYDPDSGQITLDG-VEIKTLQLKWL---RQQTGLVSQEPVLF-N 1141
Cdd:PRK11144 12 DLCLTVNLtlpaqGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLppeKRRIGYVFQDARLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1142 ETIRANIAYGkggdateteivsAAELSNAHgfisglqqgYDTMVGERGVQ---------LSGGQKQRVAIARAIVKDPKV 1212
Cdd:PRK11144 91 YKVRGNLRYG------------MAKSMVAQ---------FDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1213 LLLDEATSALDAESERVVQDALDRVM--VNRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGKHE 1274
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLE 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1032-1270 |
3.80e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.15 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1032 ESKIDPSDESGRVLDNVkgDIELRHISFKypsrpdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYdpdSGQI 1111
Cdd:COG2401 18 SSVLDLSERVAIVLEAF--GVELRVVERY--------VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1112 TLDGVEIKTLQLkwlrqqtglvSQEPVLFNetiraniAYGKGGDATE-TEIVSAAELSNAHGFISglqqgydtmvgeRGV 1190
Cdd:COG2401 85 VAGCVDVPDNQF----------GREASLID-------AIGRKGDFKDaVELLNAVGLSDAVLWLR------------RFK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1191 QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVV----QDALDRvmVNRTTVVVAHRlSTIKNA---DVIAVV- 1262
Cdd:COG2401 136 ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVarnlQKLARR--AGITLVVATHH-YDVIDDlqpDLLIFVg 212
|
....*...
gi 1063718281 1263 KNGVIVEK 1270
Cdd:COG2401 213 YGGVPEEK 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1064-1232 |
5.24e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1064 RPDVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRfydPDSGQITLDGVEIKT----LQLKWLRQQTGLvsqE 1136
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTllrLIAGLLP---PAAGTIKLDGGDIDDpdvaEACHYLGHRNAM---K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1137 PVLfneTIRANIA-----YGkggdATETEIVSAAELSNAHGfISGLQQGYdtmvgergvqLSGGQKQRVAIARAIVKDPK 1211
Cdd:PRK13539 86 PAL---TVAENLEfwaafLG----GEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRP 147
|
170 180
....*....|....*....|.
gi 1063718281 1212 VLLLDEATSALDAESERVVQD 1232
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAE 168
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1059-1272 |
5.43e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.58 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1059 FKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG--VEIKTLQLKWLRQQTGLVSQE 1136
Cdd:PRK13638 9 FRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1137 P--VLFNETIRANIAYG-KGGDATETEIV----SAAELSNAHGFisglqqgydtmvGERGVQ-LSGGQKQRVAIARAIVK 1208
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSlRNLGVPEAEITrrvdEALTLVDAQHF------------RHQPIQcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1209 DPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVV-AHRLSTIKN-ADVIAVVKNGVIVEKGK 1272
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGA 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1052-1224 |
5.91e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.96 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTV---IALLQRFydpDSGQITLDGVEIKTLQLKwlRQ 1128
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRVVNELEPA--DR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLF-NETIRANIAYG---KGGDATETE--IVSAAElsnahgfISGLQQgydtMVGERGVQLSGGQKQRVAI 1202
Cdd:PRK11650 77 DIAMVFQNYALYpHMSVRENMAYGlkiRGMPKAEIEerVAEAAR-------ILELEP----LLDRKPRELSGGQRQRVAM 145
|
170 180
....*....|....*....|..
gi 1063718281 1203 ARAIVKDPKVLLLDEATSALDA 1224
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1052-1276 |
7.03e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.34 E-value: 7.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFkypSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLRQ 1128
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNE-TIRANIAYG-KGGDATETEIVSAAELSNAHGFisGLQQGYDTMVGErgvqLSGGQKQRVAIARAI 1206
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPlREHTQLPAPLLHSTVMMKLEAV--GLRGAAKLMPSE----LSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1207 VKDPKVLLLDEATSALDAESERVVQDALDRV--MVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETL 1276
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1063-1226 |
7.18e-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: 74.70 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1063 SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRqqtglvsqepvlfne 1142
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1143 tiraNIAYGKGGDATETEIVSAAELSNAHGFISGLQQGYD---TMVGERGV------QLSGGQKQRVAIARAIVKDPKVL 1213
Cdd:TIGR01189 74 ----NILYLGHLPGLKPELSALENLHFWAAIHGGAQRTIEdalAAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLW 149
|
170
....*....|...
gi 1063718281 1214 LLDEATSALDAES 1226
Cdd:TIGR01189 150 ILDEPTTALDKAG 162
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1052-1217 |
7.83e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.45 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQifqDLCLSIRAGKTIALVGESGSGKSTViallqrFY------DPDSGQITLDGVEIKTLQLkW 1125
Cdd:COG1137 4 LEAENLVKSYGKRTVVK---DVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-H 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 LRQQTGL--VSQEPVLFNE-TIRANIAygkggdAT-ETEIVSAAE--------LSNAHgfISGLQqgyDTmvgeRGVQLS 1193
Cdd:COG1137 74 KRARLGIgyLPQEASIFRKlTVEDNIL------AVlELRKLSKKEreerleelLEEFG--ITHLR---KS----KAYSLS 138
|
170 180
....*....|....*....|....
gi 1063718281 1194 GGQKQRVAIARAIVKDPKVLLLDE 1217
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDE 162
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
414-621 |
9.61e-15 |
|
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: 75.00 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 414 ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQ---SGEVRIDGINLKEFQLKwirSKIGLVSQEPVL 490
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQ---KCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 491 FTS-SIKENIAYGKENATVEEIRKAtelanASKFID---KLPQGLDTMVG-EHGTQLSGGQKQRIAVARAILKDPRILLL 565
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDA-----IRKKRVedvLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 566 DEATSALDAESERIVQEALDRIMV-NRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKG 621
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
423-616 |
1.05e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTVVSLIERFYdPQ---SGEVRIDGinlKEFQLKWIR----SKIGLVSQEPVLFTS-S 494
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG---EELQASNIRdterAGIAIIHQELALVKElS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 495 IKENIAYGKENATVEEIRKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALdA 574
Cdd:PRK13549 99 VLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-T 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063718281 575 ESE-----RIVQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGK 616
Cdd:PRK13549 176 ESEtavllDIIRDLKAH---GIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1052-1271 |
1.15e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQ---IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKW-LR 1127
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 QQTGLVSQEPvlfNETIRANI-----AYGK---GGDATET-----EIVSAAELSNAHGFISGLqqgydtmvgergvqLSG 1194
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATIveedvAFGPenlGIPPEEIrervdESLKKVGMYEYRRHAPHL--------------LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNR----TTVVVAHRLSTIKNADVIAVVKNGVIVEK 1270
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKE--LNKkygiTIILITHYMEEAVEADRIIVMDSGKVVME 225
|
.
gi 1063718281 1271 G 1271
Cdd:PRK13633 226 G 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
425-636 |
1.22e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEV-----RIDgiNLKEFQLKWIRSKIGLVSQEPVlftSSI--KE 497
Cdd:PRK10261 344 SFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqRID--TLSPGKLQALRRDIQFIFQDPY---ASLdpRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 498 NIAYgkenaTVEEIRKATELANASKFIDKLPQGLDTmVG---EHG----TQLSGGQKQRIAVARAILKDPRILLLDEATS 570
Cdd:PRK10261 419 TVGD-----SIMEPLRVHGLLPGKAAAARVAWLLER-VGllpEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 571 ALDAE-SERIVQEALD--RIMvNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQ 636
Cdd:PRK10261 493 ALDVSiRGQIINLLLDlqRDF-GIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQHPYTR 561
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
102-297 |
1.30e-14 |
|
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: 75.84 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 102 GDVIDVFGQNQNSSDVSDKIAKVALkfvyLGLGTLVAALLQVSGWMISGERQAGRIRSLYLQTILRQDIAFFDvETNTGE 181
Cdd:cd18590 20 GRVIDILGGEYQHNAFTSAIGLMCL----FSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE-KTKTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 182 VVGRMSGDTVLiqdaMGEKVGKAIQ-LVSTFI---GGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTS 257
Cdd:cd18590 95 LTSRLSTDTTL----MSRSVALNANvLLRSLVktlGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063718281 258 YAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYR 297
Cdd:cd18590 171 IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYN 210
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1066-1274 |
1.37e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1066 DVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRfYDPDSGQITLDGVEIktlqLKWL---RQQTGL-VS-QEP 1137
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDI----LELSpdeRARAGIfLAfQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1138 VLF----NET-IRAniAYGkggdATETEIVSAAElsnahgFISGLQQgYDTMVG------ERGVQ--LSGGQKQRVAIAR 1204
Cdd:COG0396 87 VEIpgvsVSNfLRT--ALN----ARRGEELSARE------FLKLLKE-KMKELGldedflDRYVNegFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAESERVVQDALDRVMV-NRTTVVVAH--RLSTIKNADVIAVVKNGVIVEKGKHE 1274
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
424-636 |
1.41e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.69 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 424 FSLSisSGSTVALVGQSGSGKS-TVVSLIERFYDPQ--SGEVRIDG---INLKEFQLKWIRS-KIGLVSQEPVlftSSIK 496
Cdd:PRK09473 37 FSLR--AGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGreiLNLPEKELNKLRAeQISMIFQDPM---TSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 497 ENIAYGKENATV----EEIRKATELANASKFID--KLPQGLDTMvGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATS 570
Cdd:PRK09473 112 PYMRVGEQLMEVlmlhKGMSKAEAFEESVRMLDavKMPEARKRM-KMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 571 ALDAESERIVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPEGAYSQ 636
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKreFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPYSI 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1052-1271 |
1.41e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHIS--FKYPS----RPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKW 1125
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 LRQQTGLVSQEPV-----------LFNETIRANIAYgkGGDATETEIVSAAELSnahGFISGLQQGYDTMvgergvqLSG 1194
Cdd:PRK15112 85 RSQRIRMIFQDPStslnprqrisqILDFPLRLNTDL--EPEQREKQIIETLRQV---GLLPDHASYYPHM-------LAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSALDAEservVQDALDRVMVNR------TTVVVAHRLSTIKN-ADVIAVVKNGVI 1267
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMS----MRSQLINLMLELqekqgiSYIYVTQHLGMMKHiSDQVLVMHQGEV 228
|
....
gi 1063718281 1268 VEKG 1271
Cdd:PRK15112 229 VERG 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1029-1223 |
1.49e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1029 IDRESKIDPSDESGRVLDNvKGDIELRHISFKYPSRP--------DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALL 1100
Cdd:PRK10261 292 LEHPAKQEPPIEQDTVVDG-EPILQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1101 QRFYDPDSGQITLDGVEIKTL---QLKWLRQQTGLVSQEPVlfnetirANIaygkggDATETEIVSAAELSNAHGFISG- 1176
Cdd:PRK10261 371 LRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPY-------ASL------DPRQTVGDSIMEPLRVHGLLPGk 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1177 -LQQGYDTMVGERGVQ----------LSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:PRK10261 438 aAAARVAWLLERVGLLpehawrypheFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1066-1271 |
1.75e-14 |
|
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: 73.33 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1066 DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRF--YDPDSGQITLDGVEIKTLQLKwLRQQTG--LVSQEPVlfn 1141
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGifLAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1142 etiraniaygkggdatetEIvsaAELSNAHgFISGLQQGydtmvgergvqLSGGQKQRVAIARAIVKDPKVLLLDEATSA 1221
Cdd:cd03217 88 ------------------EI---PGVKNAD-FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1222 LDAESERVVQDALDRVM-VNRTTVVVAH--RLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:cd03217 135 LDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
77-358 |
2.74e-14 |
|
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: 74.83 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGNGLGFPIMTilfGDVIDvfgqnqNSSDVSDKIAKVALKFVYLGLGTLVAALLQVSGWMISGER---Q 153
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLT---RRAID------GPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSlgvE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 154 AgRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGeKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSI 233
Cdd:cd18543 72 H-DLRTDLFAHLQRLDGAFHD-RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 234 PLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTL 313
Cdd:cd18543 149 PPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1063718281 314 NIVIFCTYALAVWYGGkmilekgytggqvliiiFAVLTGSMSLGQ 358
Cdd:cd18543 229 EALPELGLAAVLALGG-----------------WLVANGSLTLGT 256
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
78-358 |
2.93e-14 |
|
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: 74.78 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 78 ILMILGTIGAVGNGLGFPImtiLFGDVID-VFGQNQnssdvSDKIAKVALkfVYLGLGTLVAALLQVSGWM--ISGERQA 154
Cdd:cd18542 2 LLAILALLLATALNLLIPL---LIRRIIDsVIGGGL-----RELLWLLAL--LILGVALLRGVFRYLQGYLaeKASQKVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 155 GRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIP 234
Cdd:cd18542 72 YDLRNDLYDHLQRLSFSFHD-KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 235 LLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLN 314
Cdd:cd18542 151 FIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1063718281 315 IVIFCTYALAVWYGGKMilekgytggqvliiifaVLTGSMSLGQ 358
Cdd:cd18542 231 FLSGLQIVLVLWVGGYL-----------------VINGEITLGE 257
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1052-1265 |
3.07e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.17 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDS--GQITLDGVEIKTLQLKWL-RQ 1128
Cdd:TIGR02633 2 LEMKGIVKTFG---GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNE-TIRANIAYGKGGDATETEIVSAAELSNAHGFISGLQqgYDTMVGERGV-QLSGGQKQRVAIARAI 1206
Cdd:TIGR02633 79 GIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQ--LDADNVTRPVgDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 1207 VKDPKVLLLDEATSALDAESERVVQDAL-DRVMVNRTTVVVAHRLSTIKN-ADVIAVVKNG 1265
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIrDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
424-646 |
3.08e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 75.33 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 424 FSLSISSGSTVALVGQSGSGKSTVVSLI------------ERFydpqsgevRIDGINL-----KEfQLKWIRSKIGLVSQ 486
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAIcgitkdnwhvtaDRF--------RWNGIDLlklspRE-RRKIIGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 487 EPvlfTSS----------IKENIaygkENATVE---------EIRKATEL------ANASKFIDKLPQgldtmvgehgtQ 541
Cdd:COG4170 97 EP---SSCldpsakigdqLIEAI----PSWTFKgkwwqrfkwRKKRAIELlhrvgiKDHKDIMNSYPH-----------E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 542 LSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVV--VAHRLSTV-RNADMIAVIHQGKIV 618
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIllISHDLESIsQWADTITVLYCGQTV 238
|
250 260
....*....|....*....|....*....
gi 1063718281 619 EKGSHSELLRDPEGAYSQ-LIRLQEDTKQ 646
Cdd:COG4170 239 ESGPTEQILKSPHHPYTKaLLRSMPDFRQ 267
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
435-622 |
3.64e-14 |
|
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: 78.13 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 435 ALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLkEFQLKWIRSKIGLVSQEPVLFTS-SIKENIAYGKE--NATVEEi 511
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQlkGRSWEE- 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 512 rkaTELANASKFIDKlpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNR 591
Cdd:TIGR01257 1038 ---AQLEMEAMLEDT---GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR 1111
|
170 180 190
....*....|....*....|....*....|..
gi 1063718281 592 TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGS 622
Cdd:TIGR01257 1112 TIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
730-1217 |
3.78e-14 |
|
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: 76.76 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPifgiLISSVIKAFFKPPEQLksdtrfwAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:COG4615 19 LLLGLLSGLANAGLIA----LINQALNATGAALARL-------LLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGdALAQTVQNLASVTAGLV-IAFVaSWQLAFIVLAMlplIGLN 888
Cdd:COG4615 88 SRRILAAPLERLERI--GAARLLAALTEDVRTISQAFV-RLPELLQSVALVLGCLAyLAWL-SPPLFLLTLVL---LGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 889 GYIYMKFMvgfsADAKRMYEEASQVANDAVGSIRTVASFCAEekvMKMYKKKCE-------GPMRTGIRQGIVSG----- 956
Cdd:COG4615 161 VAGYRLLV----RRARRHLRRAREAEDRLFKHFRALLEGFKE---LKLNRRRRRaffdedlQPTAERYRDLRIRAdtifa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 957 IGFGVSFFVLFSSYAASFYAGARLVDDGKTT--------------FDSVFRVFFALTMAAVAISQSSSlspdsskasnaa 1022
Cdd:COG4615 234 LANNWGNLLFFALIGLILFLLPALGWADPAVlsgfvlvllflrgpLSQLVGALPTLSRANVALRKIEE------------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1023 asIFAVIDRESKIDPSDESGRVLDNVKGdIELRHISFKYPSRPDVQIFQ----DLclSIRAGKTIALVGESGSGKSTVIA 1098
Cdd:COG4615 302 --LELALAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDGDEGFTlgpiDL--TIRRGELVFIVGGNGSGKSTLAK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1099 LLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETiraniaYGKGGDATETEivsAAELsnahgfisgLQ 1178
Cdd:COG4615 377 LLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPAR---AREL---------LE 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1063718281 1179 Q-GYDTMVGERG-----VQLSGGQKQRVAIARAIVKDPKVLLLDE 1217
Cdd:COG4615 439 RlELDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1070-1265 |
4.24e-14 |
|
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: 71.69 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1070 FQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWL-----------RQQTGLVSQEPV 1138
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragiayvpedRKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 LFNETIraniaygkggdateteivsaaelsnahgfisglqqgydtmvgerGVQLSGGQKQRVAIARAIVKDPKVLLLDEA 1218
Cdd:cd03215 96 AENIAL--------------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1219 TSALDAESERVVQDALDRVMVNRTTVVVahrLST-----IKNADVIAVVKNG 1265
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEG 180
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1063-1253 |
4.83e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1063 SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveiKTLQLKWLR--QQTGL--VSQEPV 1138
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKssQEAGIgiIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 LFNE-TIRANIAYGKggdateteivsaaELSNAHGFIS---------------GLQQGYDTMVGErgvqLSGGQKQRVAI 1202
Cdd:PRK10762 90 LIPQlTIAENIFLGR-------------EFVNRFGRIDwkkmyaeadkllarlNLRFSSDKLVGE----LSIGEQQMVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1203 ARAIVKDPKVLLLDEATSAL-DAESE---RVVQDALDRvmvNRTTVVVAHRLSTI 1253
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRLKEI 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1052-1271 |
5.03e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.19 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYP-------------------SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQIT 1112
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1113 LDGvEIKTLqlkwLRQQTGLVSQ----EPVLFNETI----RANIaygkggDATETEIVSAAELSNahgFIsglqqgyDTM 1184
Cdd:COG1134 85 VNG-RVSAL----LELGAGFHPEltgrENIYLNGRLlglsRKEI------DEKFDEIVEFAELGD---FI-------DQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1185 VGergvQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAE----SERVVQDALDRvmvNRTTVVVAHRLSTIKN-ADVI 1259
Cdd:COG1134 144 VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlCDRA 216
|
250
....*....|..
