|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-600 |
4.46e-163 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 498.15 E-value: 4.46e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 32 WLLMGLGLIGAVGDGFTTPLVLLITSKLMNNIGGSSfNTDTFMQSIsknsVALLYVACGSWVVCFLEGYCWTRTGERQTA 111
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLL----LLLLGLALLRALLSYLQRYLLARLAQRVVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIV 191
Cdd:COG1132 95 DLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 192 LLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGI-TIGSN 270
Cdd:COG1132 173 LLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALfFPLME 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 271 GITFAMWGFMSWYGSRMVMYHGAQGGTVFAVAAAIAIGGVSLGGGLSNLKYFFEAASVGERIMEVINRVPKIDsDNPDGH 350
Cdd:COG1132 253 LLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP-DPPGAV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 351 KLEKIRGEVEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQV 430
Cdd:COG1132 332 PLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 431 KWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIAR 510
Cdd:COG1132 410 ESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIAR 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQY 590
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLY 568
|
570
....*....|
gi 15229473 591 STLVHLQQIE 600
Cdd:COG1132 569 ARLYRLQFGE 578
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-1235 |
5.59e-163 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 524.59 E-value: 5.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 34 LMGLGLIGAVGDGFTTPLVLLITSKLMNNIG-GSSFNTDTFmqsisknsvALLYVACGSWVVCFLEGYCWTRTGERQTAR 112
Cdd:PTZ00265 61 LLGVSFVCATISGGTLPFFVSVFGVIMKNMNlGENVNDIIF---------SLVLIGIFQFILSFISSFCMDVVTTKILKT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 113 MREKYLRAVLRQDVGYFDLHVTS--TSDVitsvssdSFVIQDV---LSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGL 187
Cdd:PTZ00265 132 LKLEFLKSVFYQDGQFHDNNPGSklTSDL-------DFYLEQVnagIGTKFITIFTYASAFLGLYIWSLFKNARLTLCIT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 188 PFIVLLVIPGLMYGRAlISISRKIREEYNEAGF-VAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGIT 266
Cdd:PTZ00265 205 CVFPLIYICGVICNKK-VKINKKTSLLYNNNTMsIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 267 IGS-NGITFAMWGFMSWYGSRMVMYHGA--------QGGTVFAVAAAIAIGGVSLGGGLSNLKYFFEAASVGERIMEVIN 337
Cdd:PTZ00265 284 IGMiNGFILASYAFGFWYGTRIIISDLSnqqpnndfHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIIN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 338 RVPKIDsDNPDGHKLEKIRgEVEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGE 417
Cdd:PTZ00265 364 RKPLVE-NNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGD 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 418 ILI-DGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFG--------------KEDA-------------------- 462
Cdd:PTZ00265 442 IIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDGndsqenknkrnscrakcagd 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 463 ------SMD-----------------DVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTIL 519
Cdd:PTZ00265 522 lndmsnTTDsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKIL 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 520 LLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLSTIRNADVISVVKN--------------------------- 570
Cdd:PTZ00265 602 ILDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSNrergstvdvdiigedptkdnkennnkn 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 571 --------------------GHIVETGSHDELMENIDGQYSTLVHLQQIEK---------QDINVSVKIGPISDPSKDIR 621
Cdd:PTZ00265 682 nkddnnnnnnnnnnkinnagSYIIEQGTHDALMKNKNGIYYTMINNQKVSSkkssnndndKDSDMKSSAYKDSERGYDPD 761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 622 NSSRVSTLSRSSSANSVTGPSTIKNLSEDN--------------KPQLPSFKRLLAMNLPEWKQAL-YGCISATLFGAIQ 686
Cdd:PTZ00265 762 EMNGNSKHENESASNKKSCKMSDENASENNaggklpflrnlfkrKPKAPNNLRIVYREIFSYKKDVtIIALSILVAGGLY 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 687 PAYAYSLGSMVSVYFltSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDR 766
Cdd:PTZ00265 842 PVFALLYAKYVSTLF--DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQ 919
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 767 DENSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCFYTRRVLLKS--MSK 844
Cdd:PTZ00265 920 DKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANkdVEK 999
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 845 KAI---------KAQDESSK----LAAEAVSNVRTITAFSSQERIMKMLEKA----QESPRRESIRQSWFAGFglamSQS 907
Cdd:PTZ00265 1000 KEInqpgtvfayNSDDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFCNLIEKAidysNKGQKRKTLVNSMLWGF----SQS 1075
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 908 LTSCTWALDFWYGGRLIQDGYITAKALFETFMILVSTGRVIADAGSMTTDLAKGSDAVGSVFAVLDRYTSIDPEDPDGYE 987
Cdd:PTZ00265 1076 AQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIR 1155
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 988 ---TERITGQVEFLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDpLK------------- 1051
Cdd:PTZ00265 1156 iknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYD-LKndhhivfknehtn 1234
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1052 ------------------------------------------GIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRE 1089
Cdd:PTZ00265 1235 dmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYE 1314
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NIIYGGVSDKIDEAEIIEAAKAANahDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQ 1169
Cdd:PTZ00265 1315 NIKFGKEDATREDVKRACKFAAID--EFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1170 SERVVQDALERV--MVGRTSVVIAHRLSTIQNCDAIAVLDK----GKLVE-RGTHSSLLSkGPTGIYFSLVSL 1235
Cdd:PTZ00265 1393 SEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLS-VQDGVYKKYVKL 1464
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
651-1236 |
1.01e-161 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 494.68 E-value: 1.01e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 651 NKPQLPSFKRLLAMNLPEWKQALYGCISATLFGAIQPAYAYSLGSMVSVYFLTSHdeiKEKTRIYALSFVGLAVLSFLIN 730
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD---LSALLLLLLLLLGLALLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 731 ISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMG 810
Cdd:COG1132 79 YLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 811 LVIAWRLALVMIAVQPVIIVCFytrRVLLKSMSKKAIKAQDESSKLAA---EAVSNVRTITAFSSQERIMKMLEKAQESP 887
Cdd:COG1132 157 FVIDWRLALIVLLVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGrlqESLSGIRVVKAFGREERELERFREANEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 888 RRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYITAKALFETFMILVSTGRVIADAGSMTTDLAKGSDAVGS 967
Cdd:COG1132 234 RRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 968 VFAVLDRYTSIdPEDPDGYETERITGQVEFLDVDFSYPTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFY 1047
Cdd:COG1132 314 IFELLDEPPEI-PDPPGAVPLPPVRGEIEFENVSFSYPGDRPVL--KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1048 DPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYG--GVSD-------KIdeaeiieaakaANAHDFI 1118
Cdd:COG1132 391 DPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGrpDATDeeveeaaKA-----------AQAHEFI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1119 TSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQ 1198
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539
|
570 580 590
....*....|....*....|....*....|....*...
gi 15229473 1199 NCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVSLQ 1236
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARG--GLYARLYRLQ 575
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
359-597 |
2.11e-140 |
|
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: 425.42 E-value: 2.11e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTI 518
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 519 LLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQYSTLVHLQ 597
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
995-1236 |
1.55e-128 |
|
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: 393.83 E-value: 1.55e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAGTIRENIIYGgvSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYG--KPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1155 SVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVS 1234
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK--GVYAKLVK 236
|
..
gi 15229473 1235 LQ 1236
Cdd:cd03249 237 AQ 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
90-594 |
6.37e-127 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 407.19 E-value: 6.37e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 90 GSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFV 169
Cdd:TIGR00958 213 ASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDEN--KTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 170 GSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTAL 249
Cdd:TIGR00958 291 GLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEAL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 250 QGSVKLGIKQGLAKGITIGSNGItFAMWGFMS--WYGSRMVMYHGAQGG--TVFAVAAAIAIGGVSlggglsNLKYFF-- 323
Cdd:TIGR00958 371 EETLQLNKRKALAYAGYLWTTSV-LGMLIQVLvlYYGGQLVLTGKVSSGnlVSFLLYQEQLGEAVR------VLSYVYsg 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 324 --EAASVGERIMEVINRVPKIDsdNPDGHKLEKIRGEVEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKS 401
Cdd:TIGR00958 444 mmQAVGASEKVFEYLDRKPNIP--LTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKS 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 402 TVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFIS 481
Cdd:TIGR00958 522 TVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 482 QLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASigRTTILIAHRLSTIRN 561
Cdd:TIGR00958 602 EFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRAS--RTVLLIAHRLSTVER 679
|
490 500 510
....*....|....*....|....*....|...
gi 15229473 562 ADVISVVKNGHIVETGSHDELMENiDGQYSTLV 594
Cdd:TIGR00958 680 ADQILVLKKGSVVEMGTHKQLMED-QGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
81-598 |
5.23e-123 |
|
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: 396.90 E-value: 5.23e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 81 SVALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSS-DSfvIQDVLSEKLP 159
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESR--SVGDLASRFRDvES--IREFLTGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 160 NFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRK-IREEYNEAGFVAEqAISSVRTVYAFSGE 238
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREeSEASAKRQSLLVE-TLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 239 RKTISKFSTALQGSVKLGIKQG-LAKGITIGSNGITFAMWGFMSWYGSRMVMYHGAQGGTVFAVAAAIAIGGVSLGGGLS 317
Cdd:COG2274 354 SRFRRRWENLLAKYLNARFKLRrLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 318 NLKYFFEAASVGERIMEVINRVPKIDSDNPDGHkLEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSG 397
Cdd:COG2274 434 LLQRFQDAKIALERLDDILDLPPEREEGRSKLS-LPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 398 SGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAH 477
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLH 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 478 NFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLS 557
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15229473 558 TIRNADVISVVKNGHIVETGSHDELMENiDGQYSTLVHLQQ 598
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
84-597 |
3.94e-122 |
|
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: 389.83 E-value: 3.94e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 84 LLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNFLM 163
Cdd:TIGR02204 64 LLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSLSMALR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 164 SASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTIS 243
Cdd:TIGR02204 142 NALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 244 KFSTALQGSVKLGIKQGLAKGI-TIGSNGITFAMWGFMSWYGSRMVMYHGAQGGTVFAVAAAIAIGGVSLGGGLSNLKYF 322
Cdd:TIGR02204 222 RFGGAVEKAYEAARQRIRTRALlTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 323 FEAASVGERIMEVINRVPKIDSdnPDGHKL--EKIRGEVEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGK 400
Cdd:TIGR02204 302 QRAAGAAERLIELLQAEPDIKA--PAHPKTlpVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 401 STVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFI 480
Cdd:TIGR02204 380 STLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFI 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 481 SQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIR 560
Cdd:TIGR02204 460 SALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVL 539
|
490 500 510
....*....|....*....|....*....|....*..
gi 15229473 561 NADVISVVKNGHIVETGSHDELMENiDGQYSTLVHLQ 597
Cdd:TIGR02204 540 KADRIVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
657-1236 |
8.79e-120 |
|
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: 383.30 E-value: 8.79e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 657 SFKRLLAMNLPEWKQALYGCISATLFGAIQPAYAYSLGSMVSVYFltsHDEIKEKTRIYALSFVGLAVLSFLINISQHYN 736
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGF---GGRDRSVLWWVPLVVIGLAVLRGICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 737 FAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWR 816
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 817 LALVMIAVQPVI--IVCFYTRRvlLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQ 894
Cdd:TIGR02203 156 LTLIVVVMLPVLsiLMRRVSKR--LRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 895 SWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYITAKAlFETFMilVSTGRVIADAGSMT---TDLAKGSDAVGSVFAV 971
Cdd:TIGR02203 234 TSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFI--TAMIALIRPLKSLTnvnAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 972 LDrytSIDPEDPDGYETERITGQVEFLDVDFSYPTRpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLK 1051
Cdd:TIGR02203 311 LD---SPPEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1052 GIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYGGVSDkIDEAEIIEAAKAANAHDFITSLTEGYDTYCGD 1131
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQ-ADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1132 RGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKL 1211
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|....*
gi 15229473 1212 VERGTHSSLLSKgpTGIYFSLVSLQ 1236
Cdd:TIGR02203 546 VERGTHNELLAR--NGLYAQLHNMQ 568
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
613-1237 |
2.79e-118 |
|
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: 384.19 E-value: 2.79e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 613 ISDPSKDIRnssrvsTLSRSSSANSVTGPS---TIKNLSEDNKPQLPSFKRLLAMNLPEWKQALYGCISA---TLFGAIQ 686
Cdd:COG2274 102 IADPATGRR------KLSLEEFAESWTGVAlllEPTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASlliNLLALAT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 687 PayaysLGSMVsVYfltshDEI---KEKTRIYALS--FVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEV 761
Cdd:COG2274 176 P-----LFTQV-VI-----DRVlpnQDLSTLWVLAigLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 762 GWFDRdeNSSGAICSRLaKDANVVRSLVGDRMALVVqtVSAVTIAFTMGL--VIAWRLALVMIAVQPVIIVcfyTRRVLL 839
Cdd:COG2274 245 SFFES--RSVGDLASRF-RDVESIREFLTGSLLTAL--LDLLFVLIFLIVlfFYSPPLALVVLLLIPLYVL---LGLLFQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 840 KSMSKKAIKAQDESSKLAA---EAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALD 916
Cdd:COG2274 317 PRLRRLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVAL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 917 FWYGGRLIQDGYITAKALFeTFMILVstGRVIADAGSMTTDLAKGSDAVGSVfAVLDRYTSIDPEDPDGY---ETERITG 993
Cdd:COG2274 397 LWLGAYLVIDGQLTLGQLI-AFNILS--GRFLAPVAQLIGLLQRFQDAKIAL-ERLDDILDLPPEREEGRsklSLPRLKG 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTRpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHI 1073
Cdd:COG2274 473 DIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPTLFAGTIRENIIYGgvSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKN 1153
Cdd:COG2274 552 GVVLQDVFLFSGTIRENITLG--DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRN 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1154 PSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLV 1233
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK--GLYAELV 707
|
....