gi 1063718281 1260 AVVKNGVIVEKG 1271
Cdd:COG1134 217 IWLEKGRLVMDG 228
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
729-987 |
5.07e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 74.06 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 729 MLILGSIAAVLnGVILPIfgiLISSVI-KAFFKPpeqlksDTR--FWAIIFML-LGVASMVVFPAQTIFFSIAGCKLVQR 804
Cdd:cd18550 4 VLLLILLSALL-GLLPPL---LLREIIdDALPQG------DLGllVLLALGMVaVAVASALLGVVQTYLSARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 805 IRSMCFEKVVRMEVGWFdeTENSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPL 884
Cdd:cd18550 74 LRVQLYAHLQRMSLAFF--TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 885 IGLNGYIYMKFMVGFSADAKRMYEEASQVAND--AVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVsGIGFGVS 962
Cdd:cd18550 152 FVLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALA-GRWFFAA 230
|
250 260
....*....|....*....|....*.
gi 1063718281 963 FFVLFSSYAASFY-AGARLVDDGKTT 987
Cdd:cd18550 231 LGLFTAIGPALVYwVGGLLVIGGGLT 256
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
730-987 |
5.21e-14 |
|
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: 73.98 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIKAFFKPPEQlKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLT-ASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNG 889
Cdd:cd18541 80 FAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 890 YIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSS 969
Cdd:cd18541 158 YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLS 237
|
250
....*....|....*...
gi 1063718281 970 YAASFYAGARLVDDGKTT 987
Cdd:cd18541 238 FLIVLWYGGRLVIRGTIT 255
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
77-343 |
5.66e-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: 74.08 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGNGLGFPIMT-ILFGDVIDVFGQNQNSSdvsdkiakvalKFVYLGLGTLVAALLQ-VSGWMIS----- 149
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTkILIDDVLIQLGPGGNTS-----------LLLLLVLGLAGAYVLSaLLGILRGrllar 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 150 -GERQAGRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLV 228
Cdd:cd18563 70 lGERITADLRRDLYEHLQRLSLSFFD-KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 229 MVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVfegaSTGL 308
Cdd:cd18563 149 VLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANI----RAEK 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063718281 309 GLGTLNIVI-FCTY--ALAVWY-GGKMILEKGYTGGQVL 343
Cdd:cd18563 225 LWATFFPLLtFLTSlgTLIVWYfGGRQVLSGTMTLGTLV 263
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1052-1274 |
7.34e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.95 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPD-----SGQITLDGVEIKTLQLKWL 1126
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 --RQQTGLVSQEPVLF-NETIRANIAYG---KGGDATETEIVSAAELSNAHgfiSGLQQGYDTMVGERGVQLSGGQKQRV 1200
Cdd:PRK14267 82 evRREVGMVFQYPNPFpHLTIYDNVAIGvklNGLVKSKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHR-LSTIKNADVIAVVKNGVIVEKGKHE 1274
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
425-639 |
1.02e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.01 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKS----TVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIG----LVSQEPVlfTS--- 493
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPM--TSlnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 ------SIKENIAYGKENATVEEIRKATELANASKFIDklPQG-LDtmVGEHgtQLSGGQKQRIAVARAILKDPRILLLD 566
Cdd:PRK11022 105 cytvgfQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPD--PASrLD--VYPH--QLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 567 EATSALDAESERIVQEALDRIMV--NRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQ-LIR 639
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQaLLR 255
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1052-1265 |
1.09e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYdPD---SGQITLDGveiKTLQLKWLR- 1127
Cdd:PRK13549 6 LEMKNITKTFG---GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG---EELQASNIRd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1128 -QQTGLV--SQEPVLFNE-TIRANIAYG----KGGDATETEIVS-AAELsnahgfisgLQQ-GYDTMVGERGVQLSGGQK 1197
Cdd:PRK13549 79 tERAGIAiiHQELALVKElSVLENIFLGneitPGGIMDYDAMYLrAQKL---------LAQlKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1198 QRVAIARAIVKDPKVLLLDEATSALdAESE-----RVVQDALDRvmvNRTTVVVAHRLSTIKN-ADVIAVVKNG 1265
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASL-TESEtavllDIIRDLKAH---GIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1052-1278 |
1.13e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.22 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRF--YDPDSGQI------------------ 1111
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1112 ----------TLDGVEI------KTLQLKWLRQQTGLVSQEPVLF-NETIRANI--AYGKGGDATETEIVSAAELsnahg 1172
Cdd:TIGR03269 78 vgepcpvcggTLEPEEVdfwnlsDKLRRRIRKRIAIMLQRTFALYgDDTVLDNVleALEEIGYEGKEAVGRAVDL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1173 fISGLQQGYDTMVGERgvQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNR--TTVVVAHRL 1250
Cdd:TIGR03269 153 -IEMVQLSHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWP 229
|
250 260
....*....|....*....|....*....
gi 1063718281 1251 STIKN-ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:TIGR03269 230 EVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
128-360 |
1.26e-13 |
|
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: 73.32 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 128 FVYLGLGTLVAALLQ---------VSGWMisGERQAGRIRS-LY--LQtilRQDIAFFDvETNTGEVVGRMSGDTVLIQD 195
Cdd:cd18564 53 LLLAAAALVGIALLRglasyagtyLTALV--GQRVVLDLRRdLFahLQ---RLSLSFHD-RRRTGDLLSRLTGDVGAIQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 196 AMgekVGKAIQLVS---TFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSI 272
Cdd:cd18564 127 LL---VSGVLPLLTnllTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 273 RTVASFTGEKQAISNYNKHLVSAYRAGVfEGASTGLGLG-TLNIVIFCTYALAVWYGGKMILEKGYTGGQVLIII----- 346
Cdd:cd18564 204 RVVQAFGREEHEERRFARENRKSLRAGL-RAARLQALLSpVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLaylkn 282
|
250 260
....*....|....*....|.
gi 1063718281 347 -------FAVLTGSMSLGQAS 360
Cdd:cd18564 283 lykpvrdLAKLTGRIAKASAS 303
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1069-1271 |
1.33e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1069 IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNE-TIRAN 1147
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1148 IAYGKGGD--------ATETEIVSAAelSNAHGFISGLQQGYDTmvgergvqLSGGQKQRVAIARAIVKDPKVLLLDEAT 1219
Cdd:PRK10253 102 VARGRYPHqplftrwrKEDEEAVTKA--MQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1220 SALDAESERVVQDALDRvmVNR----TTVVVAHRLS-TIKNADVIAVVKNGVIVEKG 1271
Cdd:PRK10253 172 TWLDISHQIDLLELLSE--LNRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
417-631 |
1.36e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.98 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERF--YDPQSGEVRIDGINLKEFQLKwIRSKIG--LVSQEPVLFT 492
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGifLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 493 SSIKEN---IAYgkeNATveeiRKATELANAS--KFIDKLPQGLDtMVGEHGTQL--------SGGQKQRIAVARAILKD 559
Cdd:CHL00131 98 GVSNADflrLAY---NSK----RKFQGLPELDplEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGShSELLRDPE 631
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AELAKELE 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
414-582 |
1.58e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 414 ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLKWIRSKIGLVSQ----EPV 489
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHrnamKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 490 LftsSIKENIA-----YGKENATVEEIRKATELANaskfIDKLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILL 564
Cdd:PRK13539 88 L---TVAENLEfwaafLGGEELDIAAALEAVGLAP----LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWI 150
|
170
....*....|....*...
gi 1063718281 565 LDEATSALDAESERIVQE 582
Cdd:PRK13539 151 LDEPTAALDAAAVALFAE 168
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
773-987 |
2.52e-13 |
|
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: 72.14 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 773 AIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQ 852
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERE--TSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 853 TVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLngyiymkFMVGFSADAKRMYEEA-SQVAN------DAVGSIRTVA 925
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-------ATRWFRRRSSRAYRRArERIAAvnadlqETLAGIRVVQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 926 SFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTT 987
Cdd:cd18546 193 AFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLT 254
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
414-628 |
3.63e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 414 ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVV-SLIERFYDPQ-------SGEVRIDGINLKEF---QLKWIRSKIG 482
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGEPLAAIdapRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPvlFTSSIKENIAYGKenatVEEIRKATELANASKFIDKLP---QGLDTMVGEHGTQLSGGQKQRIAVARAILK- 558
Cdd:PRK13547 90 QAAQPA--FAFSAREIVLLGR----YPHARRAGALTHRDGEIAWQAlalAGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 559 --------DPRILLLDEATSALD-AESERIVQ--EALDRIMvNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSEL 626
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDlAHQHRLLDtvRRLARDW-NLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADV 242
|
..
gi 1063718281 627 LR 628
Cdd:PRK13547 243 LT 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1053-1269 |
3.90e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSrpdVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDS--GQITLDGveiKTLQLKWLRQ-- 1128
Cdd:NF040905 3 EMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDIRDse 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLV--SQE----PVLfneTIRANIAYG----KGG--DATETeIVSAAELSNahgfISGLQQGYDTMVGERGVqlsgGQ 1196
Cdd:NF040905 77 ALGIViiHQElaliPYL---SIAENIFLGneraKRGviDWNET-NRRARELLA----KVGLDESPDTLVTDIGV----GK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSAL-DAESERVvqdaLDRVMVNR----TTVVVAHRLSTI-KNADVIAVVKNGVIVE 1269
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
403-627 |
5.16e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWI-RSKI 481
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFTS-SIKENIAYGKENATVEEIRKATElanasKFIDKLPQGLDTMVGEHGTqLSGGQKQRIAVARAILKDP 560
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIK-----WVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 561 RILLLDEATSALdaeSERIVQEALDRIMVNR----TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHSELL 627
Cdd:PRK11614 157 RLLLLDEPSLGL---APIIIQQIFDTIEQLReqgmTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
423-598 |
5.46e-13 |
|
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: 70.13 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGS-----TVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKeFQLKWIRSKiglvsqepvlFTSSIKE 497
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD----------YEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 498 nIAYGKENATVEEIRKATELANaskfidklPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 577
Cdd:cd03237 81 -LLSSITKDFYTHPYFKTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180
....*....|....*....|...
gi 1063718281 578 RIVQEALDRIMVN--RTTVVVAH 598
Cdd:cd03237 152 LMASKVIRRFAENneKTAFVVEH 174
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1069-1236 |
5.53e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1069 IFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL------QLKWLRQQTG----LVSQEPV 1138
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGikteLTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 LFNETIRaniaygkgGDATETEIVSAaelsnahgfisgLQQgydtmVGERGV------QLSGGQKQRVAIARAIVKDPKV 1212
Cdd:PRK13538 96 RFYQRLH--------GPGDDEALWEA------------LAQ-----VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPL 150
|
170 180
....*....|....*....|....
gi 1063718281 1213 LLLDEATSALDAESERVVQDALDR 1236
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
405-576 |
6.55e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.84 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 405 LNNVNFSYParPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRI-DGInlkefqlkwirsKIGL 483
Cdd:PRK11819 9 MNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI------------KVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 484 VSQEPVLFTS-SIKENI-------------------AYG----------KENATVEEIRKATELANASKFID------KL 527
Cdd:PRK11819 75 LPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAepdadfdalaAEQGELQEIIDAADAWDLDSQLEiamdalRC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063718281 528 PQGlDTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 576
Cdd:PRK11819 155 PPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1052-1250 |
8.37e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveikTLQLKWLRQQTG 1131
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIAYGKGGDATETEIVSAAELSNAhgfisGLQQgydtmvgergvqLSGGQKQRVAIARAIVKDPK 1211
Cdd:PRK09544 78 LDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDA-----PMQK------------LSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALD--RVMVNRTTVVVAHRL 1250
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDL 181
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1052-1272 |
9.76e-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: 69.28 E-value: 9.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKY------------------PSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITL 1113
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1114 DGVEIKTLQLKWLRQQTGLVSQE-------PVLfnETIRANIA-YGKGGDATETEIVSAAELSNahgfisgLQQGYDTMV 1185
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQKtqlwwdlPVI--DSFYLLAAiYDLPPARFKKRLDELSELLD-------LEELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1186 geRgvQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVahrLSTIKNADVIAVVKNG 1265
Cdd:cd03267 152 --R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVL---LTSHYMKDIEALARRV 224
|
....*..
gi 1063718281 1266 VIVEKGK 1272
Cdd:cd03267 225 LVIDKGR 231
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
156-342 |
1.24e-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: 70.19 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 156 RIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPL 235
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFD-SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 236 LVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNi 315
Cdd:cd18589 149 LLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSS- 227
|
170 180 190
....*....|....*....|....*....|
gi 1063718281 316 viFCTYALAV---WYGGKMIlekgyTGGQV 342
Cdd:cd18589 228 --FSGLALKVgilYYGGQLV-----TAGTV 250
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
727-965 |
1.26e-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: 70.29 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 727 IPMLILG-SIAAVLNGVILPIFGILISSVIKAffkPPEQLksdtRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRI 805
Cdd:cd18565 17 APPLLIGvAIDAVFNGEASFLPLVPASLGPAD---PRGQL----WLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 806 RSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLI 885
Cdd:cd18565 90 RTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 886 GLNGYIYMKfMVGFSADAKRmyEEASQVA---NDAVGSIRTVASFCAE----EKVMKM---YKKKCEGPMRTGIRQ---- 951
Cdd:cd18565 168 IAGTYWFQR-RIEPRYRAVR--EAVGDLNarlENNLSGIAVIKAFTAEdferERVADAseeYRDANWRAIRLRAAFfpvi 244
|
250
....*....|....
gi 1063718281 952 GIVSGIGFGVSFFV 965
Cdd:cd18565 245 RLVAGAGFVATFVV 258
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
729-976 |
1.62e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 69.85 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 729 MLILGSIAAVLNGVILPIF-GILISSVIKaffkPPEQLKSDTRFWAIIFMLLG--VASMVVFPAQTIFFSIAGCKLVQRI 805
Cdd:cd18563 3 LGFLLMLLGTALGLVPPYLtKILIDDVLI----QLGPGGNTSLLLLLVLGLAGayVLSALLGILRGRLLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 806 RSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLI 885
Cdd:cd18563 79 RRDLYEHLQRLSLSFFDK--RQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 886 GLNGYIYMKFMvgfsadaKRMYEEASQ-------VANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQ------- 951
Cdd:cd18563 157 VWGSYFFWKKI-------RRLFHRQWRrwsrlnsVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAeklwatf 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1063718281 952 ----GIVSGIG------FGVSF----------FVLFSSYAASFYA 976
Cdd:cd18563 230 fpllTFLTSLGtlivwyFGGRQvlsgtmtlgtLVAFLSYLGMFYG 274
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1064-1246 |
1.76e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1064 RPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQrFYDPD----SGQITLDGVEIKTLQLK----WLRQQT----G 1131
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMRaisaYVQQDDlfipT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVLFNETIRANIAYGKggdATETEIVSAA--ELsnahgfisGLQQGYDTMVGERGVQ--LSGGQKQRVAIARAIV 1207
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTK---KEKRERVDEVlqAL--------GLRKCANTRIGVPGRVkgLSGGERKRLAFASELL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063718281 1208 KDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVV 1246
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIIC 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1052-1277 |
1.92e-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: 71.37 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPS--RPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQIT-------LDGVEIKTLQ 1122
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 LKWLRQQTGLVSQEPVLF-NETIRANIAygkggDATETEIvsAAELSNAHGFISGLQQGYDTMVGERGV-----QLSGGQ 1196
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYpHRTVLDNLT-----EAIGLEL--PDELARMKAVITLKMVGFDEEKAEEILdkypdELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDAL--DRVMVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKH 1273
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDP 512
|
....
gi 1063718281 1274 ETLI 1277
Cdd:TIGR03269 513 EEIV 516
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1073-1272 |
2.51e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1073 LCLSIRAGKTIALVGESGSGKSTVIA----LLqrfydPDSGQITLDGVEIKTLQLKWL-RQQTGLVSQEPVLFNETIRAN 1147
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1148 IAYGKGGDATETEIVSA-AELSNAhgfiSGLQQGYDTMVGergvQLSGGQKQRVAIA-------RAIVKDPKVLLLDEAT 1219
Cdd:PRK03695 90 LTLHQPDKTRTEAVASAlNEVAEA----LGLDDKLGRSVN----QLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1220 SALDaeserVVQD-ALDRVMV-----NRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKGK 1272
Cdd:PRK03695 162 NSLD-----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGR 216
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1052-1217 |
2.71e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSrpdvQIFQ--DLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQ 1129
Cdd:PRK10522 323 LELRNVTFAYQD----NGFSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSQEPVLFNETIraniayGKGGDATETEIVSA--------AELSNAHGFISGLqqgydtmvgergvQLSGGQKQRVA 1201
Cdd:PRK10522 399 FSAVFTDFHLFDQLL------GPEGKPANPALVEKwlerlkmaHKLELEDGRISNL-------------KLSKGQKKRLA 459
|
170
....*....|....*.