gi 15229473 1234 SLQT 1237
Cdd:COG2274 708 QQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
704-1236 |
2.80e-117 |
|
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: 377.12 E-value: 2.80e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 704 SHDEIKEKTRIYALsFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDAN 783
Cdd:TIGR02204 50 SKDSSGLLNRYFAF-LLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 784 VVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVII--VCFYTRRVllksmSKKAIKAQD---ESSKLAA 858
Cdd:TIGR02204 127 LLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLlpILLFGRRV-----RKLSRESQDriaDAGSYAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 859 EAVSNVRTITAFSSQE----RIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTsctwALDFWYGGRLIQDGYITAKAL 934
Cdd:TIGR02204 202 ETLGAIRTVQAFGHEDaersRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAI----VGVLWVGAHDVIAGKMSAGTL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 935 FETFMILVSTGRVIADAGSMTTDLAKGSDAVGSVFAVLDRYTSID-PEDPDGYETeRITGQVEFLDVDFSYPTRPDVIIF 1013
Cdd:TIGR02204 278 GQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKaPAHPKTLPV-PLRGEIEFEQVNFAYPARPDQPAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIY 1093
Cdd:TIGR02204 357 DGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1094 GgVSDKIDEAEIIEAAKAaNAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERV 1173
Cdd:TIGR02204 437 G-RPDATDEEVEAAARAA-HAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQL 514
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1174 VQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVSLQ 1236
Cdd:TIGR02204 515 VQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG--GLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
629-1233 |
1.36e-115 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 376.76 E-value: 1.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 629 LSRSSSANSVTGPSTIKNLSEDNKPQLPSFKRLLAMNLPEWKQAlygcISATLFGAIqpayaYSLGSMVSVYF------- 701
Cdd:TIGR00958 120 PAAALWAVLSSAGASEKEAEQGQSETADLLFRLLGLSGRDWPWL----ISAFVFLTL-----SSLGEMFIPFYtgrvidt 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 702 -LTSHDEIKEKTRIYALSF--VGLAVLSFLINISqhYNFAYmgEYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRL 778
Cdd:TIGR00958 191 lGGDKGPPALASAIFFMCLlsIASSVSAGLRGGS--FNYTM--ARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 779 AKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIivcFYTRRVLLKSMSKKAIKAQD---ESSK 855
Cdd:TIGR00958 265 SSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV---FLAEKVFGKRYQLLSEELQEavaKANQ 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 856 LAAEAVSNVRTITAFSSQE----RIMKMLEKAQESPRRESIRqswFAGFgLAMSQSLTSCTWALDFWYGGRLIQDGYITA 931
Cdd:TIGR00958 342 VAEEALSGMRTVRSFAAEEgeasRFKEALEETLQLNKRKALA---YAGY-LWTTSVLGMLIQVLVLYYGGQLVLTGKVSS 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 932 KALFeTFMIL-VSTGRVIADAGSMTTDLAKGSDAVGSVFAVLDRYTSIDPedPDGYETERITGQVEFLDVDFSYPTRPDV 1010
Cdd:TIGR00958 418 GNLV-SFLLYqEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDV 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1011 IIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIREN 1090
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 IIYGgvSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQS 1170
Cdd:TIGR00958 575 IAYG--LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1171 ERVVQDALERvmVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLV 1233
Cdd:TIGR00958 653 EQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ--GCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
662-978 |
2.42e-114 |
|
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: 359.46 E-value: 2.42e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 662 LAMNLPEWKQALYGCISATLFGAIQPAYAYSLGSMVSVYFLTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMG 741
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 742 EYLTKRIRERMLSKVLTFEVGWFDRDENSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVM 821
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 822 IAVQPVIIVCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFG 901
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 902 LAMSQSLTSCTWALDFWYGGRLIQDGYITAKALFETFMILVSTGRVIADAGSMTTDLAKGSDAVGSVFAVLDRYTSI 978
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
359-593 |
2.95e-110 |
|
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: 344.98 E-value: 2.95e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTI 518
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 519 LLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQYSTL 593
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
330-603 |
7.27e-108 |
|
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: 352.59 E-value: 7.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 330 ERIMEVINRVPKIdSDNPDGHKLEKIRGEVEFKNVKFVY-PSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQ 408
Cdd:COG5265 330 ERMFDLLDQPPEV-ADAPDAPPLVVGGGEVRFENVSFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 409 RFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYE 488
Cdd:COG5265 406 RFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 489 TQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVV 568
Cdd:COG5265 486 TRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVL 565
|
250 260 270
....*....|....*....|....*....|....*
gi 15229473 569 KNGHIVETGSHDELMENiDGQYSTLVHLQQIEKQD 603
Cdd:COG5265 566 EAGRIVERGTHAELLAQ-GGLYAQMWARQQEEEEA 599
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
995-1232 |
3.05e-103 |
|
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: 326.11 E-value: 3.05e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAGTIRENIIYGgvSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG--RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1155 SVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSL 1232
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG--GVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-597 |
8.79e-100 |
|
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: 329.37 E-value: 8.79e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 32 WLLMGLGLIGAVGDGFTTPLVLLITSKLMNniGGSSFNTDTFMQSisknsVALLYVACGSW--VVCFLEGYCWTRTGERQ 109
Cdd:TIGR02203 13 KAGLVLAGVAMILVAATESTLAALLKPLLD--DGFGGRDRSVLWW-----VPLVVIGLAVLrgICSFVSTYLLSWVSNKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 110 TARMREKYLRAVLRQDVGYFDLH--------VTSTSDVITSVSSDSF--VIQDVLseklpnflmsasTFVGSYIVGFILL 179
Cdd:TIGR02203 86 VRDIRVRMFEKLLGLPVSFFDRQptgtllsrITFDSEQVASAATDAFivLVRETL------------TVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 180 WRLAIVGLpfIVLLVIPGLM--YGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGI 257
Cdd:TIGR02203 154 WQLTLIVV--VMLPVLSILMrrVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 258 KQGLAKGITIgsngitfAMWGFMSWYGSRMVMY---HGAQGGTV----FAVAAAIAIGGVSLGGGLSNLKYFFEAASVG- 329
Cdd:TIGR02203 232 KMTSAGSISS-------PITQLIASLALAVVLFialFQAQAGSLtagdFTAFITAMIALIRPLKSLTNVNAPMQRGLAAa 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 330 ERIMEVINRVPKIDsdnpDGHK-LEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQ 408
Cdd:TIGR02203 305 ESLFTLLDSPPEKD----TGTRaIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 409 RFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGK-EDASMDDVVEAAKASNAHNFISQLPNGY 487
Cdd:TIGR02203 380 RFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 488 ETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISV 567
Cdd:TIGR02203 460 DTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVV 539
|
570 580 590
....*....|....*....|....*....|
gi 15229473 568 VKNGHIVETGSHDELMENiDGQYSTLVHLQ 597
Cdd:TIGR02203 540 MDDGRIVERGTHNELLAR-NGLYAQLHNMQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
359-597 |
1.03e-98 |
|
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: 313.78 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVY-PSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQM 437
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPT 517
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 518 ILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQYSTLVHLQ 597
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
357-584 |
1.73e-97 |
|
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: 310.31 E-value: 1.73e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:cd03254 1 GEIEFENVNFSYDE--KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 517 TILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELME 584
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
968-1236 |
1.14e-96 |
|
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: 321.77 E-value: 1.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 968 VFAVLDRytSIDPEDPDGYETERIT-GQVEFLDVDFSY-PTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIER 1045
Cdd:COG5265 332 MFDLLDQ--PPEVADAPDAPPLVVGgGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1046 FYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYG--GVSD----------KIdeaeiieaakaan 1113
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrpDASEeeveaaaraaQI------------- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1114 aHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHR 1193
Cdd:COG5265 474 -HDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHR 552
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15229473 1194 LSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVSLQ 1236
Cdd:COG5265 553 LSTIVDADEILVLEAGRIVERGTHAELLAQG--GLYAQMWARQ 593
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
995-1236 |
3.46e-95 |
|
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: 304.15 E-value: 3.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAGTIRENIIYG--GVSDKideaEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLK 1152
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGrpDATDE----EVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1153 NPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSL 1232
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG--GLYAEM 232
|
....
gi 15229473 1233 VSLQ 1236
Cdd:cd03253 233 WKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
324-585 |
2.39e-92 |
|
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: 308.61 E-value: 2.39e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 324 EAASVGERIMEVINR-VPKIDSDNPDGHKLEKIrgEVEFKNVKFVYPSRleTSIFDDFCLRVPSGKTVALVGGSGSGKST 402
Cdd:COG4988 303 NGIAAAEKIFALLDApEPAAPAGTAPLPAAGPP--SIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 403 VISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQ 482
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 483 LPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNA 562
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|...
gi 15229473 563 DVISVVKNGHIVETGSHDELMEN 585
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
323-597 |
5.00e-91 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 305.73 E-value: 5.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 323 FEAASVGERIMEVINRVPKIDsDNPDGHKLEKIRGEVEFKNVKFVYPSRleTSIFDDFCLRVPSGKTVALVGGSGSGKST 402
Cdd:PRK13657 300 FMAAPKLEEFFEVEDAVPDVR-DPPGAIDLGRVKGAVEFDDVSFSYDNS--RQGVEDVSFEAKPGQTVAIVGPTGAGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 403 VISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQ 482
Cdd:PRK13657 377 LINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIER 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 483 LPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNA 562
Cdd:PRK13657 457 KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA 536
|
250 260 270
....*....|....*....|....*....|....*
gi 15229473 563 DVISVVKNGHIVETGSHDELMENiDGQYSTLVHLQ 597
Cdd:PRK13657 537 DRILVFDNGRVVESGSFDELVAR-GGRFAALLRAQ 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
993-1224 |
3.04e-90 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 290.67 E-value: 3.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 993 GQVEFLDVDFSYptRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRH 1072
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEPTLFAGTIRENIIYGgvSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLK 1152
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG--RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1153 NPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKG 1224
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
713-1236 |
8.62e-88 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 296.55 E-value: 8.62e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 713 RIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVVRSLVGDR 792
Cdd:PRK11176 65 KWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 793 MALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSS 872
Cdd:PRK11176 143 LITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 873 QERIMKMLEKAQESPRRESIRqswfagfgLAMSQSLTSctwaldfwyggRLIQdgYITAKAL--------FETFMILVST 944
Cdd:PRK11176 223 QEVETKRFDKVSNRMRQQGMK--------MVSASSISD-----------PIIQ--LIASLALafvlyaasFPSVMDTLTA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 945 GRVIADAGSM-------------TTDLAKGSDAVGSVFAVLDrytsIDPEDPDG-YETERITGQVEFLDVDFSYPTRpDV 1010
Cdd:PRK11176 282 GTITVVFSSMialmrplksltnvNAQFQRGMAACQTLFAILD----LEQEKDEGkRVIERAKGDIEFRNVTFTYPGK-EV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1011 IIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIREN 1090
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 IIYGgVSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQS 1170
Cdd:PRK11176 437 IAYA-RTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1171 ERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVSLQ 1236
Cdd:PRK11176 516 ERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN--GVYAQLHKMQ 579
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
350-597 |
1.27e-86 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 293.46 E-value: 1.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 350 HKLEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQ 429
Cdd:PRK11176 333 RVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 430 VKWLRSQMGLVSQEPALFATTIKENILFGKEDA-SMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAI 508
Cdd:PRK11176 412 LASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDG 588
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NG 570
|
....*....
gi 15229473 589 QYSTLVHLQ 597
Cdd:PRK11176 571 VYAQLHKMQ 579
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
35-299 |
4.83e-86 |
|
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: 281.67 E-value: 4.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 35 MGLGLIGAVGDGFTTPLVLLITSKLMNNIGG---SSFNTDTFMQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQTA 111
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIV 191
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKN--GAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 192 LLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIG-SN 270
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGlLF 238
|
250 260
....*....|....*....|....*....
gi 15229473 271 GITFAMWGFMSWYGSRMVMYHGAQGGTVF 299
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVL 267
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
652-1225 |
1.63e-84 |
|
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: 286.65 E-value: 1.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 652 KPQLPSFKRLLAMNlpewkqALYGCISAtLFGAIQpayAYSLGSMVSVYFLtsHDEIKEKTRIYALSFVGLAVLSFLINI 731
Cdd:COG4988 9 KRLARGARRWLALA------VLLGLLSG-LLIIAQ---AWLLASLLAGLII--GGAPLSALLPLLGLLLAVLLLRALLAW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 732 SQHYNFAYMGEYLTKRIRERMLSKVltFEVGWFDRDENSSGAicsrlakdanvVRSLVGDRM-AL-------VVQTVSAV 803
Cdd:COG4988 77 LRERAAFRAAARVKRRLRRRLLEKL--LALGPAWLRGKSTGE-----------LATLLTEGVeALdgyfaryLPQLFLAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 804 TIAFTMGLVIA---WRLALVMIAVQPVIIVcFYtrrVLLKSMSKKAIKAQ-DESSKLAA---EAVSNVRTITAFSSQERI 876
Cdd:COG4988 144 LVPLLILVAVFpldWLSGLILLVTAPLIPL-FM---ILVGKGAAKASRRQwRALARLSGhflDRLRGLTTLKLFGRAKAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 877 MKMLEKAQESPRRESIRQswfagfgLAMSQsLTSCtwALDF----------WYGG-RLIqDGYITakaLFETFMILVstg 945
Cdd:COG4988 220 AERIAEASEDFRKRTMKV-------LRVAF-LSSA--VLEFfaslsialvaVYIGfRLL-GGSLT---LFAALFVLL--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 946 rvIA--------DAGSMTTDLAKGSDAVGSVFAVLDrytSIDPEDPDGYETERITG--QVEFLDVDFSYPTRPDVIifKN 1015
Cdd:COG4988 283 --LApefflplrDLGSFYHARANGIAAAEKIFALLD---APEPAAPAGTAPLPAAGppSIELEDVSFSYPGGRPAL--DG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1016 FSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYGg 1095
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1096 vSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQ 1175
Cdd:COG4988 435 -RPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEIL 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 15229473 1176 DALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGP 1225
Cdd:COG4988 514 QALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
108-596 |
1.07e-83 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 284.74 E-value: 1.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 108 RQTARMREKYLRAVLRQDVGYfdLHVTSTSDVITSVSSDSFVIQD----VLSeklPnFLMSASTFVGSYIVGFILLWRLA 183
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAG--LARLRSGDLLNRLVADVDALDNlylrVLL---P-LLVALLVILAAVAFLAFFSPALA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 184 IVGLPFIVL--LVIPGLMYgRALISISRKIREEYNEagfVAEQAISSVR-----TVY-AFSGERKTISKFSTALQGS-VK 254
Cdd:COG4987 159 LVLALGLLLagLLLPLLAA-RLGRRAGRRLAAARAA---LRARLTDLLQgaaelAAYgALDRALARLDAAEARLAAAqRR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 255 LGIKQGLAKGITIGSNGItfAMWGfMSWYGSRMVmYHGAQGGT-----VFAVAAAiaiggvslggglsnlkyfFEAASV- 328
Cdd:COG4987 235 LARLSALAQALLQLAAGL--AVVA-VLWLAAPLV-AAGALSGPllallVLAALAL------------------FEALAPl 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 329 -------------GERIMEVINRVPKIDSdnPDGHKLEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGG 395
Cdd:COG4987 293 paaaqhlgrvraaARRLNELLDAPPAVTE--PAEPAPAPGGPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 396 SGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASN 475
Cdd:COG4987 370 SGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 476 AHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHR 555
Cdd:COG4987 450 LGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15229473 556 LSTIRNADVISVVKNGHIVETGSHDELMENiDGQYSTLVHL 596
Cdd:COG4987 530 LAGLERMDRILVLEDGRIVEQGTHEELLAQ-NGRYRQLYQR 569
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
794-1235 |
1.28e-82 |
|
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: 281.65 E-value: 1.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 794 ALVVQTVSAVTIAFtMGLVIAWRLALVMIAVqpVIIVCFYTRRvLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQ 873
Cdd:COG4987 139 ALLVILAAVAFLAF-FSPALALVLALGLLLA--GLLLPLLAAR-LGRRAGRRLAAARAALRARLTDLLQGAAELAAYGAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 874 ERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYI----------TAKALFETFMILVS 943
Cdd:COG4987 215 DRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALsgpllallvlAALALFEALAPLPA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 944 ----TGRVIAdagsmttdlakgsdAVGSVFAVLDryTSIDPEDPDGYETERITGQVEFLDVDFSYPTRPDvIIFKNFSIK 1019
Cdd:COG4987 295 aaqhLGRVRA--------------AARRLNELLD--APPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLT 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1020 IEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYG--GVS 1097
Cdd:COG4987 358 LPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLArpDAT 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1098 DkideaeiieaAKAANA------HDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE 1171
Cdd:COG4987 438 D----------EELWAAlervglGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE 507
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1172 RVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVSL 1235
Cdd:COG4987 508 QALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN--GRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
359-597 |
2.46e-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: 268.97 E-value: 2.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:cd03252 1 ITFEHVRFRYKPD-GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTI 518
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 519 LLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQYSTLVHLQ 597
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
355-573 |
3.21e-81 |
|
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: 265.49 E-value: 3.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 355 IRGEVEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLR 434
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 435 SQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIK 514
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 515 SPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHI 573
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
799-1224 |
4.97e-81 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 278.00 E-value: 4.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 799 TVSAVTIAFTMGLVIAWRLALVMIAVqpVIIVCFYTRRVLLKSmskKAIKAQDES--SKLAA---EAVSNVRTITAFSsq 873
Cdd:PRK13657 140 TLVALVVLLPLALFMNWRLSLVLVVL--GIVYTLITTLVMRKT---KDGQAAVEEhyHDLFAhvsDAIGNVSVVQSYN-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 874 eRImkmleKAQESPRRESIRQ---------SWFAgFGLAMSQSLTSCTWALDFWYGGRLIQDGY-----ITAKALFETFM 939
Cdd:PRK13657 213 -RI-----EAETQALRDIADNllaaqmpvlSWWA-LASVLNRAASTITMLAILVLGAALVQKGQlrvgeVVAFVGFATLL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 940 IlvstGR---VIADAGSMTTDLAKGSDavgsVFAVLDRYTSIDpEDPDGYETERITGQVEFLDVDFSYP-TRPDViifKN 1015
Cdd:PRK13657 286 I----GRldqVVAFINQVFMAAPKLEE----FFEVEDAVPDVR-DPPGAIDLGRVKGAVEFDDVSFSYDnSRQGV---ED 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1016 FSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYG- 1094
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGr 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1095 -GVSDKideaEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERV 1173
Cdd:PRK13657 434 pDATDE----EMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1174 VQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKG 1224
Cdd:PRK13657 510 VKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARG 560
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
993-1211 |
4.78e-79 |
|
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: 259.33 E-value: 4.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 993 GQVEFLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRH 1072
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEPTLFAGTIRENIIYG--GVSDKideaEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAV 1150
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGlqSCSFE----CVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKL 1211
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
995-1210 |
7.78e-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: 253.46 E-value: 7.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIiFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV-LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAGTIRENIiyggvsdkideaeiieaakaanahdfitsltegydtycgdrgvqLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1155 SVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGK 1210
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
359-572 |
3.50e-76 |
|
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: 248.84 E-value: 3.50e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFATTIKENILfgkedasmddvveaakasnahnfisqlpngyetqvgergvqmSGGQKQRIAIARAIIKSPTI 518
Cdd:cd03228 80 YVPQDPFLFSGTIRENIL------------------------------------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15229473 519 LLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGH 572
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
352-600 |
9.98e-75 |
|
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: 262.76 E-value: 9.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 352 LEKIRGEVEFKNVKFVY-PSRLEtsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQV 430
Cdd:TIGR01846 449 LPELRGAITFENIRFRYaPDSPE--VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADP 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 431 KWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIAR 510
Cdd:TIGR01846 527 AWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIAR 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQY 590
Cdd:TIGR01846 607 ALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-QGLY 685
|
250
....*....|
gi 15229473 591 STLvHLQQIE 600
Cdd:TIGR01846 686 ARL-WQQQSG 694
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
995-1236 |
4.52e-73 |
|
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: 243.16 E-value: 4.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYptRPD-VIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHI 1073
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPTLFAGTIRENIIYGgvSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKN 1153
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA--DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1154 PSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLV 1233
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN--GLYAYLY 234
|
...
gi 15229473 1234 SLQ 1236
Cdd:cd03252 235 QLQ 237
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
723-1234 |
3.05e-72 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 256.02 E-value: 3.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 723 AVLSFLinisQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVVRSLVGDRMALVVQTVSA 802
Cdd:TIGR03796 208 GVLTWL----QLYYLRRLEIKLAVGMSARFLWHILRLPVRFFA--QRHAGDIASRVQLNDQVAEFLSGQLATTALDAVML 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 803 VTIAFTMgLVIAWRLALVMIAVQPVIIVCFytrRVLLKSMSKKAIKAQDESSKLAAEAVSNVR---TITAFSSQERIM-- 877
Cdd:TIGR03796 282 VFYALLM-LLYDPVLTLIGIAFAAINVLAL---QLVSRRRVDANRRLQQDAGKLTGVAISGLQsieTLKASGLESDFFsr 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 878 ------KMLEKAQESPRRESIrqswfagFGlAMSQSLTSCTWALDFWYGGRLIQDGYITAKAL--FETFMI--------L 941
Cdd:TIGR03796 358 wagyqaKLLNAQQELGVLTQI-------LG-VLPTLLTSLNSALILVVGGLRVMEGQLTIGMLvaFQSLMSsflepvnnL 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 942 VSTGRVIADagsMTTDLAKGSDavgsvfaVLDRYTSIDPEDPDGY-----ETERITGQVEFLDVDFSY-PTRPDVIifKN 1015
Cdd:TIGR03796 430 VGFGGTLQE---LEGDLNRLDD-------VLRNPVDPLLEEPEGSaatsePPRRLSGYVELRNITFGYsPLEPPLI--EN 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1016 FSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIY-- 1093
Cdd:TIGR03796 498 FSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLwd 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1094 GGVSDKideaeiIEAAKAANA--HDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE 1171
Cdd:TIGR03796 578 PTIPDA------DLVRACKDAaiHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1172 RVVQDALERVmvGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVS 1234
Cdd:TIGR03796 652 KIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVG--GAYARLIR 710
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
91-595 |
6.24e-72 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 255.25 E-value: 6.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 91 SWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFViQDVLSEKLPNFLMSASTFVG 170
Cdd:TIGR03796 207 QGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQR--HAGDIASRVQLNDQV-AEFLSGQLATTALDAVMLVF 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 171 SYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFS---- 246
Cdd:TIGR03796 284 YALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWAgyqa 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 247 TALQGSVKLGIKQGLAKGITIGSNGITFA---MWGFMSWYGSRMV--MYHGAQGgtvfavaaaiaiggvslggglsNLKY 321
Cdd:TIGR03796 364 KLLNAQQELGVLTQILGVLPTLLTSLNSAlilVVGGLRVMEGQLTigMLVAFQS----------------------LMSS 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 322 FFEAAsvgERIMEVINRVPKIDSD---------NPDGHKLE-------------KIRGEVEFKNVKFVYpSRLETSIFDD 379
Cdd:TIGR03796 422 FLEPV---NNLVGFGGTLQELEGDlnrlddvlrNPVDPLLEepegsaatsepprRLSGYVELRNITFGY-SPLEPPLIEN 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 380 FCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENI-LFg 458
Cdd:TIGR03796 498 FSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtLW- 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 459 keDASM--DDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVV 536
Cdd:TIGR03796 577 --DPTIpdADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 537 QEALENAsiGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMEnIDGQYSTLVH 595
Cdd:TIGR03796 655 DDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWA-VGGAYARLIR 710
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
343-594 |
1.21e-69 |
|
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: 245.18 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 343 DSDNP-DGHKLEKIRGEVEFKNVKFVYPSRLEtSIFDdFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILID 421
Cdd:TIGR01192 318 QREEPaDAPELPNVKGAVEFRHITFEFANSSQ-GVFD-VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILID 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 422 GVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGG 501
Cdd:TIGR01192 396 GIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 502 QKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDE 581
Cdd:TIGR01192 476 ERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQE 555
|
250
....*....|...
gi 15229473 582 LMeNIDGQYSTLV 594
Cdd:TIGR01192 556 LI-QKDGRFYKLL 567
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
330-1233 |
5.43e-69 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 255.29 E-value: 5.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 330 ERIMEVINRVPKIDSDNPdghKLEKIRGEVEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISllqr 409
Cdd:PLN03232 589 QRIEELLLSEERILAQNP---PLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS---- 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 410 fydPLAGEIL-IDGVSIDklqvkwLRSQMGLVSQEPALFATTIKENILFGkEDASMDDVVEAAKASNAHNFISQLPNGYE 488
Cdd:PLN03232 662 ---AMLGELShAETSSVV------IRGSVAYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 489 TQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSE-SERVVQEALENASIGRTTILIAHRLSTIRNADVISV 567
Cdd:PLN03232 732 TEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIIL 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 568 VKNGHIVETGSHDEL----------MENIDGQYSTlvhlQQIEKQDINVSvKIGPISdpSKDIRNSSRVSTLsRSSSANS 637
Cdd:PLN03232 812 VSEGMIKEEGTFAELsksgslfkklMENAGKMDAT----QEVNTNDENIL-KLGPTV--TIDVSERNLGSTK-QGKRGRS 883
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 638 VTgpstIKNlsEDNKPQLPSFKRLLamnlpEWKQALYGC-ISATLFGAIQPAYAYSLGSMVSVYFLTSHDEIKEKTR--- 713
Cdd:PLN03232 884 VL----VKQ--EERETGIISWNVLM-----RYNKAVGGLwVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPgfy 952
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 714 --IYALSFVGLAVLSF-----LINISQHynfaymgeyLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANV-- 784
Cdd:PLN03232 953 ivVYALLGFGQVAVTFtnsfwLISSSLH---------AAKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKDIGDid 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 785 --VRSLVGDRMALVVQTVSAVTIAFTMGLVIAWrlalvmiAVQPVIIVcFYTRRVLLKSMSKKaIKAQDESSK-----LA 857
Cdd:PLN03232 1022 rnVANLMNMFMNQLWQLLSTFALIGTVSTISLW-------AIMPLLIL-FYAAYLYYQSTSRE-VRRLDSVTRspiyaQF 1092
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 858 AEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGgrLIQDGYITAKALFET 937
Cdd:PLN03232 1093 GEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFA--VLRNGNAENQAGFAS 1170
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 938 FM-ILVSTGRVIADAgsMTTDLAKGSDAVGSVFAV--LDRYTSIDPEDPDGYETER------ITGQVEFLDVDFSY-PTR 1007
Cdd:PLN03232 1171 TMgLLLSYTLNITTL--LSGVLRQASKAENSLNSVerVGNYIDLPSEATAIIENNRpvsgwpSRGSIKFEDVHLRYrPGL 1248
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTI 1087
Cdd:PLN03232 1249 PPVL--HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTV 1326
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIiyGGVSDKIDEAEIIEAAkaaNAH--DFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PLN03232 1327 RFNI--DPFSEHNDADLWEALE---RAHikDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1166 LDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKgPTGIYFSLV 1233
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR-DTSAFFRMV 1468
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
359-1232 |
5.83e-69 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 255.26 E-value: 5.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYpSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGvsidklqvkwlrsQMG 438
Cdd:TIGR00957 637 ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFATTIKENILFGK--EDASMDDVVEAAKASNAhnfISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKalNEKYYQQVLEACALLPD---LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 517 TILLLDEATSALDSESERVVQEAL---ENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQYSTL 593
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR-DGAFAEF 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 594 VHL-----QQIEKQDINVSVKIGPiSDPSKDIRNSSRVS-----TLSRSSSANSVTGPSTIKNLSEDNKPQLPSFKRLlA 663
Cdd:TIGR00957 859 LRTyapdeQQGHLEDSWTALVSGE-GKEAKLIENGMLVTdvvgkQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEE-T 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 664 MNLPEWKQALYGCISATLFGAIQPAYAYSLGSMVSVYFLTSH-------------------DEIKEKTRIYALSFVGLAV 724
Cdd:TIGR00957 937 WKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHvsalasnywlslwtddpmvNGTQNNTSLRLSVYGALGI 1016
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 725 LSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGD--RMAL-----VV 797
Cdd:TIGR00957 1017 LQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFER--TPSGNLVNRFSKELDTVDSMIPPviKMFMgslfnVI 1094
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 798 QTVSAVTIAFTMGLVIAWRLALVMIAVQPviivcFY--TRRVL--LKSMSKKAIKAQdessklAAEAVSNVRTITAFSSQ 873
Cdd:TIGR00957 1095 GALIVILLATPIAAVIIPPLGLLYFFVQR-----FYvaSSRQLkrLESVSRSPVYSH------FNETLLGVSVIRAFEEQ 1163
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 874 ERIMKMLE-KAQESPRresirqswfagfglAMSQSLTSCTW-ALDFWYGGRLIqdgyitakALFETFMILVS-------- 943
Cdd:TIGR00957 1164 ERFIHQSDlKVDENQK--------------AYYPSIVANRWlAVRLECVGNCI--------VLFAALFAVISrhslsagl 1221
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 944 TGRVIADAGSMTTDL----AKGSDAVGSVFAV--LDRYTSIDPEDPDGYETERI------TGQVEFLDVDFSYptRPDV- 1010
Cdd:TIGR00957 1222 VGLSVSYSLQVTFYLnwlvRMSSEMETNIVAVerLKEYSETEKEAPWQIQETAPpsgwppRGRVEFRNYCLRY--REDLd 1299
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1011 IIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIREN 1090
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN 1379
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 I-IYGGVSDKideaEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQ 1169
Cdd:TIGR00957 1380 LdPFSQYSDE----EVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1170 SERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKgpTGIYFSL 1232
Cdd:TIGR00957 1456 TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ--RGIFYSM 1516
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
716-1237 |
7.52e-68 |
|
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: 243.11 E-value: 7.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 716 ALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRDEnsSGAICSRLAKDANVVRSLVGDRMAL 795
Cdd:TIGR01846 182 ALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRR--VGDTVARVRELEQIRNFLTGSALTV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 796 VVQTVSAVTIAFTMglviaWRLALVMIAVQPVIIVCFYTRRVLLKSMSKKAIKAQDESS----KLAAEAVSNVRTI--TA 869
Cdd:TIGR01846 260 VLDLLFVVVFLAVM-----FFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSaaatSFLVESVTGIETIkaTA 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 870 FSSQ--ERIMKMLEKAQESPRRESIRQSWfAGFGLAMSQSLTSctwALDFWYGGRLIQDGYITAKALFETFMIlvsTGRV 947
Cdd:TIGR01846 335 TEPQfqNRWDRQLAAYVAASFRVTNLGNI-AGQAIELIQKLTF---AILLWFGAHLVIGGALSPGQLVAFNML---AGRV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 948 IADAGSMTT---DLAKGSDAVGSVFAVLDryTSIDPEDPDGYETERITGQVEFLDVDFSY-PTRPDVIifKNFSIKIEEG 1023
Cdd:TIGR01846 408 TQPVLRLAQlwqDFQQTGIALERLGDILN--SPTEPRSAGLAALPELRGAITFENIRFRYaPDSPEVL--SNLNLDIKPG 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1024 KSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYGgvSDKIDEA 1103
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC--NPGAPFE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1104 EIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV 1183
Cdd:TIGR01846 562 HVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR 641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1184 GRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVSLQT 1237
Cdd:TIGR01846 642 GRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ--GLYARLWQQQS 693
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
357-577 |
2.84e-66 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 222.85 E-value: 2.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 517 TILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETG 577
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
330-1223 |
1.49e-65 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 244.65 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 330 ERIMEVINRVPKIDSDNPdghKLEKIRGEVEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQR 409
Cdd:PLN03130 589 KRLEELLLAEERVLLPNP---PLEPGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 410 FYDPLAGEILIdgvsidklqvkwLRSQMGLVSQEPALFATTIKENILFGKE-DASMDDvvEAAKASNAHNFISQLPNGYE 488
Cdd:PLN03130 666 ELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 489 TQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESER-VVQEALENASIGRTTILIAHRLSTIRNADVISV 567
Cdd:PLN03130 732 TEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRqVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIIL 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 568 VKNGHIVETGSHDELMENIDGQYSTLVHLQQIEKQDINVSVKIGPiSDPSKDIRNSsRVSTLSRSSSA--NSVTGPST-I 644
Cdd:PLN03130 812 VHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEENGEEEDD-QTSSKPVANG-NANNLKKDSSSkkKSKEGKSVlI 889
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 645 KnlSEDNKPQLPSFKRLLamnlpEWKQALYGC-ISATLFGAIQPAYAYSLGSMVSVYFLTSHDEIKEKTRIYALSFVGLa 723
Cdd:PLN03130 890 K--QEERETGVVSWKVLE-----RYKNALGGAwVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKTHGPLFYNLIYAL- 961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 724 vLSF---LINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKD--------ANVVRSLVGDR 792
Cdd:PLN03130 962 -LSFgqvLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFH--TNPLGRIINRFAKDlgdidrnvAVFVNMFLGQI 1038
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 793 MALVvQTVSAVTIAFTMGLviaWrlalvmiAVQPVIIVcFY---------TRRV-LLKSMSKKAIKAQdessklAAEAVS 862
Cdd:PLN03130 1039 FQLL-STFVLIGIVSTISL---W-------AIMPLLVL-FYgaylyyqstAREVkRLDSITRSPVYAQ------FGEALN 1100
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 863 NVRTITAFSSQERIMKMLEKAQESprreSIRqswfagFGLAMSQSLTSCTWALDFwYGGRLI---------QDGYITAKA 933
Cdd:PLN03130 1101 GLSTIRAYKAYDRMAEINGRSMDN----NIR------FTLVNMSSNRWLAIRLET-LGGLMIwltasfavmQNGRAENQA 1169
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 934 LFETFM-ILVSTGRVIAdaGSMTTDLAKGSDAVGSVFAV--LDRYTSIDPEDPDGYETER------ITGQVEFLDVDFSY 1004
Cdd:PLN03130 1170 AFASTMgLLLSYALNIT--SLLTAVLRLASLAENSLNAVerVGTYIDLPSEAPLVIENNRpppgwpSSGSIKFEDVVLRY 1247
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1005 -PTRPDVIIFKNFSIKIEEgkSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLF 1083
Cdd:PLN03130 1248 rPELPPVLHGLSFEISPSE--KVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLF 1325
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AGTIRENIIYGGVSDKIDeaeiiEAAKAANAH--DFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:PLN03130 1326 SGTVRFNLDPFNEHNDAD-----LWESLERAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1162 ATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:PLN03130 1401 ATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-598 |
6.18e-63 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 236.08 E-value: 6.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 21 RSIFMHADgvDWLLMGLGLIGAvgdGFTTPLVLLITSKLMnnigGSSFNTDTFMQSISKNSVALLYVACGSWVVCFLEGY 100
Cdd:PTZ00265 818 REIFSYKK--DVTIIALSILVA---GGLYPVFALLYAKYV----STLFDFANLEANSNKYSLYILVIAIAMFISETLKNY 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 101 CWTRTGERQTARMREKYLRAVLRQDVGYFDLHVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLW 180
Cdd:PTZ00265 889 YNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 181 RLAIV--GLPFIVLLVIPGlmygRALISISRKI-REEYNEAG----------------FVAEQAISSVRTVYAFSGERKT 241
Cdd:PTZ00265 969 IVAAVltGTYFIFMRVFAI----RARLTANKDVeKKEINQPGtvfaynsddeifkdpsFLIQEAFYNMNTVIIYGLEDYF 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 242 ISKFSTALQGSVKLGIKQGLAKGITIG-SNGITFAMWGFMSWYGSRMVmyhgaQGGTV----FAVAAAIAIGGVSLGGGL 316
Cdd:PTZ00265 1045 CNLIEKAIDYSNKGQKRKTLVNSMLWGfSQSAQLFINSFAYWFGSFLI-----RRGTIlvddFMKSLFTFLFTGSYAGKL 1119
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 317 SNLKYFFEAASVG-ERIMEVINRVPKIDSDNPDGHKLEK---IRGEVEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVAL 392
Cdd:PTZ00265 1120 MSLKGDSENAKLSfEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAI 1199
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 393 VGGSGSGKSTVISLLQRFYD------------------------------------------------------PLAGEI 418
Cdd:PTZ00265 1200 VGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKI 1279
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 419 LIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQM 498
Cdd:PTZ00265 1280 LLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSL 1359
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 499 SGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENA--SIGRTTILIAHRLSTIRNADVISVVKN----GH 572
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGS 1439
|
650 660
....*....|....*....|....*..