gi 1063718281 1202 IARAIVKDPKVLLLDE 1217
Cdd:PRK10522 460 LLLALAEERDILLLDE 475
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
407-591 |
2.73e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 407 NVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLK------EFQLKWIRSK 480
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlctyQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLvsqEPVLftsSIKENIAYG-KENATVEEIRKATELANASKFIDkLPQGLdtmvgehgtqLSGGQKQRIAVARAILKD 559
Cdd:PRK13540 83 SGI---NPYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSK 145
|
170 180 190
....*....|....*....|....*....|..
gi 1063718281 560 PRILLLDEATSALDaesERIVQEALDRIMVNR 591
Cdd:PRK13540 146 AKLWLLDEPLVALD---ELSLLTIITKIQEHR 174
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1076-1248 |
2.86e-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: 68.20 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1076 SIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEI--KTLQLKwlRQQTGLVSQepvLFNETIRaniayGKG 1153
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsyKPQYIK--ADYEGTVRD---LLSSITK-----DFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1154 GDAT-ETEIVSAAelsnahgfisGLQQGYDTMVGErgvqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQD 1232
Cdd:cd03237 91 THPYfKTEIAKPL----------QIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170
....*....|....*...
gi 1063718281 1233 ALDRVMVN--RTTVVVAH 1248
Cdd:cd03237 157 VIRRFAENneKTAFVVEH 174
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
422-628 |
3.83e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGIN----LKEFqlkwiRSKIGLV----SQ----EPV 489
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrRKEF-----ARRIGVVfgqrSQlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 490 LFTSSIKENIaYGKENATVEE-IRKATELANASKFidklpqgLDTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:COG4586 114 IDSFRLLKAI-YRIPDAEYKKrLDELVELLDLGEL-------LDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 569 TSALDAESERIVQEALDRImvNR---TTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGSHSELLR 628
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEY--NRergTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
403-626 |
4.05e-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: 70.22 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERF--YDPQSGEV------------------ 462
Cdd:TIGR03269 1 IEVKNLTKKFDGK---EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 463 ---------------RIDGINLKEFQLKWIRSKIGLVSQEPVLFtssikeniaYGKENATVEEIRKATELA-NASKFIDK 526
Cdd:TIGR03269 78 vgepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFAL---------YGDDTVLDNVLEALEEIGyEGKEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 527 LPQGLDTMVGEH-----GTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHR 599
Cdd:TIGR03269 149 AVDLIEMVQLSHrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHW 228
|
250 260
....*....|....*....|....*...
gi 1063718281 600 LSTVRN-ADMIAVIHQGKIVEKGSHSEL 626
Cdd:TIGR03269 229 PEVIEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1038-1223 |
5.62e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.60 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1038 SDESGRVLDNVKgdiELRhISFKYPSrPDVQIFQDLCLSIRAGKTIALVGESGSGKS-TVIALLQRFYDPD--SGQITLD 1114
Cdd:PRK09473 5 AQQQADALLDVK---DLR-VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1115 GVEIKTL---QLKWLR-QQTGLVSQEPVL-----------FNETIRANIAYGKgGDATETEI--VSAAELSNAHGFIsgl 1177
Cdd:PRK09473 80 GREILNLpekELNKLRaEQISMIFQDPMTslnpymrvgeqLMEVLMLHKGMSK-AEAFEESVrmLDAVKMPEARKRM--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063718281 1178 qqgydTMVGErgvQLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:PRK09473 156 -----KMYPH---EFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
423-618 |
5.74e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTVVSLIERFYdPQ---SGEVRIDGINLKEFQLKWIRSK-IGLVSQEPVLFTS-SIKE 497
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 498 NIAYGKE-------NATVEEIRKATELANASKfIDKLPQGLDTMvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATS 570
Cdd:TIGR02633 98 NIFLGNEitlpggrMAYNAMYLRAKNLLRELQ-LDADNVTRPVG------DYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063718281 571 AL-DAESERIVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIV 618
Cdd:TIGR02633 171 SLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
402-643 |
6.45e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.29 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 402 DIELNNVNFSYPARPEEQIFRgFSLSISSGSTVALVGQSGSGKSTVVSLI------------ERFydpqsgevRIDGINL 469
Cdd:PRK15093 5 DIRNLTIEFKTSDGWVKAVDR-VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtaDRM--------RFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 470 KEFQLKWIRSKIG----LVSQEPvlfTSSIKENIAYGKEnaTVEEI-----------------RKATELANASKFIDKlp 528
Cdd:PRK15093 76 LRLSPRERRKLVGhnvsMIFQEP---QSCLDPSERVGRQ--LMQNIpgwtykgrwwqrfgwrkRRAIELLHRVGIKDH-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 529 qglDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVV--VAHRLSTVRN- 605
Cdd:PRK15093 149 ---KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQw 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063718281 606 ADMIAVIHQGKIVEKGSHSELLRDPEGAYSQ-LIRLQED 643
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELVTTPHHPYTQaLIRAIPD 264
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
407-631 |
6.49e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 407 NVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKST----VVSLIERfydpQSGEVRIDGINLKEFQL-KWIRSKI 481
Cdd:PRK10895 8 NLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEPVLFTS-SIKENIAygkenaTVEEIRKATelaNASKFIDKLPQGLDTMVGEH-----GTQLSGGQKQRIAVARA 555
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLM------AVLQIRDDL---SAEQREDRANELMEEFHIEHlrdsmGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 556 ILKDPRILLLDEATSALDAES----ERIVQEALDRIMvnrTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHSELLRDP 630
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISvidiKRIIEHLRDSGL---GVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
.
gi 1063718281 631 E 631
Cdd:PRK10895 229 H 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1063-1227 |
6.79e-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: 65.98 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1063 SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLdgveiktlqlkwlrQQTGLVSQEPvlfne 1142
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL--------------NGGPLDFQRD----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1143 TIRANIAYGKGGDATETEIVSAAELSNAHGFIS--GLQQGYDTmVGERGV------QLSGGQKQRVAIARAIVKDPKVLL 1214
Cdd:cd03231 70 SIARGLLYLGHAPGIKTTLSVLENLRFWHADHSdeQVEEALAR-VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWI 148
|
170
....*....|...
gi 1063718281 1215 LDEATSALDAESE 1227
Cdd:cd03231 149 LDEPTTALDKAGV 161
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
729-988 |
7.02e-12 |
|
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: 67.81 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 729 MLILGSIAAVLNgVILPIF-GILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRS 807
Cdd:cd18547 4 VIILAIISTLLS-VLGPYLlGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 808 MCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIgl 887
Cdd:cd18547 83 DLFEKLQRLPLSYFDT--HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 888 ngYIYMKFMVGFSADA-KRMYEEASQV---ANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSF 963
Cdd:cd18547 159 --LLVTKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMN 236
|
250 260
....*....|....*....|....*
gi 1063718281 964 FVLFSSYAASFYAGARLVDDGKTTF 988
Cdd:cd18547 237 FINNLGYVLVAVVGGLLVINGALTV 261
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
404-619 |
7.33e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 404 ELNNVNFSYPArpeEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLKWIR----S 479
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTaalaA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQE----PVLftsSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLD--TMVGEhgtqLSGGQKQRIAVA 553
Cdd:PRK11288 80 GVAIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 554 RAILKDPRILLLDEATSALDA-ESE---RIVQEALDRimvNRTTVVVAHRLSTV-RNADMIAVIHQGKIVE 619
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
417-641 |
9.10e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLI--ERFYDPQSGEVRIDGINLKEFQLKWIRSK-IGLVSQEPVLFTS 493
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 SIKENIAYGKENAtVEEIRKATELA--NASKFID------KLPQGLDTMVGEHGtqLSGGQKQRIAVARAILKDPRILLL 565
Cdd:PRK09580 93 VSNQFFLQTALNA-VRSYRGQEPLDrfDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 566 DEATSALDAESERIVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQLIRLQ 641
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGYGWLTEQQ 248
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
423-631 |
9.44e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIrSKIGLVS--QEPVLFTS------- 493
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFREmtvienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 ------SIKENIAYG--KENATVEEIRKAteLANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLL 565
Cdd:PRK11300 102 lvaqhqQLKTGLFSGllKTPAFRRAESEA--LDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 566 DEATSALDAESERIVQEALD--RIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
417-619 |
9.56e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFY--DPQSGEVRIDGINLkefqlkwirskiglvSQEpvlftSS 494
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 495 IKENIAYGKENATVEEIRKATELANASKFIDKLPQgldtmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDA 574
Cdd:COG2401 102 LIDAIGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063718281 575 ESERIVQEALDRIM--VNRTTVVVAHRlSTVRNA---DMIAVIHQGKIVE 619
Cdd:COG2401 170 QTAKRVARNLQKLArrAGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1069-1271 |
9.58e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.16 E-value: 9.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1069 IFQDLCLSIRAGKTIALVGESGSGKSTVI-ALLQRFYDPD-------SGQITLDG---VEIKTLQLKWLRQQTGLVSQEP 1137
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGeplAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1138 VLFneTIRANIAYGK-------GGDATETEIVSAAELSNAhgfisglqqGYDTMVGERGVQLSGGQKQRVAIARAIVK-- 1208
Cdd:PRK13547 96 FAF--SAREIVLLGRypharraGALTHRDGEIAWQALALA---------GATALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1209 -------DPKVLLLDEATSALDAESERVVQDALDRVMV--NRTTVVVAHRLS-TIKNADVIAVVKNGVIVEKG 1271
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
403-626 |
1.03e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeqifrGFS-----LSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWI 477
Cdd:PRK10522 323 LELRNVTFAYQDN-------GFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 478 RSKIGLVSQEPVLFTSSIkeniayGKENATVEEirkatelANASKFIDKLPQGLDTMVGEH---GTQLSGGQKQRIAVAR 554
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQLL------GPEGKPANP-------ALVEKWLERLKMAHKLELEDGrisNLKLSKGQKKRLALLL 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 555 AILKDPRILLLDEATSALDAESERIV-QEALD--RIMvNRTTVVVAHRLSTVRNADMIAVIHQGKIVE-KGSHSEL 626
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFyQVLLPllQEM-GKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1057-1274 |
1.13e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1057 ISFKYpSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG----------VEIKTLQLKWL 1126
Cdd:PRK10261 20 IAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 RQQTG----LVSQEPVL-----------FNETIRANIAYGKggdatETEIVSAAELsnahgfisgLQQ----GYDTMVGE 1187
Cdd:PRK10261 99 RHVRGadmaMIFQEPMTslnpvftvgeqIAESIRLHQGASR-----EEAMVEAKRM---------LDQvripEAQTILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1188 RGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE-------RVVQDALDrvmvnRTTVVVAHRLSTIKN-ADVI 1259
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMS-----MGVIFITHDMGVVAEiADRV 239
|
250
....*....|....*
gi 1063718281 1260 AVVKNGVIVEKGKHE 1274
Cdd:PRK10261 240 LVMYQGEAVETGSVE 254
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1070-1275 |
1.18e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1070 FQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKtlqlKWLRQQ-TGLVSQE-------PVLFN 1141
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1142 ETIRANiAYGKGG-----DATETEIVSAAeLSNAhgfisGLQQGYDTMVGErgvqLSGGQKQRVAIARAIVKDPKVLLLD 1216
Cdd:PRK15056 99 DVVMMG-RYGHMGwlrraKKRDRQIVTAA-LARV-----DMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1217 EATSALDAESERVVQDALDRVMVN-RTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHET 1275
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1070-1271 |
1.24e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1070 FQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG-----VEIKTL---QLKWL-RQQTGLVSQEPVlf 1140
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALseaERRRLlRTEWGFVHQHPR-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1141 nETIR------ANIA----------YGKGgDATETEIVSAAELSNAHgfisglqqgydtmVGERGVQLSGGQKQRVAIAR 1204
Cdd:PRK11701 100 -DGLRmqvsagGNIGerlmavgarhYGDI-RATAGDWLERVEIDAAR-------------IDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAEservVQ----DALdRVMVNR---TTVVVAHRLSTIKN-ADVIAVVKNGVIVEKG 1271
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVS----VQarllDLL-RGLVRElglAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
77-291 |
1.49e-11 |
|
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: 66.66 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGNGLGfpimTILFGDVIDVFGQNQNSSDVSD--KIAKVALKFVYLGLGTLVAALLQvsGWMIS--GER 152
Cdd:cd18547 2 ILVIILAIISTLLSVLG----PYLLGKAIDLIIEGLGGGGGVDfsGLLRILLLLLGLYLLSALFSYLQ--NRLMArvSQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 153 QAGRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSS 232
Cdd:cd18547 76 TVYDLRKDLFEKLQRLPLSYFD-THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 233 IPLLVmsgaalaIVISKMASRGQTSYAK-----AAV--VVEQTVGSIRTVASFTGEKQAISNYNKH 291
Cdd:cd18547 155 VPLSL-------LVTKFIAKRSQKYFRKqqkalGELngYIEEMISGQKVVKAFNREEEAIEEFDEI 213
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
731-987 |
1.51e-11 |
|
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: 67.15 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 731 ILGSIAAVLNGVILPI-----FGILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPA---------QTIFFSI 796
Cdd:cd18564 1 LALALLALLLETALRLlepwpLKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLLLAAAALVGIAllrglasyaGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 797 AGCKLVQRIRSMCFEKVVRMEVGWFDETEnsSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAF 876
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 877 IVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQ-GIVS 955
Cdd:cd18564 159 IALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAaRLQA 238
|
250 260 270
....*....|....*....|....*....|..
gi 1063718281 956 GIGFGVSFFVLFSSyAASFYAGARLVDDGKTT 987
Cdd:cd18564 239 LLSPVVDVLVAVGT-ALVLWFGAWLVLAGRLT 269
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
421-613 |
1.61e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGFSLSI-SSGSTVALVGQSGSGKSTVVS-----LIERFYDPQSgEVRIDGI--------------NLKEFQLKWIRsK 480
Cdd:PRK13409 88 FKLYGLPIpKEGKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEE-EPSWDEVlkrfrgtelqnyfkKLYNGEIKVVH-K 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTssikeniayGKenaTVEEIRKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 560
Cdd:PRK13409 166 PQYVDLIPKVFK---------GK---VRELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 561 RILLLDEATSALDAEsERI-VQEALDRIMVNRTTVVVAHRLSTVrnaDMIA-VIH 613
Cdd:PRK13409 232 DFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVL---DYLAdNVH 282
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
730-1000 |
1.66e-11 |
|
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: 66.79 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIKAFFKPPEQLksdTRFWAIIFMLLGV-ASMVVFPAQTIFFS-IAGCKLVQRIRS 807
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL---GLLLGLALLLLGAyLLRALLNFLRIYLNhVAEQKVVADLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 808 MCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGL 887
Cdd:cd18778 78 DLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 888 ngyiymkFMVGFSADAKRMYEEASQVA-------NDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGF- 959
Cdd:cd18778 156 -------GAWLYSKKVRPRYRKVREALgelnallQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHp 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063718281 960 GVSFFVLFSSYAASFYaGARLVDDGKTTFDSVFRVFFALTM 1000
Cdd:cd18778 229 LMEFLTSLGTVLVLGF-GGRLVLAGELTIGDLVAFLLYLGL 268
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
730-996 |
2.30e-11 |
|
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: 66.35 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLNGVILPIFGILISSVIKAFFKPpeqlKSDTRFWAIIFMLLGVASMVVFpaqTIFFSIAGC-----KLVQR 804
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHFITP----GTLDGLTGFILLYLGLILIQAL---SVFLFIRLAgkiemGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 805 IRSMCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPL 884
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKT--PVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 885 IGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVsff 964
Cdd:cd18540 155 LAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPI--- 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1063718281 965 VLFSSYAAS---FYAGARLVDDGKTTFdSVFRVFF 996
Cdd:cd18540 232 VLFLGSIATalvLWYGGILVLAGAITI-GTLVAFI 265
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1068-1260 |
2.43e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.30 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1068 QIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQL-KWLRQQTGLVSQEPVLFN----- 1141
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRrlsvy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1142 ETIRANIAYGKggDATETEIVSAAELSNAHGFISGLQqgyDTMvgerGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSA 1221
Cdd:PRK10895 97 DNLMAVLQIRD--DLSAEQREDRANELMEEFHIEHLR---DSM----GQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1222 LDAES----ERVVQDALDR---VMVN----RTTVVVAHRLSTIKNADVIA 1260
Cdd:PRK10895 168 VDPISvidiKRIIEHLRDSglgVLITdhnvRETLAVCERAYIVSQGHLIA 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
425-619 |
3.24e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.51 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKST---VVSLIERF--YDpqsGEVRIDGinlKEFQLKWIRS--KIGLV--SQE----PVLf 491
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTlmkVLSGVYPHgsYE---GEILFDG---EVCRFKDIRDseALGIViiHQElaliPYL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 492 tsSIKENIAYGKENATV------EEIRKATELanaskfIDKLpqGL----DTMVGEHGTqlsgGQKQRIAVARAILKDPR 561
Cdd:NF040905 94 --SIAENIFLGNERAKRgvidwnETNRRAREL------LAKV--GLdespDTLVTDIGV----GKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 562 ILLLDEATSAL-DAESERIvqeaLDRIMVNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVE 619
Cdd:NF040905 160 LLILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
405-618 |
4.19e-11 |
|
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: 63.82 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 405 LNNVNF-SYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKST----VVSLIERFYDPqSGEVRIDGINLKEFQLKWiRS 479
Cdd:cd03233 6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQE----PVLftssikeniaygkenaTVEEIRKATELANASKFIDKlpqgldtmvgehgtqLSGGQKQRIAVARA 555
Cdd:cd03233 84 EIIYVSEEdvhfPTL----------------TVRETLDFALRCKGNEFVRG---------------ISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 556 ILKDPRILLLDEATSALDAESerivqeALDRIMVNRTtvvVAHRLSTVRNA-------------DMIAVIHQGKIV 618
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSST------ALEILKCIRT---MADVLKTTTFVslyqasdeiydlfDKVLVLYEGRQI 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
422-618 |
5.00e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.97 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLI--ERfyDPQSGEVRIDGINLKEFQ-LKWIRSKIGLVSQEP-----VLfTS 493
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRlgrglVP-DM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 SIKENIA----YGKENATVEEIRKATELANASKFIDKL---PQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLD 566
Cdd:COG3845 352 SVAENLIlgryRRPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 567 EATSALDAES-----ERIVQEA------------LDRIMvnrttvvvahRLStvrnaDMIAVIHQGKIV 618
Cdd:COG3845 428 QPTRGLDVGAiefihQRLLELRdagaavllisedLDEIL----------ALS-----DRIAVMYEGRIV 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
421-613 |
6.88e-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: 66.73 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGFSLSI-SSGSTVALVGQSGSGKSTVVS-----LIERFYDPQSgEVRIDGInLKEFQ-------LKWIRS-------K 480
Cdd:COG1245 88 FRLYGLPVpKKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDE-EPSWDEV-LKRFRgtelqdyFKKLANgeikvahK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 481 IGLVSQEPVLFTssikeniaygkenATVEEI-RKATELANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKD 559
Cdd:COG1245 166 PQYVDLIPKVFK-------------GTVRELlEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 560 PRILLLDEATSALD----AESERIVQEALDRimvNRTTVVVAHRLSTVrnaDMIA-VIH 613
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAIL---DYLAdYVH 283
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1070-1219 |
7.29e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1070 FQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDG--VEIKT----LQLKwL------RQQTGLVSQEP 1137
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSprdaIRAG-IayvpedRKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1138 VLFNETIrANIA-YGKGGdateteIVS-AAELSNAHGFISGLQ---QGYDTMVGergvQLSGGQKQRVAIARAIVKDPKV 1212
Cdd:COG1129 347 IRENITL-ASLDrLSRGG------LLDrRRERALAEEYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKV 415
|
....*..