gi 15229473 573 IVET-GSHDELMENIDGQYSTLVHLQQ 598
Cdd:PTZ00265 1440 FVQAhGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
358-568 |
1.07e-61 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 220.62 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSRleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQM 437
Cdd:TIGR02857 321 SLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPT 517
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 518 ILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVV 568
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
993-1215 |
1.14e-61 |
|
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: 209.75 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 993 GQVEFLDVDFSYPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRH 1072
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEPTLFAGTIRENIIYGGVSdkIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLK 1152
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1153 NPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERG 1215
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
737-1206 |
1.07e-60 |
|
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: 217.54 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 737 FAYMGEYLTKR--------IRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDanvVRSLVGDRMALVVQTVSAVTIAFT 808
Cdd:TIGR02857 60 LGWLQERAAARaaaavksqLRERLLEAVAALGPRWLQG--RPSGELATLALEG---VEALDGYFARYLPQLVLAVIVPLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 809 MGLVIA---WRLALVMIAVQPVIIVcFYtrrVLLKSMSKKAIKAQ-DESSKLAA---EAVSNVRTITAFSSQERIMKMLE 881
Cdd:TIGR02857 135 ILAAVFpqdWISGLILLLTAPLIPI-FM---ILIGWAAQAAARKQwAALSRLSGhflDRLRGLPTLKLFGRAKAQAAAIR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 882 KAQESPRRESI---RQSWFAGFGL----AMSQSLTSCTWALDFWYGGRLIQDGY---ITAKALFETfmilvstgrvIADA 951
Cdd:TIGR02857 211 RSSEEYRERTMrvlRIAFLSSAVLelfaTLSVALVAVYIGFRLLAGDLDLATGLfvlLLAPEFYLP----------LRQL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 952 GSMTTDLAKGSDAVGSVFAVLDRYTSIDPEDPDGYETERItgQVEFLDVDFSYPTRPDVIifKNFSIKIEEGKSTAIVGP 1031
Cdd:TIGR02857 281 GAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPAS--SLEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGP 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1032 SGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYG--GVSDkideAEIIEAA 1109
Cdd:TIGR02857 357 SGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLArpDASD----AEIREAL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1110 KAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVV 1189
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
|
490
....*....|....*..
gi 15229473 1190 IAHRLSTIQNCDAIAVL 1206
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
331-600 |
1.20e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 218.81 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 331 RIMEVINRVPKIDsdnpDGHK-LEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQR 409
Cdd:PRK10789 289 RIRAMLAEAPVVK----DGSEpVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 410 FYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYET 489
Cdd:PRK10789 364 HFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDT 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 490 QVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVK 569
Cdd:PRK10789 444 EVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQ 523
|
250 260 270
....*....|....*....|....*....|.
gi 15229473 570 NGHIVETGSHDELMENiDGQYSTLVHLQQIE 600
Cdd:PRK10789 524 HGHIAQRGNHDQLAQQ-SGWYRDMYRYQQLE 553
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
330-597 |
7.92e-60 |
|
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: 219.06 E-value: 7.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 330 ERIMEVINRVPKIDSDNPDGHKLekiRGEVEFKNVKFVYP--SRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLL 407
Cdd:TIGR03797 426 ERAKPILEALPEVDEAKTDPGKL---SGAIEVDRVTFRYRpdGPL---ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 408 QRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILfGKEDASMDDVVEAAKASNAHNFISQLPNGY 487
Cdd:TIGR03797 500 LGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAEDIRAMPMGM 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 488 ETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRttILIAHRLSTIRNADVISV 567
Cdd:TIGR03797 579 HTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYV 656
|
250 260 270
....*....|....*....|....*....|
gi 15229473 568 VKNGHIVETGSHDELMEnIDGQYSTLVHLQ 597
Cdd:TIGR03797 657 LDAGRVVQQGTYDELMA-REGLFAQLARRQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
357-578 |
2.86e-59 |
|
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: 203.11 E-value: 2.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPSRLETSIfDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFATTIKENI-LFGKedASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKS 515
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 516 PTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGS 578
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
993-1216 |
3.03e-59 |
|
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: 203.11 E-value: 3.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 993 GQVEFLDVDFSY-PTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRR 1071
Cdd:cd03244 1 GDIEFKNVSLRYrPNLPPVL--KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTLFAGTIRENI-IYGGVSDKideaeiIEAAKAANAH--DFITSLTEGYDTYCGDRGVQLSGGQKQRIAIAR 1148
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdPFGEYSDE------ELWQALERVGlkEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1149 AVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
793-1233 |
3.15e-59 |
|
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: 215.14 E-value: 3.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 793 MALVVQTVSAVTIAFTMGlviaWRLALVMIAVQpvIIVCFYTRRVLLKSMSKKAIKAQDESSKLA--AEAVSNVRTITAF 870
Cdd:TIGR01192 138 LATFVALFLLIPTAFAMD----WRLSIVLMVLG--ILYILIAKLVMQRTKNGQAAVEHHYHNVFKhvSDSISNVSVVHSY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 871 SSQERIMKMLEKAQES--PRRESIRQSWFAGFGLAMSQSLTSCTWALDFwyGGRLIQDGYITAKAL-----FETFMIlvs 943
Cdd:TIGR01192 212 NRIEAETSALKQFTNNllSAQYPVLDWWALASGLNRMASTISMMCILVI--GTVLVIKGELSVGEViafigFANLLI--- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 944 tGRViaDAGSMTTDLAKGSDAVGSVFAVLDRYTSIDPEDPDGYETERITGQVEFLDVDFSYPTRPDVIifKNFSIKIEEG 1023
Cdd:TIGR01192 287 -GRL--DQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELPNVKGAVEFRHITFEFANSSQGV--FDVSFEAKAG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1024 KSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYG--GVSDKid 1101
Cdd:TIGR01192 362 QTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGreGATDE-- 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1102 eaEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV 1181
Cdd:TIGR01192 440 --EVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDAL 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1182 MVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLV 1233
Cdd:TIGR01192 518 RKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKD--GRFYKLL 567
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
666-1239 |
5.07e-59 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 223.37 E-value: 5.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 666 LPEWKQALYGC--ISATLFGAIQPAYayslgsmVSVY-FLTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGE 742
Cdd:PTZ00265 54 LPASHRKLLGVsfVCATISGGTLPFF-------VSVFgVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 743 YLTKRIRERMLSKVLtFEVGWFdRDENSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMI 822
Cdd:PTZ00265 127 KILKTLKLEFLKSVF-YQDGQF-HDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCIT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 823 AVQPVIIVCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGL 902
Cdd:PTZ00265 205 CVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 903 AMSQSLTSCTWALDFWYGGRLIQDGYITAKA----------------LFETFMILVSTGRViadagsmtTDLAKGSDAVG 966
Cdd:PTZ00265 285 GMINGFILASYAFGFWYGTRIIISDLSNQQPnndfhggsvisillgvLISMFMLTIILPNI--------TEYMKSLEATN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 967 SVFAVLDRYTSIDPEDpDGYETERITgQVEFLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERF 1046
Cdd:PTZ00265 357 SLYEIINRKPLVENND-DGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1047 YDPLKGIVKI-DGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIY-------------------------------- 1093
Cdd:PTZ00265 435 YDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqenknkrnsc 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1094 -----GGVSD------------------KIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAV 1150
Cdd:PTZ00265 515 rakcaGDLNDmsnttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAI 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAHRLSTIQNCDAIAVL---------------------- 1206
Cdd:PTZ00265 595 IRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdn 674
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1207 ----------DKGK---------------LVERGTHSSLLsKGPTGIYFSLVSLQTTS 1239
Cdd:PTZ00265 675 kennnknnkdDNNNnnnnnnnkinnagsyIIEQGTHDALM-KNKNGIYYTMINNQKVS 731
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
675-968 |
7.89e-59 |
|
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: 204.63 E-value: 7.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 675 GCISATLFGAIQPAYAYSLGSMVSVY-----FLTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIR 749
Cdd:cd18577 4 GLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 750 ERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVII 829
Cdd:cd18577 84 KRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 830 VCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLT 909
Cdd:cd18577 162 IVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFII 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 910 SCTWALDFWYGGRLIQDGYITAKALFETFMILVSTGRVIADAGSMTTDLAKGSDAVGSV 968
Cdd:cd18577 242 FAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
31-299 |
1.03e-58 |
|
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: 204.99 E-value: 1.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 31 DWLLMGLGLIGAVGDGFTTPLVLLITSKLMNNIggSSFNTDTFMQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQT 110
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVF--SLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 111 ARMREKYLRAVLRQDVGYFDLHVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFI 190
Cdd:cd18578 85 RRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 191 VLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIG-S 269
Cdd:cd18578 165 PLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGlS 244
|
250 260 270
....*....|....*....|....*....|
gi 15229473 270 NGITFAMWGFMSWYGSRMVMYHGAQGGTVF 299
Cdd:cd18578 245 QSLTFFAYALAFWYGGRLVANGEYTFEQFF 274
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
382-598 |
1.49e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 210.09 E-value: 1.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYdPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKED 461
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPD 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 462 ASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE 541
Cdd:PRK11174 450 ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 542 NASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQYSTLVHLQQ 598
Cdd:PRK11174 530 AASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQA-GGLFATLLAHRQ 585
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
652-1236 |
1.75e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 209.96 E-value: 1.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 652 KPQLPSFKRLLAMNLPeWKQALyGCISATLFGAiqpAYAYSLGSMVSVYFLtshDEIKEKTRI-------YALSFVGLAV 724
Cdd:PRK10790 5 SQLWPTLKRLLAYGSP-WRKPL-GLAVLMLWVA---AAAEVSGPLLISYFI---DNMVAKGNLplglvagLAAAYVGLQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 725 LSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVgdrmalvVQTVSAV- 803
Cdd:PRK10790 77 LAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDT--QPVGQLISRVTNDTEVIRDLY-------VTVVATVl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 804 -TIAFTMGLVIA-----WRLALVMIAVQPVIIVC------FYT---RRVllksmskkaikaqdeSSKLA------AEAVS 862
Cdd:PRK10790 148 rSAALIGAMLVAmfsldWRMALVAIMIFPAVLVVmviyqrYSTpivRRV---------------RAYLAdindgfNEVIN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 863 NVRTITAFSSQERIMKMLEKAQES---PRRESIRqswFAGFGLAMSQSLTS----CTWALDFWYGGR-LIQDGYITAkal 934
Cdd:PRK10790 213 GMSVIQQFRQQARFGERMGEASRShymARMQTLR---LDGFLLRPLLSLFSalilCGLLMLFGFSASgTIEVGVLYA--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 935 FETFMilvstGRVIADAGSMTTDLAKGSDAVGS---VFAVLDRytsidPEDPDGYETERIT-GQVEFLDVDFSYptRPDV 1010
Cdd:PRK10790 287 FISYL-----GRLNEPLIELTTQQSMLQQAVVAgerVFELMDG-----PRQQYGNDDRPLQsGRIDIDNVSFAY--RDDN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1011 IIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIREN 1090
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLAN 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 IIYGgvsDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQS 1170
Cdd:PRK10790 435 VTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1171 ERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKgpTGIYFSLVSLQ 1236
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA--QGRYWQMYQLQ 575
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
330-584 |
1.87e-56 |
|
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: 206.14 E-value: 1.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 330 ERIMEVINRVPkidsDNPDGHKLEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQR 409
Cdd:COG4618 306 RRLNELLAAVP----AEPERMPLPRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 410 FYDPLAGEILIDGVSIDKlqvkWLRSQ----MGLVSQEPALFATTIKENI-LFGkeDASMDDVVEAAKASNAHNFISQLP 484
Cdd:COG4618 381 VWPPTAGSVRLDGADLSQ----WDREElgrhIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 485 NGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENA-SIGRTTILIAHRLSTIRNAD 563
Cdd:COG4618 455 DGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVD 534
|
250 260
....*....|....*....|.
gi 15229473 564 VISVVKNGHIVETGSHDELME 584
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-595 |
2.39e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 206.21 E-value: 2.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 330 ERIMEVINRVPKIDSdnPDGHKLEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQR 409
Cdd:PRK11160 312 RRINEITEQKPEVTF--PTTSTAAADQVSLTLNNVSFTYPDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 410 FYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQlPNGYET 489
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 490 QVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVK 569
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMD 547
|
250 260
....*....|....*....|....*.
gi 15229473 570 NGHIVETGSHDELMENiDGQYSTLVH 595
Cdd:PRK11160 548 NGQIIEQGTHQELLAQ-QGRYYQLKQ 572
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
112-610 |
4.41e-56 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 205.72 E-value: 4.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFI- 190
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFp 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 191 -VLLVIpgLMYGRALISISRKIRE---EYNEaGFvaEQAISSVRTVYAFS-----GE----------------------- 238
Cdd:PRK10790 177 aVLVVM--VIYQRYSTPIVRRVRAylaDIND-GF--NEVINGMSVIQQFRqqarfGErmgeasrshymarmqtlrldgfl 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 239 -RKTISKFSTA-LQGsvkLGIKQGLAKGITIGSnGITFAmwgFMSWYG----------SRMVMYHgaqggtvfavaaaia 306
Cdd:PRK10790 252 lRPLLSLFSALiLCG---LLMLFGFSASGTIEV-GVLYA---FISYLGrlneplieltTQQSMLQ--------------- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 307 iggvslggglsnlkyffEAASVGERIMEVINRvPKIDSDNpDGHKLEKirGEVEFKNVKFVYpsRLETSIFDDFCLRVPS 386
Cdd:PRK10790 310 -----------------QAVVAGERVFELMDG-PRQQYGN-DDRPLQS--GRIDIDNVSFAY--RDDNLVLQNINLSVPS 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 387 GKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKeDASMDD 466
Cdd:PRK10790 367 RGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 467 VVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIG 546
Cdd:PRK10790 446 VWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 547 RTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENiDGQYSTLVHLQQIeKQDINVSVKI 610
Cdd:PRK10790 526 TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMYQLQLA-GEELAASVRE 587
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1015-1220 |
1.15e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 204.31 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKieEGKSTAIVGPSGSGKSTIIGLIERFYdPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYG 1094
Cdd:PRK11174 370 NFTLP--AGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1095 GVSdkIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVV 1174
Cdd:PRK11174 447 NPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15229473 1175 QDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSL 1220
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
795-1232 |
2.93e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 202.75 E-value: 2.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 795 LVVQTVSAVTIAFTMGLVIAW---RLALV----MIAVQPVIIVCFYTrrvLLKSMSKKAIKAQDESSKLAAEAVSNVRTI 867
Cdd:PRK11160 137 LISPLVAALVVILVLTIGLSFfdlTLALTlggiLLLLLLLLPLLFYR---LGKKPGQDLTHLRAQYRVQLTEWLQGQAEL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 868 TAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYITAK--ALFeTFMILVSTg 945
Cdd:PRK11160 214 TLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAGGVGGNAQPGAliALF-VFAALAAF- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 946 rviadagSMTTDLAKGSDAVGSVFAVLDRYTSI-----DPEDPDGYETERITGQVEFLDVDFSYPTRPDVIIfKNFSIKI 1020
Cdd:PRK11160 292 -------EALMPVAGAFQHLGQVIASARRINEIteqkpEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVL-KGLSLQI 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1021 EEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIYGgvsdki 1100
Cdd:PRK11160 364 KAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLA------ 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1101 deaeiieaakAANAHD--FITSLT-----------EGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK11160 438 ----------APNASDeaLIEVLQqvgleklleddKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1168 SQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSL 1232
Cdd:PRK11160 508 AETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQ--GRYYQL 570
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
794-1236 |
2.34e-54 |
|
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: 202.88 E-value: 2.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 794 ALVVQTVSAVTIAFTMGLVIA--WRLALVMIAVQPVIIVCFYTRRVLLKSMSKKAikaQDESSKLAAEAVSNVRTIT--- 868
Cdd:TIGR03797 252 STLTTLLSGIFALLNLGLMFYysWKLALVAVALALVAIAVTLVLGLLQVRKERRL---LELSGKISGLTVQLINGISklr 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 869 -------AFSsqeRIMKMLEKAQESPRRESIRQSWFAGFGLAMsQSLTSctwALDFWYGGRLIQDGYITAkALFETFMIl 941
Cdd:TIGR03797 329 vagaenrAFA---RWAKLFSRQRKLELSAQRIENLLTVFNAVL-PVLTS---AALFAAAISLLGGAGLSL-GSFLAFNT- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 942 vSTGRVIADAGSMttdlakgSDAVGSVFAVLDRYTSIDP--EDPDGYETERI-----TGQVEFLDVDFSYptRPD-VIIF 1013
Cdd:TIGR03797 400 -AFGSFSGAVTQL-------SNTLISILAVIPLWERAKPilEALPEVDEAKTdpgklSGAIEVDRVTFRY--RPDgPLIL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIIy 1093
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA- 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1094 GGVSDKIDEAEIIEAAKAAnAHDfITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERV 1173
Cdd:TIGR03797 549 GGAPLTLDEAWEAARMAGL-AED-IRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAI 626
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1174 VQDALERVMVgrTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptGIYFSLVSLQ 1236
Cdd:TIGR03797 627 VSESLERLKV--TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE--GLFAQLARRQ 685
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
379-1233 |
3.27e-54 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 208.09 E-value: 3.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 379 DFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEIlidgvsidklqvkWLRSQMGLVSQEPALFATTIKENILF- 457
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNILFf 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 458 GKEDASmdDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSE-SERVV 536
Cdd:PTZ00243 745 DEEDAA--RLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVV 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 537 QEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENidGQYSTLVHLQQIEKQDINvsvkigpiSDP 616
Cdd:PTZ00243 823 EECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT--SLYATLAAELKENKDSKE--------GDA 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 617 SKDIRNSSRVSTLSRSSSANSVTGPStiKNLSEDNKPQLPSFKRLLAM------NLP--EWKQALYGCISATLFGAIQPA 688
Cdd:PTZ00243 893 DAEVAEVDAAPGGAVDHEPPVAKQEG--NAEGGDGAALDAAAGRLMTReekasgSVPwsTYVAYLRFCGGLHAAGFVLAT 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 689 YAYS-LGSMVSVYFLT--SHDEIKEKTRIYALSFVGLAVLSfLINISQHYNFAYmgeYLTKRIRERM----LSKVLTFEV 761
Cdd:PTZ00243 971 FAVTeLVTVSSGVWLSmwSTRSFKLSAATYLYVYLGIVLLG-TFSVPLRFFLSY---EAMRRGSRNMhrdlLRSVSRGTM 1046
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 762 GWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQTVsavtiaFTMGLVIawrlaLVMIAVQPVIIV-----CF-YTR 835
Cdd:PTZ00243 1047 SFFDT--TPLGRILNRFSRDIDILDNTLPMSYLYLLQCL------FSICSSI-----LVTSASQPFVLValvpcGYlYYR 1113
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 836 RVLLKSMSKKAIKAQDESSK-----LAAEAVSNVRTITAFSSQERIMkmlekaQESPRR----------ESIRQSW---- 896
Cdd:PTZ00243 1114 LMQFYNSANREIRRIKSVAKspvftLLEEALQGSATITAYGKAHLVM------QEALRRldvvyscsylENVANRWlgvr 1187
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 897 --FAG----FGLAMSQSLTSCTWALDFWYGgrLIQDGYITAKALFETFMILV-STGRVIADAGSMT-----TDLAKGSDA 964
Cdd:PTZ00243 1188 veFLSnivvTVIALIGVIGTMLRATSQEIG--LVSLSLTMAMQTTATLNWLVrQVATVEADMNSVErllyyTDEVPHEDM 1265
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 965 --VGSVFAVLDRYTS----------IDPEDPDGYETERI-TGQVEFLDVDFSYptRPDV-IIFKNFSIKIEEGKSTAIVG 1030
Cdd:PTZ00243 1266 peLDEEVDALERRTGmaadvtgtvvIEPASPTSAAPHPVqAGSLVFEGVQMRY--REGLpLVLRGVSFRIAPREKVGIVG 1343
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1031 PSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENiiyggvsdkIDEAEIIEAAK 1110
Cdd:PTZ00243 1344 RTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN---------VDPFLEASSAE 1414
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1111 AANAHDF------ITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPS-VLLLDEATSALDSQSERVVQDALERVMV 1183
Cdd:PTZ00243 1415 VWAALELvglrerVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQIQATVMSAFS 1494
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 15229473 1184 GRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKgPTGIYFSLV 1233
Cdd:PTZ00243 1495 AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMN-RQSIFHSMV 1543
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
74-595 |
5.56e-54 |
|
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: 201.89 E-value: 5.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 74 MQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhvTSTSDVITSVSSDSFVIQDV 153
Cdd:TIGR01193 192 MGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFS---TRRTGEIVSRFTDASSIIDA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 154 LSEKLPNFLMSASTFVgsyIVGFILLwrLAIVGLPFIVLLVIPglMYGRALISISR---KIREEYNEAGFVAEQAI---- 226
Cdd:TIGR01193 269 LASTILSLFLDMWILV---IVGLFLV--RQNMLLFLLSLLSIP--VYAVIIILFKRtfnKLNHDAMQANAVLNSSIiedl 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 227 SSVRTVYAFSGERKTISK----FSTALQGSVKLGIKQGLAKGITIGSNGITFAmwgFMSWYGSRMVMYHGAQGGTVFAVA 302
Cdd:TIGR01193 342 NGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQAIKAVTKLILNV---VILWTGAYLVMRGKLTLGQLITFN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 303 AAIAIGGVSLGGGLsNLKYFFEAASVGErimEVINRVPKIDSDNPDGHK---LEKIRGEVEFKNVKFVYPsrLETSIFDD 379
Cdd:TIGR01193 419 ALLSYFLTPLENII-NLQPKLQAARVAN---NRLNEVYLVDSEFINKKKrteLNNLNGDIVINDVSYSYG--YGSNILSD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 380 FCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFG- 458
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGa 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 459 KEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQE 538
Cdd:TIGR01193 573 KENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVN 652
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 539 ALENASiGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMeNIDGQYSTLVH 595
Cdd:TIGR01193 653 NLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASLIH 707
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
834-1223 |
3.39e-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: 190.73 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 834 TRRVLlksmsKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMS----QSLT 909
Cdd:COG4618 179 TRKPL-----KEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSkflrLLLQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 910 SCTWALdfwyGGRLIQDGYITAKALFETfMILVstGRVIADAgsmttDLAKGS--------DAVGSVFAVLDRYtsidPE 981
Cdd:COG4618 254 SAVLGL----GAYLVIQGEITPGAMIAA-SILM--GRALAPI-----EQAIGGwkqfvsarQAYRRLNELLAAV----PA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 982 DPDGYETERITGQVEFLDVDFSYPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKID 1057
Cdd:COG4618 318 EPERMPLPRPKGRLSVENLTVVPPGSKRPIL-RGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWP----PTAGSVRLD 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1058 GRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENIiygGVSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLS 1137
Cdd:COG4618 393 GADLSQWDREELGRHIGYLPQDVELFDGTIAENI---ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1138 GGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV-MVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
....*..
gi 15229473 1217 HSSLLSK 1223
Cdd:COG4618 550 RDEVLAR 556
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
999-1211 |
8.16e-50 |
|
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: 173.94 E-value: 8.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYP--TRPdviIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKIDGRDIRSYHLRSLRRH 1072
Cdd:cd03246 5 NVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTlarlILGLLR----PTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEPTLFAGTIRENIiyggvsdkideaeiieaakaanahdfitsltegydtycgdrgvqLSGGQKQRIAIARAVLK 1152
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1153 NPSVLLLDEATSALDSQSERVVQDALERV-MVGRTSVVIAHRLSTIQNCDAIAVLDKGKL 1211
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
613-1233 |
8.60e-49 |
|
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: 186.48 E-value: 8.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 613 ISDPSKDIRnssrVSTLSRSSSANSVTGPSTIKNLSEDNKP---QLPSFKRLLAMNLPEWKQALYGCISATLFGAIQPAY 689
Cdd:TIGR01193 100 IADPDPTVG----ITKISKEDFYEEWTGIAIFISPTPEYKPikeKENSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 690 AYSLGSMVSVYFltsHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDrdEN 769
Cdd:TIGR01193 176 SYYLQKIIDTYI---PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFS--TR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 770 SSGAICSRLAKDANVVRSLVGDRMALVVQtvsaVTIAFTMGLVIAWR------LALVMIAVQPVIIVCFYTrrvLLKSMS 843
Cdd:TIGR01193 251 RTGEIVSRFTDASSIIDALASTILSLFLD----MWILVIVGLFLVRQnmllflLSLLSIPVYAVIIILFKR---TFNKLN 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 844 KKAIKAQDESSKLAAEAVSNVRTITAFSSQE--------RIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLtsctwal 915
Cdd:TIGR01193 324 HDAMQANAVLNSSIIEDLNGIETIKSLTSEAeryskidsEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVI------- 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 916 dFWYGGRLIQDGYITAKALFeTFMILVST-GRVIADAGSMTTDLAKGSDAVGSVFAVLdrytSIDPEDPDGY---ETERI 991
Cdd:TIGR01193 397 -LWTGAYLVMRGKLTLGQLI-TFNALLSYfLTPLENIINLQPKLQAARVANNRLNEVY----LVDSEFINKKkrtELNNL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 992 TGQVEFLDVDFSYPTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRR 1071
Cdd:TIGR01193 471 NGDIVINDVSYSYGYGSNIL--SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQ 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTLFAGTIRENIIYG---GVS-DKIDEAEIIEAAKaanahDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIA 1147
Cdd:TIGR01193 549 FINYLPQEPYIFSGSILENLLLGakeNVSqDEIWAACEIAEIK-----DDIENMPLGYQTELSEEGSSISGGQKQRIALA 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1148 RAVLKNPSVLLLDEATSALDSQSERVVQDALERvMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGptG 1227
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRN--G 700
|
....*.
gi 15229473 1228 IYFSLV 1233
Cdd:TIGR01193 701 FYASLI 706
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
318-583 |
1.00e-48 |
|
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: 182.93 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 318 NLKYFFEAASVGERIMEVINRVPKidsdNPDGHKLEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSG 397
Cdd:TIGR01842 280 GWKQFSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLSVENVTIVPPGG-KKPTLRGISFSLQAGEALAIIGPSG 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 398 SGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAH 477
Cdd:TIGR01842 355 SGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 478 NFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASI-GRTTILIAHRL 556
Cdd:TIGR01842 435 ELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRP 514
|
250 260
....*....|....*....|....*..