gi 1063718281 1213 LLLDEAT 1219
Cdd:COG1129 416 LILDEPT 422
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
403-603 |
8.77e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRidginlKEFQLKwirskIG 482
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR-----IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQEPVLFTS---SIKENIAYgKENATVEEIRKATELANASKFIDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKD 559
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063718281 560 PRILLLDEATSALDAESERIVQEALDRIM--VNRTTVVVAHRLSTV 603
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRreLDCAVLMVSHDLHLV 184
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1068-1265 |
9.34e-11 |
|
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: 62.65 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1068 QIFQDLCLSIRAGKTIALVGESGSGKSTVIALL-QRFYDPD-SGQITLDGVEIKtlqlKWLRQQTGLVSQEPVLF-NETI 1144
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLD----KNFQRSTGYVEQQDVHSpNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1145 RaniaygkggdatETEIVSAAelsnahgfisglqqgydtmvgERGvqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDA 1224
Cdd:cd03232 97 R------------EALRFSAL---------------------LRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063718281 1225 ESERVVQDALDRV-MVNRTTVVVAHRLS--TIKNADVIAVVKNG 1265
Cdd:cd03232 142 QAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1043-1235 |
1.06e-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: 65.73 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1043 RVLDNVkgdIELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDgveiKTLQ 1122
Cdd:TIGR03719 317 RLGDKV---IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 LKWLRQqtglvSQEPVLFNETIRANIAYG----KGGDAtetEIVSAAELSnAHGFISGLQQgydTMVGergvQLSGGQKQ 1198
Cdd:TIGR03719 387 LAYVDQ-----SRDALDPNKTVWEEISGGldiiKLGKR---EIPSRAYVG-RFNFKGSDQQ---KKVG----QLSGGERN 450
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063718281 1199 RVAIARAIVKDPKVLLLDEATSALDAESERVVQDALD 1235
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1080-1270 |
1.09e-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: 61.24 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1080 GKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGlvsqepvlfnetiraniaygkggdatet 1159
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1160 eivsaaelsnahgfisglqqgydtmVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMV 1239
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063718281 1240 ------NRTTVVVAHRLSTIKNADVIAVVKNGVIVEK 1270
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1054-1232 |
1.21e-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: 65.73 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1054 LRHISFKYPsrPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITL-DGVEIktlqlkwlrqqtGL 1132
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV------------GY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1133 VSQEPVLFNE-TIRANIAYGKG---GDATETEIVSA----------------AEL------SNAHGFISGLQQGYDTM-- 1184
Cdd:TIGR03719 73 LPQEPQLDPTkTVRENVEEGVAeikDALDRFNEISAkyaepdadfdklaaeqAELqeiidaADAWDLDSQLEIAMDALrc 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1185 -VGERGVQ-LSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES----ERVVQD 1232
Cdd:TIGR03719 153 pPWDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
726-988 |
1.23e-10 |
|
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: 64.03 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 726 EIPMLILGSIAAVLNGVILPIF-GILISSVIkaffkppeqLKSDTR---FWAIIFMLLGVASMVVFPAQTIFFSIAGCKL 801
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLiKIAIDEYI---------PNGDLSgllIIALLFLALNLVNWVASRLRIYLMAKVGQRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 802 VQRIRSMCFEKVVRMEVGWFDETEnsSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAM 881
Cdd:cd18545 72 LYDLRQDLFSHLQKLSFSFFDSRP--VGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 882 LPLIGLngyiymkFMVGFSADAKRMYEEASQ--------VANDAVGsIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGI 953
Cdd:cd18545 150 LPLLVL-------VVFLLRRRARKAWQRVRKkisnlnayLHESISG-IRVIQSFAREDENEEIFDELNRENRKANMRAVR 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063718281 954 VSGI-GFGVSFFVLFSSyAASFYAGARLVDDGKTTF 988
Cdd:cd18545 222 LNALfWPLVELISALGT-ALVYWYGGKLVLGGAITV 256
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
415-576 |
1.35e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 415 RPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLK----EF--QLKWIRSKIGLvsqEP 488
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYhqDLLYLGHQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 489 VLftsSIKENIAY---GKENATVEEIRKATELANASKFIDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLL 565
Cdd:PRK13538 88 EL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWIL 153
|
170
....*....|.
gi 1063718281 566 DEATSALDAES 576
Cdd:PRK13538 154 DEPFTAIDKQG 164
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
381-585 |
1.64e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 381 KRKPEIDASDTTGKVLddirgdIELNNVNFSYParpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSG 460
Cdd:PRK11147 304 TAKMQVEEASRSGKIV------FEMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 461 EVRIdGINLkefqlkwirsKIGLVSQ-----EPvlfTSSIKENIAYGKENATVEEiRKATELANASKFIDKlPQGLDTMV 535
Cdd:PRK11147 375 RIHC-GTKL----------EVAYFDQhraelDP---EKTVMDNLAEGKQEVMVNG-RPRHVLGYLQDFLFH-PKRAMTPV 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063718281 536 gehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALD 585
Cdd:PRK11147 439 ----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1075-1276 |
1.81e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLKWLRQQTGLVSQEPvLFNETIRANIAyg 1151
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddEWRAVRSDIQMIFQDP-LASLNPRMTIG-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1152 kggdatetEIVsAAELSNAHGFISGLQ--QGYDTMVGERGV----------QLSGGQKQRVAIARAIVKDPKVLLLDEAT 1219
Cdd:PRK15079 119 --------EII-AEPLRTYHPKLSRQEvkDRVKAMMLKVGLlpnlinryphEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 1220 SALDAESE-RVVQ--DALDRVMvNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETL 1276
Cdd:PRK15079 190 SALDVSIQaQVVNllQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
81-358 |
1.97e-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: 63.20 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 81 ILGTIGAVGNGLGFPIMTILFGDVIDVFgqnQNSSDVSDKIAKVALkfVYLGLGTLVAALLQVSGWMISGerqAGR---- 156
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDAL---TAGTLTASQLLRYAL--LILLLALLIGIFRFLWRYLIFG---ASRriey 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 157 -IRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVgkaIQLV-STFIGGFVIA--FTEGWLLTLVMVSS 232
Cdd:cd18541 74 dLRNDLFAHLLTLSPSFYQ-KNRTGDLMARATNDLNAVRMALGPGI---LYLVdALFLGVLVLVmmFTISPKLTLIALLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 233 IPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKhLVSAYRA---------GVFEg 303
Cdd:cd18541 150 LPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDK-LNEEYVEknlrlarvdALFF- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 304 astglglGTLNIVIFCTYALAVWYGGKMilekgytggqvliiifaVLTGSMSLGQ 358
Cdd:cd18541 228 -------PLIGLLIGLSFLIVLWYGGRL-----------------VIRGTITLGD 258
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
430-613 |
2.18e-10 |
|
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: 62.77 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 430 SGSTVALVGQSGSGKSTVVSLIE--------RFYDPQSGEVRID---GINLKEF-------QLKWIRsKIGLVSQEPVLF 491
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYftkllegDVKVIV-KPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 492 TSSIKENIAYGKENATVEEIRKATELANaskfidklpqgldtMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSA 571
Cdd:cd03236 104 KGKVGELLKKKDERGKLDELVDQLELRH--------------VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063718281 572 LDA----ESERIVQEaldRIMVNRTTVVVAHRLSTVrnaDMIA-VIH 613
Cdd:cd03236 170 LDIkqrlNAARLIRE---LAEDDNYVLVVEHDLAVL---DYLSdYIH 210
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
731-931 |
3.20e-10 |
|
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: 62.89 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 731 ILGSIAAVLNGVILP-IFGILISSVIkaffkpPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:cd18543 5 LLAALLATLAGLAIPlLTRRAIDGPI------AHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDETEnsSGAIGARLSADAATVRGLVGDALaQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNG 889
Cdd:cd18543 79 FAHLQRLDGAFHDRWQ--SGQLLSRATSDLSLVQRFLAFGP-FLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063718281 890 YIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEE 931
Cdd:cd18543 156 RRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRER 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
423-610 |
3.54e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGS-----TVALVGQSGSGKSTVVSLIERFYDPQSGEVridginlkefqlkwirskiglvsqepvlftsSIKE 497
Cdd:PRK13409 352 DFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------------------------DPEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 498 NIAY------GKENATVEE-IRKATELANASKF---------IDKLpqgLDTMVGEhgtqLSGGQKQRIAVARAILKDPR 561
Cdd:PRK13409 401 KISYkpqyikPDYDGTVEDlLRSITDDLGSSYYkseiikplqLERL---LDKNVKD----LSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 562 ILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLSTVrnaDMIA 610
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
773-942 |
3.59e-10 |
|
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: 62.49 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 773 AIIFM-LLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALA 851
Cdd:cd18589 38 AITVMsLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDS--NQTGDIVSRVTTDTEDMSESLSENLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 852 QTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEE 931
Cdd:cd18589 116 LLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEE 195
|
170
....*....|.
gi 1063718281 932 KVMKMYKKKCE 942
Cdd:cd18589 196 GEAQRYRQRLQ 206
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1056-1257 |
3.64e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1056 HISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQ 1135
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1136 EPVLFNETIRANIAYG---KGGDATETEIVSAAELSNAHGFISGLqqgydtmvgergvqLSGGQKQRVAIARAIVKDPKV 1212
Cdd:PRK13540 83 SGINPYLTLRENCLYDihfSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063718281 1213 LLLDEATSALDaesERVVQDALDRVMVNR----TTVVVAHRLSTIKNAD 1257
Cdd:PRK13540 149 WLLDEPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQDLPLNKAD 194
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
417-617 |
3.98e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRI-DGINLKEF---QLKWIRSkiglvSQEPVLFT 492
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFaqhQLEFLRA-----DESPLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 493 SSIKEniaygkenatveeirKATElanaSKFIDKLP----QGldTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:PRK10636 399 ARLAP---------------QELE----QKLRDYLGgfgfQG--DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063718281 569 TSALDAESERIVQEALdrIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKI 617
Cdd:PRK10636 458 TNHLDLDMRQALTEAL--IDFEGALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
403-621 |
5.88e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYpaRPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEfQLKwiRSKIG 482
Cdd:PRK15056 7 IVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQ--KNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 483 LVSQE-------PVLFtssikENIAYGKENATVEEIRKATelANASKFIDKLPQGLDTMVGEHGT--QLSGGQKQRIAVA 553
Cdd:PRK15056 82 YVPQSeevdwsfPVLV-----EDVVMMGRYGHMGWLRRAK--KRDRQIVTAALARVDMVEFRHRQigELSGGQKKRVFLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 554 RAILKDPRILLLDEATSALDAESE-RIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 621
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
417-625 |
6.64e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 417 EEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQS--GEVRIDGINLKefqlKWIRSKIGLVSQEPVLFTS- 493
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPHl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 SIKENIAYGKENATVEEIRKATELANASKFIDKLpqGL----DTMVGEHGTQ-LSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISEL--GLtkceNTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 569 TSALDAESE-RIVQEALDRIMVNRTTVVVAHRLST--VRNADMIAVIHQGKIVEKGSHSE 625
Cdd:PLN03211 234 TSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1080-1252 |
7.49e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1080 GKTIALVGESGSGKSTVI-ALLQRFYDPD-SGQITLDGVEIKTLQLKwlrqQTGLVSQEPVLFNE-TIRANIAYGK---- 1152
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYPHlTVRETLVFCSllrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1153 GGDATETEIVSAAElsnahGFIS--GLQQGYDTMVGE---RGVqlSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE 1227
Cdd:PLN03211 170 PKSLTKQEKILVAE-----SVISelGLTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180
....*....|....*....|....*.
gi 1063718281 1228 -RVVQDALDRVMVNRTTVVVAHRLST 1252
Cdd:PLN03211 243 yRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
403-581 |
1.30e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEV-RIDGINLKEFQLKWIRski 481
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfRSAKVRMAVFSQHHVD--- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GL-VSQEPVLFTSSIKENIAYGKENATVEEIRKATELAnaskfidklpqgLDTMVgehgtQLSGGQKQRIAVARAILKDP 560
Cdd:PLN03073 584 GLdLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLA------------LQPMY-----TLSGGQKSRVAFAKITFKKP 646
|
170 180
....*....|....*....|..