gi 15229473 557 STIRNADVISVVKNGHIVETGSHDELM 583
Cdd:TIGR01842 515 SLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
992-1216 |
1.07e-48 |
|
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: 172.21 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 992 TGQVEFLDVDFSY-PTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLR 1070
Cdd:cd03369 4 HGEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1071 RHIALVSQEPTLFAGTIRENI-IYGGVSDKideaeiieaakaanahDFITSL--TEGydtycgdrGVQLSGGQKQRIAIA 1147
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLdPFDEYSDE----------------EIYGALrvSEG--------GLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1148 RAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
324-556 |
1.55e-48 |
|
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: 181.79 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 324 EAASVGERIMEVI-NRVPKIDSDNPDGHKLEKIRGEVEFKNVKFVYPSRLEtsIFDDFCLRVPSGKTVALVGGSGSGKST 402
Cdd:TIGR02868 299 RVRAAAERIVEVLdAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 403 VISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFISQ 482
Cdd:TIGR02868 377 LLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 483 LPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRL 556
Cdd:TIGR02868 457 LPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
770-1194 |
1.27e-47 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 179.09 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 770 SSGAICSRLAKDAN-----VVRSLVGDRMALVVQTVSAVTIAftmglVIAWRLALVMIAVQPVIIvcFYTRRVLLKSMSK 844
Cdd:TIGR02868 108 RRGDLLGRLGADVDalqdlYVRVIVPAGVALVVGAAAVAAIA-----VLSVPAALILAAGLLLAG--FVAPLVSLRAARA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 845 KAIKAQDESSKLAAEAVSNVR---TITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGG 921
Cdd:TIGR02868 181 AEQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 922 RLIQDGYI----------TAKALFETFMIL----VSTGRVIADAGSMTTDL-AKGSDAVGSVfavldrytsidPEDPDGY 986
Cdd:TIGR02868 261 PAVADGRLapvtlavlvlLPLAAFEAFAALpaaaQQLTRVRAAAERIVEVLdAAGPVAEGSA-----------PAAGAVG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 987 ETEritGQVEFLDVDFSYPTRPDViiFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHL 1066
Cdd:TIGR02868 330 LGK---PTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1067 RSLRRHIALVSQEPTLFAGTIRENIIYG--GVSDKideaEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRI 1144
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLFDTTVRENLRLArpDATDE----ELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRL 480
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15229473 1145 AIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRL 1194
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
998-1221 |
7.63e-46 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 174.90 E-value: 7.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 998 LDVD---FSYPTRpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:PRK10789 314 LDVNirqFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAGTIRENIIYG---GVSDKIDEAEIIEaakaaNAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVL 1151
Cdd:PRK10789 393 VVSQTPFLFSDTVANNIALGrpdATQQEIEHVARLA-----SVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1152 KNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLL 1221
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
359-571 |
4.69e-44 |
|
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: 158.79 E-value: 4.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETS--IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLqrfydplAGEI-LIDGVSidklqvkWLRS 435
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-------LGELeKLSGSV-------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALFATTIKENILFGKE-DASM-DDVVEAAKASNAhnfISQLPNGYETQVGERGVQMSGGQKQRIAIARAII 513
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKACALEPD---LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 514 KSPTILLLDEATSALDSES-----ERVVQEALENasiGRTTILIAHRLSTIRNADVISVVKNG 571
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVgrhifENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
996-1211 |
1.38e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 157.67 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 996 EFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIAL 1075
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1076 VSQEPTLFAGTIRENIIYGgvsdkidEAEIIEAAKAANAHDFITSLteGYDTYCGDRGV-QLSGGQKQRIAIARAVLKNP 1154
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFP-------FQLRERKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1155 SVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAHRLSTIQN-CDAIAVLDKGKL 1211
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
995-1215 |
1.51e-43 |
|
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: 158.11 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYD-----PLKGIVKIDGRDIRS--YHLR 1067
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1068 SLRRHIALVSQEPTLFAGTIRENIIYG----GVSDKIDEAEIIEaakaanahdfiTSLTE-GYDTYCGDR--GVQLSGGQ 1140
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhGIKLKEELDERVE-----------EALRKaALWDEVKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1141 KQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNC-DAIAVLDKGKLVERG 1215
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFG 222
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1012-1223 |
1.85e-43 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 167.14 E-value: 1.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENI 1091
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1092 IYGGvsDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE 1171
Cdd:TIGR01842 413 ARFG--ENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1172 RVVQDALERVMV-GRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:TIGR01842 491 QALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
673-935 |
2.63e-43 |
|
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: 159.35 E-value: 2.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 673 LYGCISATLFGAIQPAYAYSLGSMVSVYFLTShDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERM 752
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDG-DPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 753 LSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCF 832
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 833 YTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCT 912
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260
....*....|....*....|...
gi 15229473 913 WALDFWYGGRLIQDGYITAKALF 935
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLV 261
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
360-554 |
2.82e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.90 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGL 439
Cdd:COG4619 2 ELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQEPALFATTIKENILFG----KEDASMDDVVEAAKASNahnfisqLPNGY-ETQVGErgvqMSGGQKQRIAIARAIIK 514
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlrERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15229473 515 SPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAH 554
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
359-582 |
4.25e-43 |
|
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: 156.96 E-value: 4.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYD-----PLAGEILIDGVSIDKLQ--VK 431
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 432 WLRSQMGLVSQEPALFATTIKENILFG------KEDASMDDVVEAA--KAsnahnfisQLPNgyetQVGER--GVQMSGG 501
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlrKA--------ALWD----EVKDRlhALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 502 QKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHD 580
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTE 225
|
..
gi 15229473 581 EL 582
Cdd:cd03260 226 QI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
359-587 |
5.78e-43 |
|
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: 156.72 E-value: 5.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPA--LFATTIKENILFG-----KEDASMDDVV-EAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIAR 510
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlgLPREEIRERVeEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELMENID 587
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
35-299 |
6.24e-43 |
|
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: 158.19 E-value: 6.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 35 MGLGLIGAVGDGFTTPLVLLITSKLMNNIGGSSfNTDTfmQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQTARMR 114
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDG-DPET--QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 115 EKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLV 194
Cdd:pfam00664 78 RKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 195 IPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIG-SNGIT 273
Cdd:pfam00664 156 LVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGiTQFIG 235
|
250 260
....*....|....*....|....*.
gi 15229473 274 FAMWGFMSWYGSRMVMYHGAQGGTVF 299
Cdd:pfam00664 236 YLSYALALWFGAYLVISGELSVGDLV 261
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
995-1215 |
1.43e-42 |
|
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: 153.62 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIiFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHlRSLRRHIA 1074
Cdd:cd03247 1 LSINNVSFSYPEQEQQV-LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAGTIRENIiyggvsdkideaeiieaakaanahdfitsltegydtycgdrGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1155 SVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERG 1215
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
995-1223 |
1.73e-42 |
|
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: 155.18 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPT--LFAGTIRENIIYG----GVS-DKIDeaeiieaakaANAHDFITSL-TEGYdtycGDRGV-QLSGGQKQRIA 1145
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlGLPrEEIR----------ERVEEALELVgLEHL----ADRPPhELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1146 IARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIA-HRLSTI-QNCDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
359-577 |
3.26e-42 |
|
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: 152.47 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQvKWLRSQMG 438
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFATTIKENIlfgkedasmddvveaakasnahnfisqlpngyetqvgerGVQMSGGQKQRIAIARAIIKSPTI 518
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 519 LLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETG 577
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
360-572 |
2.01e-41 |
|
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: 151.47 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGL 439
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQEPA--LFATTIKENILFGKEDASMDD------VVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARA 511
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGLENLGLPEeeieerVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 512 IIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIRN-ADVISVVKNGH 572
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
357-578 |
2.71e-41 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 151.03 E-value: 2.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPSRLEtSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFATTIKENI-LFGKEDAsmDDVVEAAKasnahnfisqlpngyetqVGERGVQMSGGQKQRIAIARAIIKS 515
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDEYSD--EEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 516 PTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGS 578
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
360-573 |
3.63e-41 |
|
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: 149.29 E-value: 3.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGL 439
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQEPALFATTIKENILfgkedasmddvveaakasnahnfisqlpngyetqvgergvqmSGGQKQRIAIARAIIKSPTIL 519
Cdd:cd03246 81 LPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 520 LLDEATSALDSESERVVQEALENASI-GRTTILIAHRLSTIRNADVISVVKNGHI 573
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
995-1223 |
2.65e-40 |
|
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: 148.88 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRP-DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI---RSYHLRSLR 1070
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1071 RHIALVSQEPTLFAG-TIRENIIY----GGVSDKideaeiieaAKAANAHDFIT--SLTEGYDTYCGdrgvQLSGGQKQR 1143
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALpleiAGVPKA---------EIEERVLELLElvGLEDKADAYPA----QLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1144 IAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSL 1220
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 15229473 1221 LSK 1223
Cdd:cd03258 229 FAN 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
359-585 |
3.96e-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: 156.60 E-value: 3.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETSIF--DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWL 433
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRavDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 434 RSQMGLVSQEP--ALFAT-TIKENILFG-------KEDASMDDVVEAAKASN-AHNFISQLPNgyetqvgergvQMSGGQ 502
Cdd:COG1123 341 RRRVQMVFQDPysSLNPRmTVGDIIAEPlrlhgllSRAERRERVAELLERVGlPPDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 503 KQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSH 579
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*.
gi 15229473 580 DELMEN 585
Cdd:COG1123 490 EEVFAN 495
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
359-575 |
1.05e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.11 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPS-RLETSIFDDFCLRVPSGKTVALVGGSGSGKST---VISLLQRfydPLAGEILIDGVSIDKL----QV 430
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 431 KWLRSQMGLVSQEPALFAT-TIKENILFGKEDASMDDVVEAAKASNA------HNFISQLPNgyetqvgergvQMSGGQK 503
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARELlervglGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 504 QRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRNADVISVVKNGHIVE 575
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1013-1164 |
1.72e-39 |
|
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: 143.56 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAG-TIRENI 1091
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1092 IYGGVSDKIDEAEIIEAakaanAHDFIT--SLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR-----AEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
377-526 |
1.79e-39 |
|
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: 143.56 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 377 FDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALF-ATTIKENI 455
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 456 LFGKEDASMDDVVEAAKASNAHNFISqLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATS 526
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
996-1210 |
2.26e-39 |
|
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: 143.54 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 996 EFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIAL 1075
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1076 VSQeptlfagtireniiyggvsdkideaeiieaakaanahdfitsltegydtycgdrgvqLSGGQKQRIAIARAVLKNPS 1155
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1156 VLLLDEATSALDSQSERVVQDALERVMV-GRTSVVIAHRLSTIQN-CDAIAVLDKGK 1210
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
996-1210 |
3.28e-39 |
|
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: 144.92 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 996 EFLDVDFSYPTRpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIAL 1075
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1076 VSQEPT--LFAGTIRENIIYG----GVSDKIDEAEIIEAAKAANAHDFitsltEGYDTYcgdrgvQLSGGQKQRIAIARA 1149
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGlenlGLPEEEIEERVEEALELVGLEGL-----RDRSPF------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1150 VLKNPSVLLLDEATSALDSQSERVVQDALERVM-VGRTSVVIAHRLSTIQN-CDAIAVLDKGK 1210
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1009-1233 |
7.00e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 145.21 E-value: 7.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyHLRSLRRHIALVSQEPTLFAG-TI 1087
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIYGGVSDKIDEAEIIEAakaanAHDFI--TSLTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:COG1131 91 RENLRFFARLYGLPRKEARER-----IDELLelFGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1166 LDSQSERVVQDALERVMVGRTSVVIA-HRLSTIQN-CDAIAVLDKGKLVERGTHSSLLSKGPTGIYFSLV 1233
Cdd:COG1131 162 LDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKARLLEDVFLELT 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
995-1213 |
8.40e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.42 E-value: 8.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPT-RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKST---IIGLIERfydPLKGIVKIDGRDIRSY------ 1064
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1065 HLRslRRHIALVSQEPTLFAG-TIRENI----IYGGVSDKIDEAEiieaakaanAHDFITSLteGYDTYCGDRGVQLSGG 1139
Cdd:COG1136 82 RLR--RRHIGFVFQFFNLLPElTALENValplLLAGVSRKERRER---------ARELLERV--GLGDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1140 QKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVE 1213
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
359-585 |
1.46e-38 |
|
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: 143.88 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSR-LETSIFDDFCLRVPSGKTVALVGGSGSGKSTV---ISLLQRfydPLAGEILIDGVSIDKLQVKWL- 433
Cdd:cd03258 2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER---PTSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 434 --RSQMGLVSQEPALFAT-TIKENILFGKEDASMDDVVEAAKASNAHNFIsqlpnGYETQVGERGVQMSGGQKQRIAIAR 510
Cdd:cd03258 79 kaRRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELV-----GLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1006-1210 |
1.50e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 141.94 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1006 TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSY--HLRSLRRHIALVSQEPTLF 1083
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AG-TIRENIIYGgvsdkideaeiieaakaanahdfitsltegydtycgdrgvqLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:cd03229 89 PHlTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1163 TSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTIQN-CDAIAVLDKGK 1210
Cdd:cd03229 128 TSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
359-577 |
1.85e-38 |
|
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: 143.04 E-value: 1.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQMG 438
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFAT-TIKENILFGKEDASMDdvvEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPT 517
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVP---KAEIRARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 518 ILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETG 577
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
359-584 |
7.03e-38 |
|
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: 142.43 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRS 435
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALF-ATTIKENILF------GKEDASMDDVVEAA-KASNAHNFISQLPNgyetqvgergvQMSGGQKQRIA 507
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFplrehtDLSEAEIRELVLEKlELVGLPGAADKMPS-----------ELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 508 IARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELME 584
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
995-1210 |
7.09e-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: 141.07 E-value: 7.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVI--IFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIERfydpLKGIVKIDGRdirsyhlrs 1068
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSllsaLLGELEK----LSGSVSVPGS--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1069 lrrhIALVSQEPTLFAGTIRENIIYGGVSDK-------------IDeaeiieaakaanahdfITSLTEGYDTYCGDRGVQ 1135
Cdd:cd03250 68 ----IAYVSQEPWIQNGTIRENILFGKPFDEeryekvikacalePD----------------LEILPDGDLTEIGEKGIN 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1136 LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQ-SERVVQDAL-ERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGK 1210
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
359-582 |
1.20e-37 |
|
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: 141.49 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWL---RS 435
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALF-ATTIKENILF-----GKEDASM--DDVVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIA 507
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFplrehTRLSEEEirEIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 508 IARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
995-1222 |
2.25e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.51 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRP--DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYH---LRSL 1069
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1070 RRHIALVSQEPT--LFAG-TIRENI-----IYGGVSDKideaeiieaakaaNAHDFITSLTE--GYDTYCGDR-GVQLSG 1138
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIaeplrLHGLLSRA-------------ERRERVAELLErvGLPPDLADRyPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*..
gi 15229473 1216 THSSLLS 1222
Cdd:COG1123 488 PTEEVFA 494
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
999-1216 |
2.64e-37 |
|
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: 140.95 E-value: 2.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQ 1078
Cdd:COG1120 6 NLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EPTL-FAGTIRENIIYG--------GVSDKIDEAEIIEAAKAANAHDFItsltegydtycgDRGV-QLSGGQKQRIAIAR 1148
Cdd:COG1120 83 EPPApFGLTVRELVALGryphlglfGRPSAEDREAVEEALERTGLEHLA------------DRPVdELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1149 AVLKNPSVLLLDEATSALD--SQSE--RVVQD-ALERvmvGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGT 1216
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDlaHQLEvlELLRRlARER---GRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
357-594 |
3.54e-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: 140.81 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPSRLEtSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:cd03288 18 GEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFATTIKENIlfGKEDASMDDVV-EAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKS 515
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL--DPECKCTDDRLwEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 516 PTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENIDGQYSTLV 594
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
673-971 |
3.90e-37 |
|
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: 142.42 E-value: 3.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 673 LYGCISATLFGAIQPAYAYSLGSMVSVYFLTSHDEI-----------------KEKTRIYALSFVGLAVLSFLINISQHY 735
Cdd:cd18558 2 VVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 736 NFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAW 815
Cdd:cd18558 82 FWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 816 RLALVMIAVQPVIIVCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQS 895
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 896 WFAGFGLAMSQSLTSCTWALDFWYGGRLI-QDGYITAKALFETFMILVSTgrviADAGSMTTDLAKGSDAVGSVFAV 971
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVtQQEYSIGEVLTVFFSVLIGA----FSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
83-289 |
5.06e-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: 141.54 E-value: 5.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 83 ALLYVACGswVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFL 162
Cdd:cd18557 43 LAIYLLQS--VFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH--KTGELTSRLSSDTSVLQSAVTDNLSQLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 163 MSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTI 242
Cdd:cd18557 119 RNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15229473 243 SKFSTALQGSVKLGIKQGLAKGITIGSNGItFAMWGFMS--WYGSRMVM 289
Cdd:cd18557 199 RRYSEALDRSYRLARKKALANALFQGITSL-LIYLSLLLvlWYGGYLVL 246
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
359-576 |
5.85e-37 |
|
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: 139.14 E-value: 5.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPS-RLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLqvkwlRSQM 437
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEPALFA-TTIKENILFGKEDASMDDvveAAKASNAHNFISQlpngyetqVGERGV------QMSGGQKQRIAIAR 510
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPK---AEARERAEELLEL--------VGLSGFenayphQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLS-TIRNADVISVVKN--GHIVET 576
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
359-577 |
6.83e-37 |
|
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: 139.18 E-value: 6.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSR-LETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLR 434
Cdd:cd03257 2 LEVKNLSVSFPTGgGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 435 SQMGLVSQEP--ALFAT-TIKENILFGKEDASMDDVVEAAKA---------SNAHNFISQLPNgyetqvgergvQMSGGQ 502
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRmTIGEQIAEPLRIHGKLSKKEARKEavllllvgvGLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 503 KQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
999-1223 |
1.41e-36 |
|
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: 138.84 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPtrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYhLRSLRRHIALVSQ 1078
Cdd:COG4555 6 NLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EPTLFAG-TIRENI-----IYGGVSDKIDEAEIIEaakaanAHDFItsLTEGYDTYCGDrgvqLSGGQKQRIAIARAVLK 1152
Cdd:COG4555 82 ERGLYDRlTVRENIryfaeLYGLFDEELKKRIEEL------IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1153 NPSVLLLDEATSALDSQSERVVQDALERVM-VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
999-1215 |
4.46e-36 |
|
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: 136.87 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPDVI-IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI--RSYHLRSLRRH-IA 1074
Cdd:cd03257 6 NLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlkLSRRLRKIRRKeIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQE------PTLfagTIRENI-----IYGGVSDK--IDEAEIIEAAKAANAHDFITSLTEgydtycgdrgvQLSGGQK 1141
Cdd:cd03257 86 MVFQDpmsslnPRM---TIGEQIaeplrIHGKLSKKeaRKEAVLLLLVGVGLPEEVLNRYPH-----------ELSGGQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1142 QRIAIARAVLKNPSVLLLDEATSALDsqseRVVQDALERVMV------GRTSVVIAHRLSTIQN-CDAIAVLDKGKLVER 1214
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALD----VSVQAQILDLLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
.
gi 15229473 1215 G 1215
Cdd:cd03257 228 G 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
359-585 |
4.81e-36 |
|
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: 144.28 E-value: 4.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDP---LAGEILIDGVSIDKLQVKWLRS 435
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEP--ALFATTIKENILFGKEDASMDD------VVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIA 507
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRaeararVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 508 IARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELME 584
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 15229473 585 N 585
Cdd:COG1123 233 A 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
995-1211 |
9.45e-36 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 135.31 E-value: 9.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPD-VIIFKNFSIKIEEGKSTAIVGPSGSGKST---IIGLIERfydPLKGIVKIDGRDIRSYHLRSL- 1069
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1070 ---RRHIALVSQE----PTLfagTIRENI----IYGGVSDKideaeiieaAKAANAHDFITS--LTEGYDTYCGdrgvQL 1136
Cdd:cd03255 78 afrRRHIGFVFQSfnllPDL---TALENVelplLLAGVPKK---------ERRERAEELLERvgLGDRLNHYPS----EL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTIQNCDAIAVLDKGKL 1211
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
359-573 |
9.73e-36 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 135.31 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPS-RLETSIFDDFCLRVPSGKTVALVGGSGSGKST---VISLLQRfydPLAGEILIDGVSIDKL----QV 430
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLsekeLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 431 KWLRSQMGLVSQEPALFAT-TIKENILFGKEDASmddVVEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIA 509
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDlTALENVELPLLLAG---VPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 510 RAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRNADVISVVKNGHI 573
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
359-572 |
1.29e-35 |
|
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: 133.47 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPsrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL--QVKWLRSQ 436
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFAT-TIKENILFGkedasmddvveaakasnahnfisqlpngyetqvgergvqMSGGQKQRIAIARAIIKS 515
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 516 PTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLS-TIRNADVISVVKNGH 572
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
356-584 |
1.62e-35 |
|
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: 147.78 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 356 RGEVEFKNVKFVYPSRLETsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRS 435
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALFATTIKENI-LFGKedASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIK 514
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 515 SPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELME 584
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
359-591 |
2.44e-35 |
|
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: 135.32 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETS-IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQM 437
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEPAL-------FATTIKENILFGKEDASMDDVVEAAKASN-AHNFISQLPNgyetqvgergvQMSGGQKQRIAIA 509
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 510 RAIIKSPTILLLDEATSALDSeserVVQ-EALE-----NASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDEL 582
Cdd:COG1124 151 RALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADL 226
|
....*....
gi 15229473 583 MENIDGQYS 591
Cdd:COG1124 227 LAGPKHPYT 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
360-596 |
2.85e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 134.99 E-value: 2.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKlQVKWLRSQMGL 439
Cdd:COG4555 3 EVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQEPALFAT-TIKENILFGKEDASMDDVVEAAKASN-AHNFisQLPNGYETQVGErgvqMSGGQKQRIAIARAIIKSPT 517
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEElIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 518 ILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMENIDGQ--YSTL 593
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEEnlEDAF 232
|
...
gi 15229473 594 VHL 596
Cdd:COG4555 233 VAL 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
359-586 |
2.96e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 134.42 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWlRSQMG 438
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFAT-TIKENI-----LFGKEDASMDDVVEAAKAsnahnfISQLPNGYETQVGergvQMSGGQKQRIAIARAI 512
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDELLE------LFGLTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 513 IKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIA-HRLSTI-RNADVISVVKNGHIVETGSHDELMENI 586
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-595 |
3.30e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 146.66 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 3 KEEEKESGRNKMNcfgsVRSIFMHADGVDWLLMGLGLIGavgdgFTTPLVLLITSKLMnniggsSFNTDtfmQSISKNSV 82
Cdd:PLN03232 887 KQEERETGIISWN----VLMRYNKAVGGLWVVMILLVCY-----LTTEVLRVSSSTWL------SIWTD---QSTPKSYS 948
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 83 ALLYVAC------GSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFdlHVTSTSDVITSVSSDSFVIQDVLSE 156
Cdd:PLN03232 949 PGFYIVVyallgfGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFF--HTNPTGRVINRFSKDIGDIDRNVAN 1026
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 157 KLPNFLMSA----STFVGSYIVGFILLWRLaivgLPFIVLLVIPGLMYG------RALISISRK-IREEYNEAgfvaEQA 225
Cdd:PLN03232 1027 LMNMFMNQLwqllSTFALIGTVSTISLWAI----MPLLILFYAAYLYYQstsrevRRLDSVTRSpIYAQFGEA----LNG 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 226 ISSVRTVYAFSGERKTISKfstalqgSVKLGIKQGLAkgiTIGSNG-ITF---AMWGFMSWY-GSRMVMYHG-AQGGTVF 299
Cdd:PLN03232 1099 LSSIRAYKAYDRMAKINGK-------SMDNNIRFTLA---NTSSNRwLTIrleTLGGVMIWLtATFAVLRNGnAENQAGF 1168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 300 AVAAAIAIGGVSLGGGLsnLKYFFEAASVGERIMEVINRV----------PKIDSDN--PDGHKLekiRGEVEFKNVKFV 367
Cdd:PLN03232 1169 ASTMGLLLSYTLNITTL--LSGVLRQASKAENSLNSVERVgnyidlpseaTAIIENNrpVSGWPS---RGSIKFEDVHLR 1243
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 368 YPSRLeTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALF 447
Cdd:PLN03232 1244 YRPGL-PPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLF 1322
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 448 ATTIKENI-LFGKEDASmdDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATS 526
Cdd:PLN03232 1323 SGTVRFNIdPFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 527 ALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENIDGQYSTLVH 595
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
359-585 |
3.71e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.50 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:PRK13632 8 IKVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEP--ALFATTIKENILFGKED-----ASMDDVV-EAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIAR 510
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENkkvppKKMKDIIdDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
995-1221 |
4.58e-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: 134.35 E-value: 4.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAG-TIRENI-----IYGGVSDKIDeaeiieaakaANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIAR 1148
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIalvpkLLKWPKEKIR----------ERADELLALVGLDPAEFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1149 AVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRL-STIQNCDAIAVLDKGKLVERGTHSSLL 1221
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
359-586 |
4.77e-35 |
|
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: 135.25 E-value: 4.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVS-IDKLQVKWLRSQM 437
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEP--ALFATTIKENILFGKEDASMDD------VVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIA 509
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLGVPReemrkrVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 510 RAIIKSPTILLLDEATSALDSESER-VVQEALE-NASIGRTTILIAHRLSTIRNADVISVVKNGHIVETG------SHDE 581
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKeVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*
gi 15229473 582 LMENI 586
Cdd:TIGR04520 229 LLKEI 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
359-585 |
5.39e-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: 5.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFA-TTIKENI-----LFGKEDASMDdvveaAKASNAHNFISQLPNGYetqvGER-GVQMSGGQKQRIAIARA 511
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkLLKWPKEKIR-----ERADELLALVGLDPAEF----ADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 512 IIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRL-STIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
359-586 |
6.70e-35 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 134.02 E-value: 6.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPAL-FATTIKENIL---------FGKEDASMDDVVEAA-KASNAHNFIsqlpngyetqvgERGV-QMSGGQKQRI 506
Cdd:COG1120 79 YVPQEPPApFGLTVRELVAlgryphlglFGRPSAEDREAVEEAlERTGLEHLA------------DRPVdELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 507 AIARAIIKSPTILLLDEATSALD----SESERVVQEalENASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDE 581
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRR--LARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEE 224
|
....*..
gi 15229473 582 LM--ENI 586
Cdd:COG1120 225 VLtpELL 231
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
35-289 |
8.57e-35 |
|
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: 135.87 E-value: 8.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 35 MGLGLIGAVGDGFTTPLVLLITSKLMNNI--GGSSFNTDTFMQSISK-----------NSVALLY--VACGSWVVCFLEG 99
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnGGMTNITGNSSGLNSSagpfekleeemTLYAYYYliIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 100 YCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILL 179
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVN--DTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 180 WRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQ 259
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270
....*....|....*....|....*....|.
gi 15229473 260 GLAKGITIG-SNGITFAMWGFMSWYGSRMVM 289
Cdd:cd18558 239 AITFNISMGaAFLLIYASYALAFWYGTYLVT 269
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
999-1222 |
9.64e-35 |
|
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: 133.39 E-value: 9.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRP-DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVS 1077
Cdd:COG1124 6 NLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1078 QEPTLFA---GTIRENI-----IYG--GVSDKIDEAEIIeaakaanahdfiTSLTEGYdtycGDRGV-QLSGGQKQRIAI 1146
Cdd:COG1124 86 QDPYASLhprHTVDRILaeplrIHGlpDREERIAELLEQ------------VGLPPSF----LDRYPhQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1147 ARAVLKNPSVLLLDEATSALDSqserVVQ----DALERVMV--GRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSS 1219
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
...
gi 15229473 1220 LLS 1222
Cdd:COG1124 226 LLA 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
995-1211 |
9.75e-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: 130.98 E-value: 9.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyHLRSLRRHIA 1074
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAG-TIRENIiyggvsdkideaeiieaakaanahdfitsltegydtycgdrgvQLSGGQKQRIAIARAVLKN 1153
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1154 PSVLLLDEATSALDSQSERVVQDAL-ERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKL 1211
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLrELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
995-1216 |
1.08e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 136.36 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRP-DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLI---ERfydPLKGIVKIDGRDIRSYH---LR 1067
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1068 SLRRHIALVSQEPTLFAG-TIRENIIY----GGVS-DKIDEAeiieaakaanahdfITSLTE--GYdtycGDRG----VQ 1135
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALpleiAGVPkAEIRKR--------------VAELLElvGL----SDKAdaypSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1136 LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV---MvGRTSVVIAHRLSTIQN-CDAIAVLDKGKL 1211
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInreL-GLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 15229473 1212 VERGT 1216
Cdd:COG1135 220 VEQGP 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
360-582 |
1.23e-34 |
|
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: 133.08 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWL---RSQ 436
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFA-TTIKENILFGKedasmddvveaakaSNAHNFISQLPNGYE-----------TQVG------ERGVQM 498
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGR--------------LGRRSTWRSLFGLFPkeekqralaalERVGlldkayQRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 499 SGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIR-NADVISVVKNGHIVE 575
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAReYADRIVGLKDGRIVF 225
|
....*..
gi 15229473 576 TGSHDEL 582
Cdd:cd03256 226 DGPPAEL 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
995-1216 |
1.25e-34 |
|
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: 132.63 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRS---YHLRSLRR 1071
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTLFAG-TIRENI--------------IYGGVSDKIDEAeiieaakaanahdfitSLTEGYDTYCGdrgvQL 1136
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVafplrehtrlseeeIREIVLEKLEAV----------------GLRGAEDLYPA----EL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTI-QNCDAIAVLDKGKLVE 1213
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVA 217
|
...
gi 15229473 1214 RGT 1216
Cdd:cd03261 218 EGT 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
995-1215 |
1.25e-34 |
|
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: 131.87 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrsYHLRSLRRHIA 1074
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAG-TIRENIIYGGVSDKIDEAEIIeaakaaNAHDFITSLTeGYDTYCGDRGVQLSGGQKQRIAIARAVLKN 1153
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVPKAEIR------ARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1154 PSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERG 1215
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQreLGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
360-572 |
2.04e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 129.29 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGL 439
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQepalfattikenilfgkedasmddvveaakasnahnfisqlpngyetqvgergvqMSGGQKQRIAIARAIIKSPTIL 519
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 520 LLDEATSALDSESERVVQEAL-ENASIGRTTILIAHRLSTIRNA-DVISVVKNGH 572
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
995-1206 |
2.21e-34 |
|
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: 131.44 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPT-RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyhlrsLRRHI 1073
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPTLFA-GTIRENIIYG----GVSDKIdeaeiieaaKAANAHDFITS--LTEGYDTYCGdrgvQLSGGQKQRIAI 1146
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqGVPKAE---------ARERAEELLELvgLSGFENAYPH----QLSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1147 ARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRLS-TIQNCDAIAVL 1206
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVL 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
382-585 |
3.82e-34 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 132.38 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRS----QMGLVSQEPALFA-TTIKENIL 456
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPhRTVLENVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 457 FGKEDASMDDVVEAAKASNA------HNFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSPTILLLDEATSALDS 530
Cdd:cd03294 125 FGLEVQGVPRAEREERAAEAlelvglEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 531 ESERVVQEALEN--ASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:cd03294 194 LIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
999-1215 |
4.63e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 131.70 E-value: 4.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYD--P---LKGIVKIDGRDI--RSYHLRSLRR 1071
Cdd:COG1117 16 NLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTLFAGTIRENIIYG----GVSDKIDEaeiieaakaanahDFI--TSLTEgydtyCG------DR----GVQ 1135
Cdd:COG1117 93 RVGMVFQKPNPFPKSIYDNVAYGlrlhGIKSKSEL-------------DEIveESLRK-----AAlwdevkDRlkksALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1136 LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERvMVGRTSVVI-------AHRLStiqncDAIAVLDK 1208
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE-LKKDYTIVIvthnmqqAARVS-----DYTAFFYL 228
|
....*..
gi 15229473 1209 GKLVERG 1215
Cdd:COG1117 229 GELVEFG 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
359-554 |
9.02e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 130.98 E-value: 9.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRL-ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLqvkwlRSQM 437
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEPALFA-TTIKENILFGkedASMDDVVEAAKASNAHNFISQlpngyetqVGERGV------QMSGGQKQRIAIAR 510
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELLEL--------VGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAH 554
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
359-578 |
1.16e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 133.28 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRL-ETSIFDDFCLRVPSGKTVALVGGSGSGKST---VISLLQRfydPLAGEILIDGVSIDKLQVKWL- 433
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 434 --RSQMGLVSQEPALFAT-TIKENILFGKEDASMDDVVEAAKASN----------AHNFISQLpngyetqvgergvqmSG 500
Cdd:COG1135 79 aaRRKIGMIFQHFNLLSSrTVAENVALPLEIAGVPKAEIRKRVAEllelvglsdkADAYPSQL---------------SG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 501 GQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKdiNRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
.