gi 1063718281 561 RILLLDEATSALDAES-ERIVQ 581
Cdd:PLN03073 647 HILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1077-1273 |
1.31e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1077 IRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDgVEI--KTLQLKwlRQQTGLVSQepVLFNETIRANIAYGKgg 1154
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIsyKPQYIK--PDYDGTVED--LLRSITDDLGSSYYK-- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1155 dateTEIVsaaelsnaHGFisGLQQGYDTMVGErgvqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDAL 1234
Cdd:PRK13409 435 ----SEII--------KPL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063718281 1235 DRVMVNR--TTVVVAHRLSTIknaDVIAvvkNGVIV---EKGKH 1273
Cdd:PRK13409 497 RRIAEEReaTALVVDHDIYMI---DYIS---DRLMVfegEPGKH 534
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1067-1268 |
1.48e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.89 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1067 VQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQL-KWLRQQTGLVSQEPVLFNE-TI 1144
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSRmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1145 RANIAYGkggdateteivsaaelsnahGFISGLQQG-------YDTM--VGERGVQ----LSGGQKQRVAIARAIVKDPK 1211
Cdd:PRK11614 98 EENLAMG--------------------GFFAERDQFqerikwvYELFprLHERRIQragtMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1212 VLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLS--TIKNADVIAVVKNGVIV 1268
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVV 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
403-629 |
1.52e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPArpeEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKW-IRSKI 481
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQE-PVLFTSSIKENIAYGKE------NATVEEIRKATELANASKFIDKLPQGLDTMVGEhgtqLSGGQKQRIAVAR 554
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 555 AILKDPRILLLDEATSAL-DAESERIVQeALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRD 629
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1066-1271 |
1.70e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1066 DVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALlQRFYDPDSGQITLDGVEIKTLQLKwLRQQTG--LVSQEPVLF 1140
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTlskVIAG-HPAYKILEGDILFKGESILDLEPE-ERAHLGifLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1141 NETIRAN---IAYG---KGGDATETEIVSAAELSNAHGFISGLQQGYDTmvgeRGVQ--LSGGQKQRVAIARAIVKDPKV 1212
Cdd:CHL00131 97 PGVSNADflrLAYNskrKFQGLPELDPLEFLEIINEKLKLVGMDPSFLS----RNVNegFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 1213 LLLDEATSALDAESERVVQDALDRVM-VNRTTVVVAH--RLSTIKNADVIAVVKNGVIVEKG 1271
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
772-1002 |
1.79e-09 |
|
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: 60.49 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 772 WAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETENSSgaIGARLSADAATVRGLVGDALA 851
Cdd:cd18548 41 TGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSS--LITRLTNDVTQVQNFVMMLLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 852 QTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEE 931
Cdd:cd18548 119 MLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNRED 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 932 KVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTTFDSV-------FRVFFALTMAA 1002
Cdd:cd18548 199 YEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLS 276
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
423-600 |
1.94e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLKWIRSK----IGLVSQEPVLFTS-SIKE 497
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 498 NIAYGKENAT-VEEIRKATELANASKFIDKL--PQGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSAL-D 573
Cdd:PRK10762 99 NIFLGREFVNrFGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD 174
|
170 180 190
....*....|....*....|....*....|
gi 1063718281 574 AESE---RIVQEALDRimvNRTTVVVAHRL 600
Cdd:PRK10762 175 TETEslfRVIRELKSQ---GRGIVYISHRL 201
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1076-1274 |
1.99e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1076 SIRAGKTIALVGESGSGKS----TVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGlvSQEPVLFNETIRA-NIAY 1150
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVG--AEVAMIFQDPMTSlNPCY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1151 GKGgdateTEIVSAAELSNAHGFISGLQQGYD--TMVG------ERGV---QLSGGQKQRVAIARAIVKDPKVLLLDEAT 1219
Cdd:PRK11022 107 TVG-----FQIMEAIKVHQGGNKKTRRQRAIDllNQVGipdpasRLDVyphQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1220 SALDAESERVVQDALDRVMV--NRTTVVVAHRLSTI-KNADVIAVVKNGVIVEKGKHE 1274
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAH 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1075-1287 |
2.12e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 59.62 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQtGLVS--QEPVLFNETIraniaygk 1152
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQHVRLFREMT-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1153 ggdATETEIVSAAELSNAhGFISGL----------------------QQGYDTMVGERGVQLSGGQKQRVAIARAIVKDP 1210
Cdd:PRK11300 97 ---VIENLLVAQHQQLKT-GLFSGLlktpafrraesealdraatwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1211 KVLLLDEATSALDAESERVVQDALD--RVMVNRTTVVVAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLINIKDGVYASL 1287
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVIKAYL 252
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1065-1226 |
2.67e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1065 PDVQIFQDLCLSIRAGKTIALVGESGSGKSTV---IALLqrfyDPDS-GQITL-DGVEIktlqlkwlrqqtGLVSQEPVL 1139
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLlriMAGV----DKEFeGEARPaPGIKV------------GYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1140 FNE-TIRANI-------------------AYGKGGDATETEIVSAAEL------SNAHGFISGLQQG--------YDTMV 1185
Cdd:PRK11819 82 DPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFDALAAEQGELqeiidaADAWDLDSQLEIAmdalrcppWDAKV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063718281 1186 GergvQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAES 1226
Cdd:PRK11819 162 T----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
423-610 |
3.21e-09 |
|
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: 61.34 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 423 GFSLSISSGS-----TVALVGQSGSGKSTVVSLIERFYDPQSGEVridginlkEFQLKwirskiglvsqepvlftssike 497
Cdd:COG1245 353 GFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK---------------------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 498 nIAY------GKENATVEE-IRKA-TELANASKF---------IDKLpqgLDTMVGEhgtqLSGGQKQRIAVARAILKDP 560
Cdd:COG1245 403 -ISYkpqyisPDYDGTVEEfLRSAnTDDFGSSYYkteiikplgLEKL---LDKNVKD----LSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 561 RILLLDEATSALDAESERIVQEALDRIMVNR--TTVVVAHRLSTVrnaDMIA 610
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1076-1260 |
6.27e-09 |
|
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: 60.18 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1076 SIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDgveiktlqLKwlrqqtglVSQEP----VLFNETIRANI--A 1149
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--------LK--------ISYKPqyisPDYDGTVEEFLrsA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1150 YGKGGDAT--ETEIVSAAelsnahgfisGLQQGYDTMVGErgvqLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESE 1227
Cdd:COG1245 426 NTDDFGSSyyKTEIIKPL----------GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190
....*....|....*....|....*....|....*
gi 1063718281 1228 RVVQDALDRVMVNR--TTVVVAHRLSTIknaDVIA 1260
Cdd:COG1245 492 LAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
407-615 |
6.29e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.25 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 407 NVNFSYP-ARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTV---------VSLIErfydpqsGEVRIDGINLKE-FQlk 475
Cdd:cd03232 8 NLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLldvlagrktAGVIT-------GEILINGRPLDKnFQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 476 wiRSkIGLVSQEPVLFtssikeniaygkENATVEEirkatelanASKFIDKLpQGldtmvgehgtqLSGGQKQRIAVARA 555
Cdd:cd03232 79 --RS-TGYVEQQDVHS------------PNLTVRE---------ALRFSALL-RG-----------LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRI-MVNRTTVVVAHRLSTV--RNADMIAVIHQG 615
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
156-351 |
7.00e-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: 58.61 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 156 RIRSLYLQTILRQDIAFFDVeTNTGEVVGRMSgDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPL 235
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFET-RKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 236 LVMSGAALAIVISKMASRGQTSYAK-AAVVVEqTVGSIRTVASFTGEKQAI----SNYNKHLVSAYRAGVFE---GASTG 307
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAElNSYLIE-SLKGIETIKSLNAEEQFLkkieKKFSKLLKKSFKLGKLSnlqSSIKG 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063718281 308 LGLGTLNIVIFctyalavWYGGKMILEKGYTGGQvLIIIFAVLT 351
Cdd:cd18570 233 LISLIGSLLIL-------WIGSYLVIKGQLSLGQ-LIAFNALLG 268
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
430-610 |
1.05e-08 |
|
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: 55.46 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 430 SGSTVALVGQSGSGKSTVVSLIERFYDPQSGEV-RIDGINLKEFQLKWIRskiglvsqepvlftssikeniaygkenatv 508
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 509 eeirkatelanaskfidklpqglDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALD--- 585
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180
....*....|....*....|....*....
gi 1063718281 586 ----RIMVNRTTVVVAHRLSTVRNADMIA 610
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1070-1223 |
1.19e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1070 FQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQ--------LKWL---RQQTGLVSQEPV 1138
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlargLVYLpedRQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 LFNetiraniaygkggdateteiVSAAeLSNAHGFIsgLQQGYDTMVGER-----GVQ----------LSGGQKQRVAIA 1203
Cdd:PRK15439 359 AWN--------------------VCAL-THNRRGFW--IKPARENAVLERyrralNIKfnhaeqaartLSGGNQQKVLIA 415
|
170 180
....*....|....*....|
gi 1063718281 1204 RAIVKDPKVLLLDEATSALD 1223
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVD 435
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1041-1254 |
1.26e-08 |
|
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: 59.38 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1041 SGRVLDNVKGdIELRHISFKYPSRpDVQIfQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveikt 1120
Cdd:TIGR00954 442 RGIVEYQDNG-IKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1121 lqlkwlRQQTGLVSQEPVLFNETIRANIAYGKGGDATETEIVSAAEL----SNAH-GFISGLQQGYDTMVGERGVqLSGG 1195
Cdd:TIGR00954 514 ------KGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLeqilDNVQlTHILEREGGWSAVQDWMDV-LSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 1196 QKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRvmVNRTTVVVAHRLSTIK 1254
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
403-598 |
2.01e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYdPQ--------------SGEVRIDgin 468
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQgysndltlfgrrrgSGETIWD--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 469 lkefqlkwIRSKIGLVSQEPVL---FTSSIKENI------AYGKENATVEEIRKAtelanASKFIDKLpqGLDTMVGEHG 539
Cdd:PRK10938 334 --------IKKHIGYVSSSLHLdyrVSTSVRNVIlsgffdSIGIYQAVSDRQQKL-----AQQWLDIL--GIDKRTADAP 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 540 TQ-LSGGQkQRIA-VARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTT--VVVAH 598
Cdd:PRK10938 399 FHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSH 460
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1057-1247 |
2.43e-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: 55.73 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1057 ISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKST---VIALLQRFYDPDSGQITLDGVEIKTlqlkwlrqqtglv 1133
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKE------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1134 sqepvlFNETIRANIAYGKGGD---ATET--EIVSAAELSNAHGFISGlqqgydtmvgergvqLSGGQKQRVAIARAIVK 1208
Cdd:cd03233 77 ------FAEKYPGEIIYVSEEDvhfPTLTvrETLDFALRCKGNEFVRG---------------ISGGERKRVSIAEALVS 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063718281 1209 DPKVLLLDEATSALDAEServvqdALD-----RVMVN--RTTVVVA 1247
Cdd:cd03233 136 RASVLCWDNSTRGLDSST------ALEilkciRTMADvlKTTTFVS 175
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
78-354 |
2.56e-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: 57.11 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 78 ILMILGTIgAVGNGLGfPIMTILFGDVID--VFGQNQNSsdvsdkiakvalkFVYLGLGTLVAALLQ-----VSGWMIS- 149
Cdd:cd18550 1 LALVLLLI-LLSALLG-LLPPLLLREIIDdaLPQGDLGL-------------LVLLALGMVAVAVASallgvVQTYLSAr 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 150 -GERQAGRIR-SLY--LQtilRQDIAFFdVETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLL 225
Cdd:cd18550 66 iGQGVMYDLRvQLYahLQ---RMSLAFF-TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 226 TLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQT--VGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEG 303
Cdd:cd18550 142 ALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 304 ASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQvlIIIFAVLTGSM 354
Cdd:cd18550 222 LAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGT--LVAFTALLGRL 270
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
731-1000 |
2.95e-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: 56.69 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 731 ILGSIAAVLNGVILPIF-GILISSVIkaffkpPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:cd18570 8 LLLSLLITLLGIAGSFFfQILIDDII------PSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFDETEnsSGAIGARLSaDAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNG 889
Cdd:cd18570 82 FKHLLKLPLSFFETRK--TGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILII 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 890 YIYMKFMVgfSADAKRMYEEASQVAN--DAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLF 967
Cdd:cd18570 159 LLFNKPFK--KKNREVMESNAELNSYliESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISL 236
|
250 260 270
....*....|....*....|....*....|...
gi 1063718281 968 SSYAASFYAGARLVDDGKTTFDSVFrVFFALTM 1000
Cdd:cd18570 237 IGSLLILWIGSYLVIKGQLSLGQLI-AFNALLG 268
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1054-1253 |
2.98e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1054 LRHIsFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKST---VIAL-LQRFYDPDSGQITLDGV---EIKtlqlKWL 1126
Cdd:TIGR00956 62 FRKL-KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTllkTIASnTDGFHIGVEGVITYDGItpeEIK----KHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1127 RQQTGLVSQEPVLF-----NETIRANIAYGKGGDATE--TEIVSAAELSNAHGFISGLQQGYDTMVGE---RGVqlSGGQ 1196
Cdd:TIGR00956 137 RGDVVYNAETDVHFphltvGETLDFAARCKTPQNRPDgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGE 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSALDAEServvqdALDRVMVNRTTVVVAHRLSTI 1253
Cdd:TIGR00956 215 RKRVSIAEASLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1063-1225 |
3.28e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1063 SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQ----LKWLRQQTGLVSQEPV 1138
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrsrfMAYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 LfnetirANIAYGKGGDATETEIVSAAELSnahgfISGLQQGYDTMVGergvQLSGGQKQRVAIARAIVKDPKVLLLDEA 1218
Cdd:PRK13543 100 L------ENLHFLCGLHGRRAKQMPGSALA-----IVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*..
gi 1063718281 1219 TSALDAE 1225
Cdd:PRK13543 165 YANLDLE 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1036-1250 |
4.51e-08 |
|
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: 58.10 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1036 DPSDESGRVLDN-VKGDI-ELRHISFKYP--SRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQI 1111
Cdd:TIGR01257 1920 DVAEERQRIISGgNKTDIlRLNELTKVYSgtSSPAVD---RLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDA 1996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1112 TLDGVEIKTlQLKWLRQQTGLVSQ----EPVLFNETIRANIAYGKGGDATETEIVSAAELSNAhgfisGLQQGYDTMVGe 1187
Cdd:TIGR01257 1997 TVAGKSILT-NISDVHQNMGYCPQfdaiDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSL-----GLSLYADRLAG- 2069
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1188 rgvQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN-RTTVVVAHRL 1250
Cdd:TIGR01257 2070 ---TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSM 2130
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
400-598 |
5.87e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 400 RGDIELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVridginlkefqlKWI-R 478
Cdd:PRK15064 317 RNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 479 SKIGLVSQEPvlftssikeniaygkenatveeirkATELANASKFID-----KLPQGLDTMV-GEHG------------- 539
Cdd:PRK15064 382 ANIGYYAQDH-------------------------AYDFENDLTLFDwmsqwRQEGDDEQAVrGTLGrllfsqddikksv 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 540 TQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDriMVNRTTVVVAH 598
Cdd:PRK15064 437 KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSH 493
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
77-354 |
6.07e-08 |
|
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: 55.87 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGNGLGFPIMTilfGDVIDVFGQNQNSSDvsdkIAKVALKFVYLGLGTLVAALLqvSGWMIS--GERQA 154
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLM---ADIIDEGIANGDLSY----ILRTGLLMLLLALLGLIAGIL--AGYFAAkaSQGFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 155 GRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAmgekVGKAIQLVS----TFIGGFVIAFTEGWLLTLVMV 230
Cdd:cd18548 72 RDLRKDLFEKIQSFSFAEID-KFGTSSLITRLTNDVTQVQNF----VMMLLRMLVrapiMLIGAIIMAFRINPKLALILL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 231 SSIPLLVmsgAALAIVISKMA---SRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTG 307
Cdd:cd18548 147 VAIPILA---LVVFLIMKKAIplfKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 308 LGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQV-------LIIIFAVLTGSM 354
Cdd:cd18548 224 LLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1078-1262 |
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 1063718281 1078 RAGKTIALVGESGSGKSTVIALLQ--------RFYDPDSGQITLDGVEIKTLQ--LKWLRQQTGLVSQEPVLFNETIRAn 1147
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDEFRGSELQnyFTKLLEGDVKVIVKPQYVDLIPKA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1148 iAYGKGGDATET--------EIVSAAELSNahgfisglqqgydtmVGERGV-QLSGGQKQRVAIARAIVKDPKVLLLDEA 1218
Cdd:cd03236 103 -VKGKVGELLKKkdergkldELVDQLELRH---------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063718281 1219 TSALDAEsERVVQDALDRVMV--NRTTVVVAHRLSTIKN-ADVIAVV 1262
Cdd:cd03236 167 SSYLDIK-QRLNAARLIRELAedDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
403-646 |
7.47e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARpeeQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKE-FQLKWIRSKI 481
Cdd:NF033858 2 ARLEGVSHRYGKT---VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADaRHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQ------EPVLftsSIKENIAY--------GKE-NATVEEIRKATELAnasKFIDKlPQGldtmvgehgtQLSGGQ 546
Cdd:NF033858 79 AYMPQglgknlYPTL---SVFENLDFfgrlfgqdAAErRRRIDELLRATGLA---PFADR-PAG----------KLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 547 KQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRT--TVVVAhrlstvrNADM--------IAVIHQGK 616
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVA-------TAYMeeaerfdwLVAMDAGR 214
|
250 260 270
....*....|....*....|....*....|....*
gi 1063718281 617 IVEKGSHSELLR-----DPEGAYsqlIRLQEDTKQ 646
Cdd:NF033858 215 VLATGTPAELLArtgadTLEAAF---IALLPEEKR 246
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1052-1231 |
7.77e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQItldgveiktlqLKWLRQQTG 1131
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEPVlfnetiraniaygKGGDATETEIvsaaeLSNAHGFISGLQQGYDTMVGERGVQ----------LSGGQKQRVA 1201
Cdd:PLN03073 576 VFSQHHV-------------DGLDLSSNPL-----LYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVA 637
|
170 180 190
....*....|....*....|....*....|.
gi 1063718281 1202 IARAIVKDPKVLLLDEATSALDAES-ERVVQ 1231
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
421-617 |
9.88e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGFSLSISSGSTVALVGQSGSGKStvvSLIERFY---DPQSGEVRIDGINLKEFQLKwIRSKIGLV-----SQEPVLF- 491
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 492 -------TSSIKEN-----IAYGKENATVEEIRKATELanasKFidklpqgldtmvgEHGTQ----LSGGQKQRIAVARA 555
Cdd:PRK15439 355 daplawnVCALTHNrrgfwIKPARENAVLERYRRALNI----KF-------------NHAEQaartLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKI 617
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
767-973 |
1.03e-07 |
|
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: 55.20 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 767 SDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLV 846
Cdd:cd18580 36 SSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTT--PSGRILNRFSKDIGLIDEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 847 GDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIglngYIYMKFMVGFSADAKRMYEEA-----SQVaNDAVGSI 921
Cdd:cd18580 114 PLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVY----YLLQRYYLRTSRQLRRLESESrsplySHF-SETLSGL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 922 RTVASFCAEEKVMKMYKKKCEGPMRT-----------GIR-QGIVSGIGFGVSFFVLFSSYAAS 973
Cdd:cd18580 189 STIRAFGWQERFIEENLRLLDASQRAfylllavqrwlGLRlDLLGALLALVVALLAVLLRSSIS 252
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1052-1274 |
1.14e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQItldgveiktlqlKWlrqqtg 1131
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 lvsqepvlfneTIRANIAYgkggdateteivsAAElSNAHGFISGL----------QQGYD-TMVgeRGV---------- 1190
Cdd:PRK15064 379 -----------SENANIGY-------------YAQ-DHAYDFENDLtlfdwmsqwrQEGDDeQAV--RGTlgrllfsqdd 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1191 ------QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDrvMVNRTTVVVAH------RLSTiknaDV 1258
Cdd:PRK15064 432 ikksvkVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHdrefvsSLAT----RI 505
|
250
....*....|....*.
gi 1063718281 1259 IAVVKNGVIVEKGKHE 1274
Cdd:PRK15064 506 IEITPDGVVDFSGTYE 521
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
422-609 |
1.23e-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: 54.54 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVV------SLIERFY--DPQSGEV-RIDGINLKEfqlkwirsKIGLVSQEPV--- 489
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHlkKEQPGNHdRIEGLEHID--------KVIVIDQSPIgrt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 490 ----------LFTSsIKE----------------NIAY-GKENA-----TVEEirkatelanASKFIDKLPQ-------- 529
Cdd:cd03271 84 prsnpatytgVFDE-IRElfcevckgkrynretlEVRYkGKSIAdvldmTVEE---------ALEFFENIPKiarklqtl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 530 ---GLDTM-VGEHGTQLSGGQKQRIAVARAILKDPR---ILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLS 601
Cdd:cd03271 154 cdvGLGYIkLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLD 233
|
....*...
gi 1063718281 602 TVRNADMI 609
Cdd:cd03271 234 VIKCADWI 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
403-617 |
1.29e-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: 55.99 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQ-SGEVRIDG--INLKEFQlKWIRS 479
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPA-QAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 480 KIGLVSQE-------PVLFT------SSIKENIAYGKENATVEE--IRKATELANASKFIDKLPQGldtmvgehgtQLSG 544
Cdd:TIGR02633 337 GIAMVPEDrkrhgivPILGVgknitlSVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 545 GQKQRIAVARAILKDPRILLLDEATSALD----AESERIV-QEALDRIMVnrttVVVAHRLSTVRN-ADMIAVIHQGKI 617
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDvgakYEIYKLInQLAQEGVAI----IVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
424-629 |
1.96e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 424 FSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlKEFQLK----WIRSKIGLV----SQEPVLFTSSI 495
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRsprdAIRAGIMLCpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 496 KENI---AYGKENATVEEIRKATELANASKFIDKL----PQGlDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEA 568
Cdd:PRK11288 349 ADNInisARRHHLRAGCLINNRWEAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 569 TSALD--AESE--RIVQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVekgshSELLRD 629
Cdd:PRK11288 424 TRGIDvgAKHEiyNVIYELAAQ---GVAVLFVSSDLPEVLGvADRIVVMREGRIA-----GELARE 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
419-601 |
2.13e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 419 QIFRGFSLSISSGSTVALVGQSGSGKSTVVSL---------IErfydpqsGEVRIDGINLKEFQLKWIRskiGLVSQ--- 486
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVlagrktggyIE-------GDIRISGFPKKQETFARIS---GYCEQndi 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 487 --------EPVLFTSSIKENIAYGKENAT--VEEIRKATELANASkfidklpqglDTMVGEHG-TQLSGGQKQRIAVARA 555
Cdd:PLN03140 964 hspqvtvrESLIYSAFLRLPKEVSKEEKMmfVDEVMELVELDNLK----------DAIVGLPGvTGLSTEQRKRLTIAVE 1033
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063718281 556 ILKDPRILLLDEATSALDAESERIVQEAL-DRIMVNRTTVVVAHRLS 601
Cdd:PLN03140 1034 LVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
401-617 |
2.42e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 401 GDI--ELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQS-GEVRIDGINLK-EFQLKW 476
Cdd:PRK13549 256 GEVilEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKiRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 477 IRSKIGLVSQE-------PVLftsSIKENI--AYGKENATVEEIRKATELANASKFIDKL---PQGLDTMVGehgtQLSG 544
Cdd:PRK13549 336 IAQGIAMVPEDrkrdgivPVM---GVGKNItlAALDRFTGGSRIDDAAELKTILESIQRLkvkTASPELAIA----RLSG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 545 GQKQRIAVARAILKDPRILLLDEATSALD--AESE------RIVQEALDRIMvnrttvvVAHRLSTVRN-ADMIAVIHQG 615
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyklinQLVQQGVAIIV-------ISSELPEVLGlSDRVLVMHEG 481
|
..
gi 1063718281 616 KI 617
Cdd:PRK13549 482 KL 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1077-1262 |
2.95e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1077 IRAGKTIALVGESGSGKSTVIALLqrfydpdSGQIT--LDGVEIKTlqlKW---LRQQTGLVSQEPV--LFNETIRA--N 1147
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIpnLGDYEEEP---SWdevLKRFRGTELQNYFkkLYNGEIKVvhK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1148 IAY---------GKGGDATET--------EIVSAAELSNahgfisglqqgydtmVGERGV-QLSGGQKQRVAIARAIVKD 1209
Cdd:PRK13409 166 PQYvdlipkvfkGKVRELLKKvdergkldEVVERLGLEN---------------ILDRDIsELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1210 PKVLLLDEATSALDAEsERV-VQDALDRVMVNRTTVVVAHRLSTIKN-ADVIAVV 1262
Cdd:PRK13409 231 ADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
391-601 |
3.34e-07 |
|
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: 54.75 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 391 TTGKVLDDIRGdIELNNVNFSYPArpEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlk 470
Cdd:TIGR00954 441 GRGIVEYQDNG-IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA---- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 471 efqlkwiRSKIGLVSQEPVLFTSSIKENIAY----------GKENATVEEIRKATELANaskfIDKLPQGLDTmVGEHGT 540
Cdd:TIGR00954 514 -------KGKLFYVPQRPYMTLGTLRDQIIYpdssedmkrrGLSDKDLEQILDNVQLTH----ILEREGGWSA-VQDWMD 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 541 QLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRimVNRTTVVVAHRLS 601
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1076-1223 |
3.38e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1076 SIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveikTLQLKWLRQQTGLVSQepvlfnetirANIAYGKGGD 1155
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQLAWVNQETPALPQ----------PALEYVIDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1156 ----ATETEIVSAAELSNAHGfISGLQQGYDTM---------------VGERGVQL-------SGGQKQRVAIARAIVKD 1209
Cdd:PRK10636 89 reyrQLEAQLHDANERNDGHA-IATIHGKLDAIdawtirsraasllhgLGFSNEQLerpvsdfSGGWRMRLNLAQALICR 167
|
170
....*....|....
gi 1063718281 1210 PKVLLLDEATSALD 1223
Cdd:PRK10636 168 SDLLLLDEPTNHLD 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
403-585 |
4.72e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 403 IELNNVNFSYPARPeeqIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRI-DGInlkefqlkwirsKI 481
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 482 GLVSQEpvlftssiKENIAYGKenaTV-EEIRKATEL-----------ANASKFIDKlpqGLD--TMVGehgtQLSGGQK 547
Cdd:TIGR03719 388 AYVDQS--------RDALDPNK---TVwEEISGGLDIiklgkreipsrAYVGRFNFK---GSDqqKKVG----QLSGGER 449
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063718281 548 QRIAVARAILKDPRILLLDEATSALDAESERIVQEALD 585
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1050-1223 |
5.16e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1050 GDI--ELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKS-TVIALLQRFYDPDSGQITLDG--VEIKTLQ-- 1122
Cdd:PRK13549 256 GEVilEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIRNPQqa 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 -------LKWLRQQTGLVSQEPVLFNETIRANIAYGKGGdatetEIVSAAELSNAHGFISGLQqgYDTMVGERGV-QLSG 1194
Cdd:PRK13549 336 iaqgiamVPEDRKRDGIVPVMGVGKNITLAALDRFTGGS-----RIDDAAELKTILESIQRLK--VKTASPELAIaRLSG 408
|
170 180
....*....|....*....|....*....
gi 1063718281 1195 GQKQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1052-1223 |
5.31e-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: 53.68 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKS-TVIALLQRFYDPDSGQITLDG--VEIKTLQ------ 1122
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGkpVDIRNPAqairag 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 ---LKWLRQQTGLVSQEPVLFNETIRANIAYgkggdATETEIVSAAELSNAHGFISGLQ---QGYDTMVGergvQLSGGQ 1196
Cdd:TIGR02633 338 iamVPEDRKRHGIVPILGVGKNITLSVLKSF-----CFKMRIDAAAELQIIGSAIQRLKvktASPFLPIG----RLSGGN 408
|
170 180
....*....|....*....|....*..
gi 1063718281 1197 KQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
77-333 |
8.49e-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: 52.15 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGNGLGFPIMTilfGDVIDVFGQNQNSSDVSDKIAKVALkFVYLG---LGTLVAALLQVSGWMISGErq 153
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLI---RELVDLVTIGSKSLGLLLGLALLLL-GAYLLralLNFLRIYLNHVAEQKVVAD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 154 agrIRS-LYlQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSS 232
Cdd:cd18778 75 ---LRSdLY-DKLQRLSLRYFD-DRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 233 IPLLVMSGAALAIVISKMASRGQTSYAK-AAVVVEQTVGsIRTVASFTGEKQA---ISNYNKHLVSA------YRAGVFE 302
Cdd:cd18778 150 IPFLALGAWLYSKKVRPRYRKVREALGElNALLQDNLSG-IREIQAFGREEEEakrFEALSRRYRKAqlramkLWAIFHP 228
|
250 260 270
....*....|....*....|....*....|.
gi 1063718281 303 GASTGLGLGTLnivifctyaLAVWYGGKMIL 333
Cdd:cd18778 229 LMEFLTSLGTV---------LVLGFGGRLVL 250
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
396-617 |
8.96e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 396 LDDIRGDIELNNVNFSYPArpeeqiFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--INLKEFQ 473
Cdd:PRK10762 249 LDKAPGEVRLKVDNLSGPG------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 474 ------LKWI---RSKIGLVsqepvlFTSSIKENI---AYGKENATVEEIRKATELANASKFID----KLPqGLDTMVGE 537
Cdd:PRK10762 323 dglangIVYIsedRKRDGLV------LGMSVKENMsltALRYFSRAGGSLKHADEQQAVSDFIRlfniKTP-SMEQAIGL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 538 hgtqLSGGQKQRIAVARAILKDPRILLLDEATSALD--AESE------RIVQEALDRIMVNRTTVVVahrlstVRNADMI 609
Cdd:PRK10762 396 ----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgAKKEiyqlinQFKAEGLSIILVSSEMPEV------LGMSDRI 465
|
....*...
gi 1063718281 610 AVIHQGKI 617
Cdd:PRK10762 466 LVMHEGRI 473
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
768-906 |
1.04e-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: 52.08 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 768 DTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVG 847
Cdd:cd18604 41 SVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTT--PVGRILNRFSKDIETIDSELA 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 848 DALAQTVQNLASVTAGLVIAFVASWqlAFIVLAmLPLIGLNGYIYMKFMVGfSADAKRM 906
Cdd:cd18604 119 DSLSSLLESTLSLLVILIAIVVVSP--AFLLPA-VVLAALYVYIGRLYLRA-SRELKRL 173
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
77-344 |
1.18e-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: 51.70 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 77 IILMILGTIGAVGNGLGFPImtiLFGDVIDVFGQNQNSSDvsdkIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAGR 156
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPY---LIKIAIDEYIPNGDLSG----LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 157 IRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLL 236
Cdd:cd18545 75 LRQDLFSHLQKLSFSFFD-SRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 237 VmsgaALAIVISKMASRG-QTSYAKAAVV---VEQTVGSIRTVASFTGEKQAISNY----NKHLVSAYRAGVFEGA---- 304
Cdd:cd18545 154 V----LVVFLLRRRARKAwQRVRKKISNLnayLHESISGIRVIQSFAREDENEEIFdelnRENRKANMRAVRLNALfwpl 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063718281 305 ---STGLGlgtlnivifctYALAVWYGGKMILEKGYTGGqVLI 344
Cdd:cd18545 230 velISALG-----------TALVYWYGGKLVLGGAITVG-VLV 260
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1063-1222 |
1.18e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1063 SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLK-WLRQQTGLVSQEPVLFN 1141
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1142 E-TIRANIAYGKGgdATETEIVSAAELSNAHGFISGlQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATS 1220
Cdd:PRK10982 87 QrSVMDNMWLGRY--PTKGMFVDQDKMYRDTKAIFD-ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
..
gi 1063718281 1221 AL 1222
Cdd:PRK10982 164 SL 165
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1066-1248 |
1.43e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1066 DVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITL-DGVEIKTL---QLKWLRQQTG----LVSQEP 1137
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFaqhQLEFLRADESplqhLARLAP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1138 VLFNETIRANI-AYGKGGDAteteivsaaelsnahgfisglqqgydtmVGERGVQLSGGQKQRVAIARAIVKDPKVLLLD 1216
Cdd:PRK10636 404 QELEQKLRDYLgGFGFQGDK----------------------------VTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|..
gi 1063718281 1217 EATSALDAESERVVQDALdrVMVNRTTVVVAH 1248
Cdd:PRK10636 456 EPTNHLDLDMRQALTEAL--IDFEGALVVVSH 485
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1075-1226 |
1.46e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLD--------------------------GVEIKTLQLKWLRQ 1128
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprnvegtvydfvaeGIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFN----ETIRANIAYgKGGDATETEIVSAAELsnahgfisgLQQGYDTMVGErgvqLSGGQKQRVAIAR 1204
Cdd:PRK11147 104 ISHLVETDPSEKNlnelAKLQEQLDH-HNLWQLENRINEVLAQ---------LGLDPDAALSS----LSGGWLRKAALGR 169
|
170 180
....*....|....*....|..
gi 1063718281 1205 AIVKDPKVLLLDEATSALDAES 1226
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
165-331 |
1.56e-06 |
|
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: 51.30 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 165 ILRQDIAFFDvETNTGEVVGRMSGDTVLIqdamGEKVGKA-----IQLVsTFIGGFVIAFTEGWLLTLVMVSSIPLLvms 239
Cdd:cd18549 85 LQKLSFSFFD-NNKTGQLMSRITNDLFDI----SELAHHGpedlfISII-TIIGSFIILLTINVPLTLIVFALLPLM--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 240 gAALAIVIS-KMASRGQTSYAKAAVV---VEQTVGSIRTVASFTGEKQAISNY---NKHLVSA----YRAGVFEGASTGL 308
Cdd:cd18549 156 -IIFTIYFNkKMKKAFRRVREKIGEInaqLEDSLSGIRVVKAFANEEYEIEKFdegNDRFLESkkkaYKAMAYFFSGMNF 234
|
170 180
....*....|....*....|...
gi 1063718281 309 GLGTLNIVIFCTYALAVwYGGKM 331
Cdd:cd18549 235 FTNLLNLVVLVAGGYFI-IKGEI 256
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
422-621 |
1.81e-06 |
|
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: 49.63 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSliERFYdpQSGEVRIDGiNLKEFqlkwirskiglvSQEPVLFTSSIKENIAY 501
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLIS-FLPKF------------SRNKLIFIDQLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 502 GKENATveeirkatelanaskfidkLPQGLDTmvgehgtqLSGGQKQRIAVARAILKDPR--ILLLDEATSALDAESERI 579
Cdd:cd03238 75 GLGYLT-------------------LGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063718281 580 VQEALDRIMVNRTTV-VVAHRLSTVRNADMI------AVIHQGKIVEKG 621
Cdd:cd03238 128 LLEVIKGLIDLGNTViLIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1071-1278 |
2.45e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.24 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQqTGLV----SQ----EPVLfnE 1142
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQlwwdLPAI--D 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1143 TIRANIA-YGkggdateteiVSAAEL-SNAHGFISGLQQG--YDTMVgeRgvQLSGGQKQRVAIARAIVKDPKVLLLDEA 1218
Cdd:COG4586 116 SFRLLKAiYR----------IPDAEYkKRLDELVELLDLGelLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 1219 TSALDAESERVVQDALDRvmVNR---TTVVVA-HRLSTIKN-ADVIAVVKNGVIVEKGKHETLIN 1278
Cdd:COG4586 182 TIGLDVVSKEAIREFLKE--YNRergTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
416-622 |
2.51e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 416 PEEQIFRGFSLSISSGSTVALVGQSGSGKST----VVSLIERFYDPQSGEVRIDGINLKEFQlKWIRSKIGLVSQEPVLF 491
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIK-KHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 492 TS-SIKENIAYGKENATVE-EIRKATELANASKFID------KLPQGLDTMVGEHGTQ-LSGGQKQRIAVARAILKDPRI 562
Cdd:TIGR00956 151 PHlTVGETLDFAARCKTPQnRPDGVSREEYAKHIADvymatyGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 563 LLLDEATSALDAESerivqeALDRIMVNRTTVVVAHRLSTV------RNA----DMIAVIHQGKIVEKGS 622
Cdd:TIGR00956 231 QCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGP 294
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1051-1278 |
2.79e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.96 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1051 DIELRHISFKYPSRPdVQIFQDLCLSIRAGKTIALVGESGSGKStVIALLQRFYDPDSGQITLDGV---EIKTLQL---- 1123
Cdd:PRK15093 5 DIRNLTIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKS-LIAKAICGVTKDNWRVTADRMrfdDIDLLRLspre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1124 --KWLRQQTGLVSQEP-----------VLFNETIRANIAYGKGGDATETEIVSAAELSNAhgfiSGLQQGYDTMvGERGV 1190
Cdd:PRK15093 83 rrKLVGHNVSMIFQEPqscldpservgRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHR----VGIKDHKDAM-RSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1191 QLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVV--VAHRLSTI-KNADVIAVVKNGVI 1267
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLsQWADKINVLYCGQT 237
|
250
....*....|.
gi 1063718281 1268 VEKGKHETLIN 1278
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
425-631 |
3.04e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefQLKWIRSKIGLVSQEPVLftssikENIAYgke 504
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQLTGI------ENIEF--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 505 natveeirKATELANASKFIDKL-PQGLD-TMVGEHGTQ----LSGGQKQRIAVARAILKDPRILLLDEATSALDaesER 578
Cdd:PRK13546 109 --------KMLCMGFKRKEIKAMtPKIIEfSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 579 IVQEALDRIM----VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHSELLRDPE 631
Cdd:PRK13546 178 FAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1075-1287 |
3.46e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTL---QLK------WLRQQTGLVSQEPVLFNETIR 1145
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfeQLQklvsdeWQRNNTDMLSPGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1146 aniaygkggdatetEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAE 1225
Cdd:PRK10938 104 --------------EIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 1226 SERVVQDALDRVMVNRTTVV-VAHRLSTIKN-ADVIAVVKNGVIVEKGKHETLINikDGVYASL 1287
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ--QALVAQL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1191-1262 |
4.26e-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: 50.94 E-value: 4.26e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 1191 QLSGGQKQRVAIARAIVKDPKVLLLDEATSALD----AESERVVQDALDRvmvNRTTVVVAHRLSTI-KNADVIAVV 1262
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAILdYLADYVHIL 285
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
424-606 |
5.13e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 424 FSLSIS--SGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQ---LKWIRSKIGLVSQEPVLftssikEN 498
Cdd:PRK13541 17 FDLSITflPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLEMTVF------EN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 499 IAYGKEnatveeIRKATELANASKFIDKLPQGLDtmvgEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 578
Cdd:PRK13541 91 LKFWSE------IYNSAETLYAAIHYFKLHDLLD----EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180 190
....*....|....*....|....*....|
gi 1063718281 579 IVQEaLDRIMVNRTTVVV--AHRLSTVRNA 606
Cdd:PRK13541 161 LLNN-LIVMKANSGGIVLlsSHLESSIKSA 189
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
398-576 |
5.47e-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: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 398 DIRGDI-ELNNVNFSYPARPEE-QIFRGFSLSISSGSTVALVGQSGSGKSTVVS-LIERFYDP--QSGEVRIDGINLKE- 471
Cdd:TIGR00956 754 ESGEDIfHWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVTTGviTGGDRLVNGRPLDSs 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 472 FQlkwiRSkIGLVSQEPV-LFTSSIKENIAYGKEnatveeIRKATELANASK--FIDKLPQGL------DTMVGEHGTQL 542
Cdd:TIGR00956 834 FQ----RS-IGYVQQQDLhLPTSTVRESLRFSAY------LRQPKSVSKSEKmeYVEEVIKLLemesyaDAVVGVPGEGL 902
|
170 180 190
....*....|....*....|....*....|....*
gi 1063718281 543 SGGQKQRIAVARAILKDPRILL-LDEATSALDAES 576
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1052-1235 |
5.90e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLdGveiKTLQLkwlrqqtG 1131
Cdd:PRK11819 325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G---ETVKL-------A 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1132 LVSQEpvlfnetiRANIAYGK-------GGDAT----ETEIVSAAELSnAHGFISGLQQgydTMVGergvQLSGGQKQRV 1200
Cdd:PRK11819 391 YVDQS--------RDALDPNKtvweeisGGLDIikvgNREIPSRAYVG-RFNFKGGDQQ---KKVG----VLSGGERNRL 454
|
170 180 190
....*....|....*....|....*....|....*
gi 1063718281 1201 AIARAIVKDPKVLLLDEATSALDAESERVVQDALD 1235
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
507-626 |
6.06e-06 |
|
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: 50.78 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 507 TVEEirkatelanASKFIDKLP---QGLDTMV---------GEHGTQLSGGQKQRIAVARAILKD---PRILLLDEATSA 571
Cdd:TIGR00630 792 TVEE---------AYEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTG 862
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063718281 572 LDAESERIVQEALDRIMVNRTTVVV-AHRLSTVRNADMIAVI------HQGKIVEKGSHSEL 626
Cdd:TIGR00630 863 LHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1052-1259 |
6.43e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRpdvQIFqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQ---LKWLRQ 1128
Cdd:PRK13541 2 LSLHQLQFNIEQK---NLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1129 QTGLVSQEPVLFNETIRANIAygkggDATETeIVSAAELSNAHGFISglqqgydtmvgERGVQLSGGQKQRVAIARAIVK 1208
Cdd:PRK13541 78 NLGLKLEMTVFENLKFWSEIY-----NSAET-LYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIAC 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063718281 1209 DPKVLLLDEATSALDAESERVVQDaLDRVMVNRTTVVV--AHRLSTIKNADVI 1259
Cdd:PRK13541 141 QSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGIVLlsSHLESSIKSAQIL 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
419-573 |
7.93e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 419 QIFRGF-------SLSISSGSTVALVGQSGSGKSTVVSLIErfydpqsGEVRIDGINL---KEFQLKWirskiglVSQE- 487
Cdd:PRK10636 8 QIRRGVrvlldnaTATINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYtfpGNWQLAW-------VNQEt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 488 PVLFTSSIKENIAYGKENATVE-EIRKATElANASKFIDKLPQGLDTM---------------VGEHGTQL-------SG 544
Cdd:PRK10636 74 PALPQPALEYVIDGDREYRQLEaQLHDANE-RNDGHAIATIHGKLDAIdawtirsraasllhgLGFSNEQLerpvsdfSG 152
|
170 180
....*....|....*....|....*....
gi 1063718281 545 GQKQRIAVARAILKDPRILLLDEATSALD 573
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
425-627 |
8.40e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 425 SLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGinlkefQLKWIRSKIGLVSQEPVLFTSSIKeNIAYGKE 504
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGIENIELK-GLMMGLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 505 NATVEEIR-KATELANASKFIDklpQGLDTMvgehgtqlSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEA 583
Cdd:PRK13545 117 KEKIKEIIpEIIEFADIGKFIY---QPVKTY--------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063718281 584 LDRIMVN-RTTVVVAHRLSTVRNADMIAV-IHQGKIVEKGSHSELL 627
Cdd:PRK13545 186 MNEFKEQgKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVV 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1077-1226 |
9.07e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1077 IRAGKTIALVGESGSGKSTVI-ALLQRFydpDSGQITLDG--VEIKTLQLKWLRQqTGLVSQEPV-LFNETIRaniaygk 1152
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLnVLAERV---TTGVITGGDrlVNGRPLDSSFQRS-IGYVQQQDLhLPTSTVR------- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1153 ggdatETEIVSA-----AELSNAHGF--------ISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLL-LDEA 1218
Cdd:TIGR00956 855 -----ESLRFSAylrqpKSVSKSEKMeyveevikLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
....*...
gi 1063718281 1219 TSALDAES 1226
Cdd:TIGR00956 930 TSGLDSQT 937
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1071-1259 |
9.93e-06 |
|
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: 48.76 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVI------ALLQRFYDpdSGQITLDGVEIKTLQ-LKWLRQqtglVSQEPV----- 1138
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHL--KKEQPGNHDRIEGLEhIDKVIV----IDQSPIgrtpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 --------LFNEtIRA----------------NIAY-GKG-GDATETEIVSAAEL----SNAHGFISGLQQ---GYDTMv 1185
Cdd:cd03271 86 snpatytgVFDE-IRElfcevckgkrynretlEVRYkGKSiADVLDMTVEEALEFfeniPKIARKLQTLCDvglGYIKL- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 1186 GERGVQLSGGQKQRVAIARAIVK---DPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTIKNADVI 1259
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWI 241
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
772-988 |
1.08e-05 |
|
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: 48.74 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 772 WAIIFMLLGVA--SMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSaDAATVRG-LVGD 848
Cdd:cd18782 42 YVIGVVMLVAAllEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDK--RPVGELSTRIS-ELDTIRGfLTGT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 849 ALAQTVQNLASVTAgLVIAFVASWQLAFIVLAMLPLIGLngyiymkFMVGFSADAKRMYEEASQVA-------NDAVGSI 921
Cdd:cd18782 119 ALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLL-------LTFLFGPILRRQIRRRAEASaktqsylVESLTGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063718281 922 RTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTTF 988
Cdd:cd18782 191 QTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTL 257
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1063-1273 |
1.49e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1063 SRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALL--QRFYDPDSGQITLDGVEIKTLQLKwLRQQTG--LVSQEPV 1138
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGifMAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1139 --------LFNETirANIAYGKGGDATETEIVSAAELSNAHgfISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDP 1210
Cdd:PRK09580 89 eipgvsnqFFLQT--ALNAVRSYRGQEPLDRFDFQDLMEEK--IALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1211 KVLLLDEATSALDAESERVVQDALDRVM-VNRTTVVVAH--RLSTIKNADVIAVVKNGVIVEKGKH 1273
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
124-334 |
1.60e-05 |
|
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: 48.25 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 124 VALKFVYLGLGTLVAALLQ--VSGWMisGER--QAGRIRSL-YLQtilRQDIAFFDVETnTGEVVGRMSGDTVLIQDAMG 198
Cdd:cd18546 41 AAAAYLAVVLAGWVAQRAQtrLTGRT--GERllYDLRLRVFaHLQ---RLSLDFHERET-SGRIMTRMTSDIDALSELLQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 199 EKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLvmsgAALAIVISKMASRG--QTSYAKAAVVVE--QTVGSIRT 274
Cdd:cd18546 115 TGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPL----ALATRWFRRRSSRAyrRARERIAAVNADlqETLAGIRV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 275 VASFTGEKQAISNYnKHLVSAYRA---------GVFEGASTGLGlgtlNIvifcTYALAVWYGGKMILE 334
Cdd:cd18546 191 VQAFRRERRNAERF-AELSDDYRDarlraqrlvAIYFPGVELLG----NL----ATAAVLLVGAWRVAA 250
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1190-1262 |
1.78e-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: 46.80 E-value: 1.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1190 VQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVN--RTTVVVAHRLSTIKN-ADVIAVV 1262
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYlSDRIHVF 145
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1054-1274 |
1.91e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1054 LRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPD---SGQITLDGVEIKTLQLkwlRQQT 1130
Cdd:PLN03140 165 LGMLGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP---RKTS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1131 GLVSQEPV-------------------------LFNETIR----ANIAYGKGGD----ATETEIVSAAELSNAHGFISGL 1177
Cdd:PLN03140 242 AYISQNDVhvgvmtvketldfsarcqgvgtrydLLSELARrekdAGIFPEAEVDlfmkATAMEGVKSSLITDYTLKILGL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1178 QQGYDTMVGE---RGVqlSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDR-VMVNRTTVVVahrlSTI 1253
Cdd:PLN03140 322 DICKDTIVGDemiRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQiVHLTEATVLM----SLL 395
|
250 260
....*....|....*....|....*...
gi 1063718281 1254 KNA-------DVIAVVKNGVIVEKGKHE 1274
Cdd:PLN03140 396 QPApetfdlfDDIILLSEGQIVYQGPRD 423
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1067-1251 |
2.15e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1067 VQIFQDLCLSIRAGKTIALVGESGSGKSTVIALL--QRFYDPDSGQITLDGVEIKtlQLKWLR-----QQTGLVS----- 1134
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKK--QETFARisgycEQNDIHSpqvtv 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1135 QEPVLFNETIRANIAYGKGGDATET-EIVSAAELSNAHgfisglqqgyDTMVGERGVQ-LSGGQKQRVAIARAIVKDPKV 1212
Cdd:PLN03140 971 RESLIYSAFLRLPKEVSKEEKMMFVdEVMELVELDNLK----------DAIVGLPGVTgLSTEQRKRLTIAVELVANPSI 1040
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063718281 1213 LLLDEATSALDAESERVVQDAL-DRVMVNRTTVVVAHRLS 1251
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1052-1248 |
2.18e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1052 IELRHISFKYPSRPdvqIFQDLCLSIRAGKTIALVGESGSGKSTVIALL-----QRFydpdSGQITLDGVEIKTLQLKW- 1125
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGY----SNDLTLFGRRRGSGETIWd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1126 LRQQTGLVSQEPVL---FNETIRANIAYGKGGDATETEIVSAAELSNAHGFISGLqqGYDTMVGERGVQ-LSGGQKQRVA 1201
Cdd:PRK10938 334 IKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSWGQQRLAL 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063718281 1202 IARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTT--VVVAH 1248
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSH 460
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
80-334 |
3.36e-05 |
|
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: 47.56 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 80 MILGTIGAVGNGLGFPIMTILFGDVIDVFGQNQNSSD--VSDK--IAKVALKFVYLGLGTLVAALLQVS-------GWMI 148
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLplVPASlgPADPRGQLWLLGGLTVAAFLLESLfqylsgvLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 149 SGERQAGRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLV 228
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFE-DRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 229 MVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHlvSA-YRAGVFEGASTG 307
Cdd:cd18565 160 ALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADA--SEeYRDANWRAIRLR 237
|
250 260
....*....|....*....|....*...
gi 1063718281 308 LGL-GTLNIVIFCTYALAVWYGGKMILE 334
Cdd:cd18565 238 AAFfPVIRLVAGAGFVATFVVGGYWVLD 265
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
402-598 |
3.98e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 402 DIELNNVNFSYPARpeEQIFRGfSLSISSGSTVALVGQSGSGKSTV--------VSLIERFYDPQSGEVRIDGINLKEFQ 473
Cdd:PLN03073 177 DIHMENFSISVGGR--DLIVDA-SVTLAFGRHYGLVGRNGTGKTTFlrymamhaIDGIPKNCQILHVEQEVVGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 474 ---------LKWIRSKIGLVSQEPVLFTSSIKENiAYGKENATV---------EEIRKATEL-------ANASKFIDKLP 528
Cdd:PLN03073 254 cvlntdierTQLLEEEAQLVAQQRELEFETETGK-GKGANKDGVdkdavsqrlEEIYKRLELidaytaeARAASILAGLS 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 529 QGLDTMVGEHGTqLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALdrIMVNRTTVVVAH 598
Cdd:PLN03073 333 FTPEMQVKATKT-FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1051-1248 |
4.23e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1051 DIELRHISFKYPSRpdvQIFQDLCLSIRAGKTIALVGESGSGKSTVI-ALLQRFYD--PDSGQI-----TLDGVEIKTLQ 1122
Cdd:PLN03073 177 DIHMENFSISVGGR---DLIVDASVTLAFGRHYGLVGRNGTGKTTFLrYMAMHAIDgiPKNCQIlhveqEVVGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 ---------LKWLRQQTGLVSQEPVLFNETIRANiAYGKGGDATETEIVS----------------AAElSNAHGFISGL 1177
Cdd:PLN03073 254 cvlntdierTQLLEEEAQLVAQQRELEFETETGK-GKGANKDGVDKDAVSqrleeiykrlelidayTAE-ARAASILAGL 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 1178 QQGYDtMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALdrVMVNRTTVVVAH 1248
Cdd:PLN03073 332 SFTPE-MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
69-344 |
5.04e-05 |
|
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: 46.61 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 69 FAFAdsfdIILMILGTIGAVgnglgfpIMTILFGDVIDVFGQNQNSSdvSDKIAKVALkfVYLGLgTLVAALLQVSGWMI 148
Cdd:cd18544 1 FILA----LLLLLLATALEL-------LGPLLIKRAIDDYIVPGQGD--LQGLLLLAL--LYLGL-LLLSFLLQYLQTYL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 149 ---SGERQAGRIRSLYLQTILRQDIAFFDvETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLL 225
Cdd:cd18544 65 lqkLGQRIIYDLRRDLFSHIQRLPLSFFD-RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 226 TLVMVSSIPLLVmsgaaLAIVISKMASRgqTSYAKA--------AVVVEQTVGsIRTVASFTGEKQAISNYNKHLVSAYR 297
Cdd:cd18544 144 ALISLLVLPLLL-----LATYLFRKKSR--KAYREVreklsrlnAFLQESISG-MSVIQLFNREKREFEEFDEINQEYRK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1063718281 298 AGVFEGASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGqVLI 344
Cdd:cd18544 216 ANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG-VLY 261
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1045-1223 |
5.53e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1045 LDNVKGDIELRHISFkypSRPDVQifqDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKT---- 1120
Cdd:PRK10762 249 LDKAPGEVRLKVDNL---SGPGVN---DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspq 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1121 -------LQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGGdateTEIVSAAELSNAHGFISGLQ---QGYDTMVGErgv 1190
Cdd:PRK10762 323 dglangiVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAG----GSLKHADEQQAVSDFIRLFNiktPSMEQAIGL--- 395
|
170 180 190
....*....|....*....|....*....|...
gi 1063718281 1191 qLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:PRK10762 396 -LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1034-1225 |
7.64e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1034 KIDPSDESGRVLdnvkgdIELRHISFKYPsrpDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITl 1113
Cdd:PRK11147 308 QVEEASRSGKIV------FEMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1114 dgVEIKtLQLKWLRQQTGLVSQEpvlfnETIRANIAYGKggdaTETEI--VSAAELSNAHGFIsglqqgYDTMVGERGVQ 1191
Cdd:PRK11147 378 --CGTK-LEVAYFDQHRAELDPE-----KTVMDNLAEGK----QEVMVngRPRHVLGYLQDFL------FHPKRAMTPVK 439
|
170 180 190
....*....|....*....|....*....|....*
gi 1063718281 1192 -LSGGQKQRVAIARAIVKDPKVLLLDEATSALDAE 1225
Cdd:PRK11147 440 aLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
540-576 |
8.04e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 8.04e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1063718281 540 TQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 576
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1075-1268 |
8.38e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1075 LSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGveiKTLQLKWL--------------RQQTGLVSQEPVLF 1140
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPrdairagimlcpedRKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1141 NETIRANIAYGKGGDAteteIVSAAELSNAHGFISGLQ---QGYDTMVGergvQLSGGQKQRVAIARAIVKDPKVLLLDE 1217
Cdd:PRK11288 351 NINISARRHHLRAGCL----INNRWEAENADRFIRSLNiktPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 1218 ATSALD--AESE--RVVQDALDRvmvNRTTVVVAHRL-STIKNADVIAVVKNGVIV 1268
Cdd:PRK11288 423 PTRGIDvgAKHEiyNVIYELAAQ---GVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
542-600 |
8.98e-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: 44.49 E-value: 8.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063718281 542 LSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVN--RTTVVVAHRL 600
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDL 132
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
845-1003 |
1.25e-04 |
|
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: 45.63 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 845 LVGDALaQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSadaKRMYEEASQVAN---DAVGSI 921
Cdd:cd18568 115 LTRSAL-TTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNS---REIFQANAEQQSflvEALTGI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 922 RTVASFCAEEKVMKMYKKKCEGPMRTGIR-QGIVSGIGFGVSFFVLFSSyAASFYAGARLVDDGKTTFDSV--FRVFFAL 998
Cdd:cd18568 191 ATIKALAAERPIRWRWENKFAKALNTRFRgQKLSIVLQLISSLINHLGT-IAVLWYGAYLVISGQLTIGQLvaFNMLFGS 269
|
....*
gi 1063718281 999 TMAAV 1003
Cdd:cd18568 270 VINPL 274
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
541-623 |
1.28e-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: 43.89 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 541 QLSGGQKQRIAVARAI---LKDPRIL-LLDEATSALDAESERIVQEALDRIMVNRTTVVVA-HRLSTVRNADmiAVIHQG 615
Cdd:cd03227 77 QLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELAD--KLIHIK 154
|
....*...
gi 1063718281 616 KIVEKGSH 623
Cdd:cd03227 155 KVITGVYK 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
422-619 |
1.29e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 422 RGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLK-EFQLKWIRSKIGLVSQ---EPVLFTS-SIK 496
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 497 ENIAY------GKENATVEEIRKATELANASKFIDKLPQGLDTmVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATS 570
Cdd:PRK09700 360 QNMAIsrslkdGGYKGAMGLFHEVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 571 ALD----AESERIVQEALDRimvNRTTVVVAHRLSTVRNA-DMIAVIHQGKIVE 619
Cdd:PRK09700 439 GIDvgakAEIYKVMRQLADD---GKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1046-1223 |
1.37e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1046 DNVKGDI--ELRHI-SFKYPSrpdvqiFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQ 1122
Cdd:PRK10982 243 ENKPGEVilEVRNLtSLRQPS------IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1123 -----------LKWLRQQTGLVSQEPVLFNETIrANIAYGKggdaTETEIVSAAEL-SNAHGFISGLQ---QGYDTMVGe 1187
Cdd:PRK10982 317 aneainhgfalVTEERRSTGIYAYLDIGFNSLI-SNIRNYK----NKVGLLDNSRMkSDTQWVIDSMRvktPGHRTQIG- 390
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063718281 1188 rgvQLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:PRK10982 391 ---SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1085-1248 |
1.64e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1085 LVGESGSGKSTVIALLQRFYDPDSGQITLDGVEiktlQLKWLRQ-----------------QTGL--VSQEpvlfNETIR 1145
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE----RLGKLRQdqfafeeftvldtvimgHTELweVKQE----RDRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1146 ANiaygkgGDATETEIVSAAELSNAHGFISG-----------------LQQGYDTMVgergvQLSGGQKQRVAIARAIVK 1208
Cdd:PRK15064 104 AL------PEMSEEDGMKVADLEVKFAEMDGytaearagelllgvgipEEQHYGLMS-----EVAPGWKLRVLLAQALFS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063718281 1209 DPKVLLLDEATSALDAESERVVQDAL-DRvmvNRTTVVVAH 1248
Cdd:PRK15064 173 NPDILLLDEPTNNLDINTIRWLEDVLnER---NSTMIIISH 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1071-1259 |
1.87e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.47 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1071 QDLCLSIRAGKTIALVGESGSGKSTVIallqrfydpdsgqitldgveiktlqlkwlrqQTGLVSQEPVLFNETIRANiay 1150
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLV-------------------------------NEGLYASGKARLISFLPKF--- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1151 gkggdaTETEIVSAAELSnahgFISGLQQGYDTMvGERGVQLSGGQKQRVAIARAIVKDPK--VLLLDEATSALDAESER 1228
Cdd:cd03238 58 ------SRNKLIFIDQLQ----FLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|..
gi 1063718281 1229 VVQDALDRVMVNRTTV-VVAHRLSTIKNADVI 1259
Cdd:cd03238 127 QLLEVIKGLIDLGNTViLIEHNLDVLSSADWI 158
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
426-572 |
2.61e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 426 LSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDG--INLKEFQlKWIRSKIGLVSQE-PVLFTSSIKENI--- 499
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSK-EALENGISMVHQElNLVLQRSVMDNMwlg 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718281 500 AYGKENATVEEirkaTELANASKFI-DKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL 572
Cdd:PRK10982 98 RYPTKGMFVDQ----DKMYRDTKAIfDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1053-1223 |
2.95e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1053 ELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKsTVIA--LLQRFYDPD-SGQITLDGVEIktlqlkwlrqQ 1129
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELAmsVFGRSYGRNiSGTVFKDGKEV----------D 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1130 TGLVSqepvlfnETIRANIAYgkggdATE-------------TEIVSAAELSN--AHGFISGLQ-----QGY-DTM---- 1184
Cdd:NF040905 328 VSTVS-------DAIDAGLAY-----VTEdrkgyglnliddiKRNITLANLGKvsRRGVIDENEeikvaEEYrKKMnikt 395
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063718281 1185 --VGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALD 1223
Cdd:NF040905 396 psVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
381-573 |
3.08e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 381 KRKPEIdasdttGKVLDDIRgdielnNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKS-TVVSLIERFYDPQ- 458
Cdd:NF040905 248 ERTPKI------GEVVFEVK------NWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNi 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 459 SGEVRIDGinlKEFQLKWIRSKI--------------GLVSQEpvlftsSIKENI---AYGK--ENATVEEIRkatELAN 519
Cdd:NF040905 316 SGTVFKDG---KEVDVSTVSDAIdaglayvtedrkgyGLNLID------DIKRNItlaNLGKvsRRGVIDENE---EIKV 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063718281 520 ASKFIDKL----PqGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 573
Cdd:NF040905 384 AEEYRKKMniktP-SVFQKVG----NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1192-1277 |
3.60e-04 |
|
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: 45.00 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1192 LSGGQKQRVAIARAIVKD---PKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVV-AHRLSTIKNADVI------AV 1261
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYIidlgpeGG 909
|
90
....*....|....*.
gi 1063718281 1262 VKNGVIVEKGKHETLI 1277
Cdd:TIGR00630 910 DGGGTVVASGTPEEVA 925
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
793-958 |
3.80e-04 |
|
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: 44.11 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 793 FFSIAGCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLsADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASW 872
Cdd:cd18566 65 ILAWIGARFDHRLSNAAFEHLLSLPLSFFER--EPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 873 QLAFIVLAMLPLIGLNGYIYMKFM-----VGFSADAKRMyeeasQVANDAVGSIRTVASFCAE----EKVMKMYKKKCEG 943
Cdd:cd18566 142 KLVLVPLVLLGLFVLVAILLGPILrralkERSRADERRQ-----NFLIETLTGIHTIKAMAMEpqmlRRYERLQANAAYA 216
|
170
....*....|....*
gi 1063718281 944 PMRTGIRQGIVSGIG 958
Cdd:cd18566 217 GFKVAKINAVAQTLG 231
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
798-942 |
3.83e-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: 43.98 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 798 GCKLVQRIRSMCFEKVVRMEVGWFDEteNSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFI 877
Cdd:cd18549 70 GARIETDMRRDLFEHLQKLSFSFFDN--NKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLI 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 878 VLAMLPLIGLNGYIYM-KFMVGFSADAKRMYEEASQVaNDAVGSIRTVASFCAEEKVMKMYKKKCE 942
Cdd:cd18549 148 VFALLPLMIIFTIYFNkKMKKAFRRVREKIGEINAQL-EDSLSGIRVVKAFANEEYEIEKFDEGND 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1186-1260 |
4.50e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1186 GERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVV-----------VAHRLSTIK 1254
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVID 218
|
....*.
gi 1063718281 1255 NADVIA 1260
Cdd:NF000106 219 RGRVIA 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
518-626 |
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 1063718281 518 ANASKFIDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVA 597
Cdd:NF000106 123 ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|.
gi 1063718281 598 HRL--STVRNADMIAVIHQGKIVEKGSHSEL 626
Cdd:NF000106 201 TQYmeEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1061-1263 |
7.43e-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: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1061 YPSRPDVQIFQDLCLSIragktialVGESGSGKSTVIallqrfydpdsgqitldgveiktlqlkwlrQQTGLVsqepvlf 1140
Cdd:cd03227 10 YFVPNDVTFGEGSLTII--------TGPNGSGKSTIL------------------------------DAIGLA------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1141 neTIRANIAYGKGGDATETEIVSAAELSnahgFISGLqqgydtmvgergVQLSGGQKQRVAIARAI----VKDPKVLLLD 1216
Cdd:cd03227 45 --LGGAQSATRRRSGVKAGCIVAAVSAE----LIFTR------------LQLSGGEKELSALALILalasLKPRPLYILD 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063718281 1217 EATSALDAESERVVQDALDRVMVNRTTVVVA-HRLSTIKNADVIAVVK 1263
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELADKLIHIK 154
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
215-352 |
7.61e-04 |
|
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: 43.26 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 215 FVIAFTEGWLLTLVMVSSIPL-LVMSGAALAIVISKMASRGQTSYAKAAVVVEqTVGSIRTVASFTGEKQAISNYNKHLv 293
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLyALLSLLVTPILRRRLEEKFQRGAENQSFLVE-TVTGIETVKSLAVEPQFQRRWEELL- 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 294 SAYRAGVFEGASTGLGLGTLNIVIFCTYALAV-WYGGKMILEKGYTGGQVliIIFAVLTG 352
Cdd:cd18588 211 ARYVKASFKTANLSNLASQIVQLIQKLTTLAIlWFGAYLVMDGELTIGQL--IAFNMLAG 268
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
421-573 |
1.19e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 421 FRGF---SLSISSGSTVaLVGQSGSGKSTVVSLIERFYDPQSGEvridGINLKEF----QLKWIRSKIGLVsqepvlFTS 493
Cdd:COG3593 11 FRSIkdlSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSR----KFDEEDFylgdDPDLPEIEIELT------FGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 494 SIKENIAYGKENATVEEIRKATELANASkfIDKLPQGLDTMVGEHGTQLSGGQKQRIAVA----RAILKDPRILLLDEAT 569
Cdd:COG3593 80 LLSRLLRLLLKEEDKEELEEALEELNEE--LKEALKALNELLSEYLKELLDGLDLELELSldelEDLLKSLSLRIEDGKE 157
|
....
gi 1063718281 570 SALD 573
Cdd:COG3593 158 LPLD 161
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
768-906 |
1.25e-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: 42.55 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 768 DTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETenSSGAIGARLSADAATVRGLVG 847
Cdd:cd18599 56 DLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTT--PTGRILNRFSKDLDEVDVRLP 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 848 DALAQTVQNLASVTAGLV-IAFVASWqlafIVLAMLPLIGLNGYIYMKFMVGFSaDAKRM 906
Cdd:cd18599 134 FTLENFLQNVLLVVFSLIiIAIVFPW----FLIALIPLAIIFVFLSKIFRRAIR-ELKRL 188
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
730-939 |
1.49e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 42.21 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 730 LILGSIAAVLngviLPIFgilISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMC 809
Cdd:cd18560 5 LILGKACNVL----APLF---LGRAVNALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 FEKVVRMEVGWFdeTENSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVI-AFVASWQLAFIVLAMLPLigln 888
Cdd:cd18560 78 FAHLHSLSLDWH--LSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVfAFHFGAWLALIVFLSVLL---- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718281 889 gYIYMKFMV-----GFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKK 939
Cdd:cd18560 152 -YGVFTIKVtewrtKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGE 206
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
455-634 |
2.01e-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: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 455 YDPQSGEVRIDGINLKEFQlkwirskiGLVSQEPVLFTSSIKENiayGKENATVEEIRKatELANASKFIDKLpqGLDTM 534
Cdd:TIGR00630 416 LKPEALAVTVGGKSIADVS--------ELSIREAHEFFNQLTLT---PEEKKIAEEVLK--EIRERLGFLIDV--GLDYL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 535 -VGEHGTQLSGGQKQRIAVARAI----------LKDPRILLLDEATSALDAESERIvqealdRIMVNrTTVVVAHRLSTV 603
Cdd:TIGR00630 481 sLSRAAGTLSGGEAQRIRLATQIgsgltgvlyvLDEPSIGLHQRDNRRLINTLKRL------RDLGN-TLIVVEHDEDTI 553
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063718281 604 RNADMI------AVIHQGKIVEKGSHSELLRDPE---GAY 634
Cdd:TIGR00630 554 RAADYVidigpgAGEHGGEVVASGTPEEILANPDsltGQY 593
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
732-999 |
2.13e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)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. ABC transporters typically consist 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: 350023 [Multi-domain] Cd Length: 289 Bit Score: 41.70 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 732 LGSIAAVLNGVILPIFGILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFpAQTIFFSIagcKLVQRIRSMC-- 809
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLL-HQYFFLSF---RLGMRVRSALss 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 810 --FEKVVRMEVGWFDETenSSGAIGARLSADAATVrglvgDALAQTVQNLASVTAGLVIAFVASWQL----AFI-VLAML 882
Cdd:cd18579 77 liYRKALRLSSSARQET--STGEIVNLMSVDVQRI-----EDFFLFLHYLWSAPLQIIVALYLLYRLlgwaALAgLGVLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 883 PLIGLNGYIyMKFMVGFSADA-----KRMyeeasQVANDAVGSIRTV------ASFcaEEKV-------MKMYKKKcegp 944
Cdd:cd18579 150 LLIPLQAFL-AKLISKLRKKLmkatdERV-----KLTNEILSGIKVIklyaweKPF--LKRIeelrkkeLKALRKF---- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1063718281 945 mrtGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLvddgkttfdSVFRVFFALT 999
Cdd:cd18579 218 ---GYLRALNSFLFFSTPVLVSLATFATYVLLGNPL---------TAAKVFTALS 260
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
735-904 |
2.34e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 41.63 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 735 IAAVLNGVILPIFGILISSVIKAFFKPPEQLkSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVV 814
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARIIAGVFLEGAGL-AALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 815 RMEVGWFDETenSSGAIGARLSADAATVRGLVGDALAQTVqnLASVT--AGLVIAFVASWQLAFIVLAMLPLIGLngyiy 892
Cdd:cd18584 82 ALGPALLRRQ--SSGELATLLTEGVDALDGYFARYLPQLV--LAAIVplLILVAVFPLDWVSALILLVTAPLIPL----- 152
|
170
....*....|....
gi 1063718281 893 mkFM--VGFSADAK 904
Cdd:cd18584 153 --FMilIGKAAQAA 164
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
435-609 |
3.33e-03 |
|
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: 40.28 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 435 ALVGQSGSGKSTVvslierfydpqsgevrIDGINLKEFQLKWIRSKIGLVSQEPVlftsSIKENIAYGK---ENATVEE- 510
Cdd:cd03240 26 LIVGQNGAGKTTI----------------IEALKYALTGELPPNSKGGAHDPKLI----REGEVRAQVKlafENANGKKy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 511 -IRKATELANASKFIdklPQG-LDTMVGEHGTQLSGGQKQ------RIAVARAILKDPRILLLDEATSALDAESeriVQE 582
Cdd:cd03240 86 tITRSLAILENVIFC---HQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEE 159
|
170 180 190
....*....|....*....|....*....|...
gi 1063718281 583 ALDRIM------VNRTTVVVAHRLSTVRNADMI 609
Cdd:cd03240 160 SLAEIIeerksqKNFQLIVITHDEELVDAADHI 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
530-621 |
3.57e-03 |
|
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: 40.32 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 530 GLD--TMVGEHGTqLSGGQKQRIAVARAI---LKDPrILLLDEATSAL-DAESERIVqEALDRIM-VNRTTVVVAHRLST 602
Cdd:cd03270 125 GLGylTLSRSAPT-LSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLhPRDNDRLI-ETLKRLRdLGNTVLVVEHDEDT 201
|
90 100
....*....|....*....|....*
gi 1063718281 603 VRNADMI------AVIHQGKIVEKG 621
Cdd:cd03270 202 IRAADHVidigpgAGVHGGEIVAQG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1044-1269 |
3.93e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.31 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1044 VLDNVKGDI--ELRHISfkypsRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIK-T 1120
Cdd:PRK09700 256 NVSNLAHETvfEVRNVT-----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1121 LQLKWLRQQTGLVSQ---EPVLF-NETIRANIAY----------GKGGDATETEIVSAAElsNAHGFISGLQQGYDTMVG 1186
Cdd:PRK09700 331 SPLDAVKKGMAYITEsrrDNGFFpNFSIAQNMAIsrslkdggykGAMGLFHEVDEQRTAE--NQRELLALKCHSVNQNIT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 1187 ErgvqLSGGQKQRVAIARAIVKDPKVLLLDEATSALD----AESERVVQDALDRvmvNRTTVVVAHRLSTIKNA-DVIAV 1261
Cdd:PRK09700 409 E----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQLADD---GKVILMVSSELPEIITVcDRIAV 481
|
....*...
gi 1063718281 1262 VKNGVIVE 1269
Cdd:PRK09700 482 FCEGRLTQ 489
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
864-987 |
4.95e-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: 40.50 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 864 LVIAFVAsWQLAFIVLAMLPLIGLNGYIYMKFMvgfSADAKRMYEEASQ---VANDAVGSIRTVASFCAEEKVMKMYKKK 940
Cdd:cd18587 133 AVIALIG-GPLALVPLVAIPLVLLYGLLLQKPL---RRLVEESMRESAQknaLLVESLSGLETIKALGAEGRMQRRWEEA 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063718281 941 CEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTT 987
Cdd:cd18587 209 VAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELT 255
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
436-472 |
7.28e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 39.27 E-value: 7.28e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1063718281 436 LVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEF 472
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFREL 52
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
729-935 |
7.39e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) 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: 350040 [Multi-domain] Cd Length: 309 Bit Score: 40.17 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 729 MLILGSIAAVLNgvILPIFGILisSVIKAFFKPPEQLKSDTRFWaIIFMLLGVASMVVFPAQTIFFsiaGCKLVQRIRSM 808
Cdd:cd18596 2 QALLAVLSSVLS--FAPPFFLN--RLLRYLEDPGEDATVRPWVW-VLLLFLGPLLSSLLDQQYLWI---GRRLSVRLRAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 809 C----FEKVVRMEVgwFDETENSSGAIGARLSADAATVrglvGDALAQTVQNLASVTAG------------------LVI 866
Cdd:cd18596 74 LtqliFEKALRRRD--KSGSSKSSESKKKDKEEDEDEK----SSASVGKINNLMSVDANrisefaaflhllvsaplqIVI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063718281 867 AFVASWQL----AFI-VLAMLPLIGLNGYIyMKFMVGFSADA-----KRMyeeasQVANDAVGSIRTVASFCAEEKVMK 935
Cdd:cd18596 148 AIVFLYRLlgwsALVgLAVMVLLLPLNGYL-AKRYSRAQKELmkardARV-----QLVTEVLQGIRMIKFFAWERKWEE 220
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
128-238 |
7.57e-03 |
|
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: 39.79 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718281 128 FVYLGLGTLVAALLQVSGWMISGERQAGRIRSLYLQTILRQDIAFFDVeTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQL 207
Cdd:cd18580 45 AALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDT-TPSGRILNRFSKDIGLIDEELPLALLDFLQS 123
|
90 100 110
....*....|....*....|....*....|.
gi 1063718281 208 VSTFIGGFVIAFTEGWLLTLVMvssIPLLVM 238
Cdd:cd18580 124 LFSVLGSLIVIAIVSPYFLIVL---PPLLVV 151
|
|
| |