gi 15229473 578 S 578
Cdd:COG1135 224 P 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
999-1215 |
1.62e-33 |
|
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: 127.55 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQ 1078
Cdd:cd03214 4 NLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 eptlfagtireniiyggVSDKIDeaeiieaakaanahdfITSLTegydtycgDRGV-QLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:cd03214 81 -----------------ALELLG----------------LAHLA--------DRPFnELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1158 LLDEATSALD--SQSE---RVVQDALERvmvGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERG 1215
Cdd:cd03214 120 LLDEPTSHLDiaHQIElleLLRRLARER---GKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
995-1222 |
2.30e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.19 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIERFYDpLKGIVKIDGRDIRSYHLRSLR 1070
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGR-ISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1071 RHIALVSQEPT--LFAGTIRENIIYGGVSDKIDEAEiieaakaanAHDFITSLTE--GYDTYCGDRGVQLSGGQKQRIAI 1146
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAE---------ARARVLELLEavGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1147 ARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
359-585 |
2.59e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.53 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPsrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVkWLRsQMG 438
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKR-NVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFA-TTIKENILFGkedASMDDVVEAAKASNAHNFIS--QLPnGYEtqvgERGV-QMSGGQKQRIAIARAIIK 514
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFG---LRMRGVPKAEIRARVAELLElvGLE-GLA----DRYPhQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 515 SPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLS---TIrnADVISVVKNGHIVETGSHDELMEN 585
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
673-935 |
2.70e-33 |
|
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: 130.75 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 673 LYGCISATLFGAIQPAYAYSLGSMVsvyfltshDEIKEKTR-----IYALSFVGLAVLSFLINISQHYNFAYMGEYLTKR 747
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLI--------DDVIPAGDlslllWIALLLLLLALLRALLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 748 IRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPV 827
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 828 IIVCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQS 907
Cdd:cd07346 152 YVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260
....*....|....*....|....*...
gi 15229473 908 LTSCTWALDFWYGGRLIQDGYITAKALF 935
Cdd:cd07346 232 LTALGTALVLLYGGYLVLQGSLTIGELV 259
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1009-1216 |
3.09e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 128.96 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI--RSYHLRSLRRHIALVSQEPTLFAG- 1085
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 TIRENIIYG-----------------------GVSDKIDEaeiieaakaanahdfitsltegydtYCGdrgvQLSGGQKQ 1142
Cdd:COG1126 93 TVLENVTLApikvkkmskaeaeeramellervGLADKADA-------------------------YPA----QLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1143 RIAIARAVLKNPSVLLLDEATSALDSQserVVQDALErVMV-----GRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRdlakeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
376-585 |
1.35e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.03 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSID--KLQVKWLRSQMGLVSQEPALFA-TTIK 452
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQFNLFPhLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 453 ENILFG--------KEDAsmddvVEAAK--------ASNAHNFISQLpngyetqvgergvqmSGGQKQRIAIARAIIKSP 516
Cdd:COG1126 96 ENVTLApikvkkmsKAEA-----EERAMellervglADKADAYPAQL---------------SGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 517 TILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
359-575 |
2.21e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.94 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLEtsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRS 435
Cdd:COG2884 2 IRFENVSKRYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALFAT-TIKENILF-----GKEDASMDDVVEAA--------KAsnaHNFISQLpngyetqvgergvqmSGG 501
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRRVREVldlvglsdKA---KALPHEL---------------SGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 502 QKQRIAIARAIIKSPTILLLDEATSALDSE-SERVVqEALENASIGRTTILIA-HRLSTIRNAD--VIsVVKNGHIVE 575
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPkrVL-ELEDGRLVR 217
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
82-288 |
2.52e-32 |
|
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: 128.14 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 82 VALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNF 161
Cdd:cd18780 46 LILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 162 LMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKT 241
Cdd:cd18780 124 LRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229473 242 ISKFSTALQGSVKLGIKQGLAKGITIGSNG-ITFAMWGFMSWYGSRMV 288
Cdd:cd18780 204 VSRYSEKINESYLLGKKLARASGGFNGFMGaAAQLAIVLVLWYGGRLV 251
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
58-289 |
3.06e-32 |
|
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: 127.63 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 58 KLMNNIGGSSFNTDTFMQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTSTS 137
Cdd:cd18573 21 KLIDVASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD--KNKTG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 138 DVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNE 217
Cdd:cd18573 99 ELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALAD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 218 AGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIGSNGITfamwGFMS-----WYGSRMVM 289
Cdd:cd18573 179 ATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFS----GNLSllsvlYYGGSLVA 251
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1014-1221 |
6.38e-32 |
|
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: 126.22 E-value: 6.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYH---LRSLRRH-IALVSQEPTLFAG-TIR 1088
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPHrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1089 ENIIYG----GVSDKIDEAEIIEAAKAANAHDFITSLTEgydtycgdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:cd03294 121 ENVAFGlevqGVPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1165 ALDSQSERVVQDALERV--MVGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGTHSSLL 1221
Cdd:cd03294 190 ALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
995-1209 |
9.12e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.20 E-value: 9.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRP-DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyhlrsLRRHI 1073
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPTLFA-GTIRENIIYG----GVSDKideaeiieaAKAANAHDFITS--LTEGYDTYCGdrgvQLSGGQKQRIAI 1146
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrGVPKA---------ERRERARELLELvgLAGFEDAYPH----QLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1147 ARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAH------RLStiqncDAIAVLDKG 1209
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHdvdeavFLA-----DRVVVLSAR 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
359-573 |
1.06e-31 |
|
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: 122.12 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwLRSQMG 438
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFAT-TIKENILFgkedasmddvveaakasnahnfisqlpngyetqvgergvqmSGGQKQRIAIARAIIKSPT 517
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 518 ILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIRN-ADVISVVKNGHI 573
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
995-1216 |
2.05e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.84 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPT-RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSY---HLRSLR 1070
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1071 RHIALVSQEPTLFAG-TIRENI-----IYGGVSDKIDEAEIIEAAkaanahdfITSLTEGYDTYcgdrGVQLSGGQKQRI 1144
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNValpleLAGTPKAEIKARVTELLE--------LVGLSDKADRY----PAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1145 AIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERGT 1216
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
995-1216 |
2.18e-31 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 123.55 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKIDGRDI---RSYHLR 1067
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVllklIIGLLR----PDSGEILVDGQDItglSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1068 SLRRHIALVSQEPTLFAG-TIRENI-----IYGGVSDKIdeaeiieaakaanahdfITSLTEgydtYC----GDRGV--- 1134
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVafplrEHTDLSEAE-----------------IRELVL----EKlelvGLPGAadk 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1135 ---QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVV-------QDALervmvGRTSVVIAHRLSTIQN-CDAI 1203
Cdd:COG1127 138 mpsELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLDSAFAiADRV 212
|
250
....*....|...
gi 15229473 1204 AVLDKGKLVERGT 1216
Cdd:COG1127 213 AVLADGKIIAEGT 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
995-1221 |
2.20e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.72 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:PRK13632 8 IKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEP-TLFAG-TIRENIIYGGVSDKIDEAEIIeaakaanahDFITSLTE--GYDTYCGDRGVQLSGGQKQRIAIARAV 1150
Cdd:PRK13632 87 IIFQNPdNQFIGaTVEDDIAFGLENKKVPPKKMK---------DIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIA--HRLSTIQNCDAIAVLDKGKLVERGTHSSLL 1221
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
995-1216 |
2.38e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 126.75 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyHLRSLRRHIA 1074
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAG-TIRENIIYG----GVS-DKIDEAeiieaakaanAHDFItSLT--EGYdtycGDRGV-QLSGGQKQRIA 1145
Cdd:COG3842 81 MVFQDYALFPHlTVAENVAFGlrmrGVPkAEIRAR----------VAELL-ELVglEGL----ADRYPhQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1146 IARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAH------RLStiqncDAIAVLDKGKLVERGT 1216
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHdqeealALA-----DRIAVMNDGRIEQVGT 219
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
684-940 |
3.08e-31 |
|
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: 124.60 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 684 AIQPAYAYSLGSMVSVyflTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGW 763
Cdd:cd18557 10 AAQLLLPYLIGRLIDT---IIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 764 FDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVC--FYTRRvlLKS 841
Cdd:cd18557 87 FDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIAskIYGRY--IRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 842 MSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGG 921
Cdd:cd18557 163 LSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGG 242
|
250
....*....|....*....
gi 15229473 922 RLIQDGYITAKALFeTFMI 940
Cdd:cd18557 243 YLVLSGQLTVGELT-SFIL 260
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
359-574 |
3.20e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.24 E-value: 3.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRS 435
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALFA-TTIKENILFGKED-----ASM------DDVVEAAKAsnahnfisqLpngyeTQVG------ERGVQ 497
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRLGrtstwRSLlglfppEDRERALEA---------L-----ERVGladkayQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 498 MSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEAL--ENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIV 574
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrrIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
378-585 |
7.92e-31 |
|
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: 124.40 E-value: 7.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLA---GEILIDGVSIDKL---QVKWLR-SQMGLVSQEP--AL-- 446
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLsekELRKIRgREIQMIFQDPmtSLnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 447 -------FATTIKENILFGKEDAsMDDVVEAAKA---SNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSP 516
Cdd:COG0444 102 vmtvgdqIAEPLRIHGGLSKAEA-RERAIELLERvglPDPERRLDRYPH-----------ELSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 517 TILLLDEATSALDseserV-VQ-EALE-----NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:COG0444 170 KLLIADEPTTALD-----VtIQaQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
358-585 |
8.49e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.87 E-value: 8.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDG--VSIDkLQVKwlRS 435
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdLFTN-LPPR--ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALFA-TTIKENILFGKEDASMDDVVEAAKASN----------AHNFISQLpngyetqvgergvqmSGGQKQ 504
Cdd:COG1118 76 RVGFVFQHYALFPhMTVAENIAFGLRVRPPSKAEIRARVEEllelvqleglADRYPSQL---------------SGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 505 RIAIARAIIKSPTILLLDEATSALDS----ESERVVQEALENasIGRTTILIAH-RLSTIRNADVISVVKNGHIVETGSH 579
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTP 218
|
....*.
gi 15229473 580 DELMEN 585
Cdd:COG1118 219 DEVYDR 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1013-1215 |
9.36e-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: 120.86 E-value: 9.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKIE---EGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGR---DIR-SYHLRSLRRHIALVSQEPTLFAG 1085
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 -TIRENIIYG--GVSDKIDEaeiieaakaanahDFITSLTEGYD-TYCGDRGV-QLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:cd03297 90 lNVRENLAFGlkRKRNREDR-------------ISVDELLDLLGlDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1161 EATSALDSQSERVVQDALERVM--VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKknLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
382-585 |
9.75e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.45 E-value: 9.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYD--PLA---GEILIDGVSI--DKLQVKWLRSQMGLVSQEPALFATTIKEN 454
Cdd:COG1117 32 LDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFG------KEDASMDDVVEAAkasnahnfisqLpngyeTQVG----------ERGVQMSGGQKQRIAIARAIIKSPTI 518
Cdd:COG1117 112 VAYGlrlhgiKSKSELDEIVEES-----------L-----RKAAlwdevkdrlkKSALGLSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 519 LLLDEATSALDSESERVVQEALENASiGRTTILI-------AHRLStirnaDVISVVKNGHIVETGSHDELMEN 585
Cdd:COG1117 176 LLMDEPTSALDPISTAKIEELILELK-KDYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQIFTN 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
359-585 |
1.01e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPsrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI--DKLQVKWLRSQ 436
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFA-TTIKENILFG--------KEDA---SMDDVVEAAKASNAHNFISQLpngyetqvgergvqmSGGQKQ 504
Cdd:PRK09493 79 AGMVFQQFYLFPhLTALENVMFGplrvrgasKEEAekqARELLAKVGLAERAHHYPSEL---------------SGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 505 RIAIARAIIKSPTILLLDEATSALDSESE----RVVQEALENasiGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSH 579
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEE---GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDP 220
|
....*.
gi 15229473 580 DELMEN 585
Cdd:PRK09493 221 QVLIKN 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1014-1216 |
2.68e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.72 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKST---IIGLIERfydPLKGIVKIDGRDIRSyHLRSLRRHIALVSQEPTLFAG-TIRE 1089
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDLFT-NLPPRERRVGFVFQHYALFPHmTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NIIYGgvsdkIDEAEIIEAAKAANAHDFItSLT--EGYdtycGDRGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:COG1118 95 NIAFG-----LRVRPPSKAEIRARVEELL-ELVqlEGL----ADRYPsQLSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1167 DSQservVQDALERVM------VGRTSVVIAH------RLstiqnCDAIAVLDKGKLVERGT 1216
Cdd:COG1118 165 DAK----VRKELRRWLrrlhdeLGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
360-577 |
2.73e-30 |
|
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: 118.31 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGL 439
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQepalfattikenilfgkedasmddVVEAAKASN-AHNFISQLpngyetqvgergvqmSGGQKQRIAIARAIIKSPTI 518
Cdd:cd03214 78 VPQ------------------------ALELLGLAHlADRPFNEL---------------SGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 519 LLLDEATSALD--SESE--RVVQEalENASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETG 577
Cdd:cd03214 119 LLLDEPTSHLDiaHQIEllELLRR--LARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1012-1211 |
3.27e-30 |
|
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: 119.17 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI--RSYHLRSLRRHIALVSQEPTLFAG-TIR 1088
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1089 ENIIYG-----GVSDKideaeiieaAKAANAHDFIT--SLTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:cd03262 95 ENITLApikvkGMSKA---------EAEERALELLEkvGLADKADAYPA----QLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1162 ATSALDSQserVVQDALErVMV-----GRTSVVIAHRLSTIQN-CDAIAVLDKGKL 1211
Cdd:cd03262 162 PTSALDPE---LVGEVLD-VMKdlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
359-585 |
3.57e-30 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 119.65 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQMG 438
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFA-TTIKENILFGKEDASMDDVVEAAKASNAHNFIsQLpNGYEtqvGERGVQMSGGQKQRIAIARAIIKSPT 517
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGLRLKKLPKAEIKERVAEALDLV-QL-EGYA---NRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 518 ILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
56-297 |
3.88e-30 |
|
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: 121.50 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 56 TSKLMNNIGGSsFNTDTFMQSIsknsVALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTS 135
Cdd:cd18572 19 TGAVIDAVVAD-GSREAFYRAV----LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 136 TSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEY 215
Cdd:cd18572 92 TGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 216 NEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIGSNgiTFAMWG---FMSWYGSRMVMYHG 292
Cdd:cd18572 172 AEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVN--TLLQNGtqvLVLFYGGHLVLSGR 249
|
....*
gi 15229473 293 AQGGT 297
Cdd:cd18572 250 MSAGQ 254
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
359-564 |
4.24e-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: 119.05 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRS 435
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALFAT-TIKENILFGKE--DASMDDVVEAAKASnahnfISQLpnGYETQVGERGVQMSGGQKQRIAIARAI 512
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAA-----LELV--GLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 513 IKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIA-----------HRLSTIRNADV 564
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAthakelvdttrHRVIALERGKL 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
357-594 |
5.32e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 129.86 E-value: 5.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPSRLETSIFDDFCLRVPSGKtVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEK-VGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFATTIKENI-LFGK-EDAsmdDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIK 514
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFNLdPFNEhNDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 515 SPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENIDGQYSTLV 594
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMV 1471
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
995-1224 |
1.28e-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: 119.46 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRS-YHLRSLRRHI 1073
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPT--LFAGTIRENIIYG----GVS-----DKIDEAEIIEaakaaNAHDFITSLTEgydtycgdrgvQLSGGQKQ 1142
Cdd:TIGR04520 80 GMVFQNPDnqFVGATVEDDVAFGlenlGVPreemrKRVDEALKLV-----GMEDFRDREPH-----------LLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1143 RIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSL 1220
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
....
gi 15229473 1221 LSKG 1224
Cdd:TIGR04520 224 FSQV 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
359-578 |
2.66e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.68 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYP-SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRS-- 435
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 -QMGLVSQEPALFAT-TIKENILF-----GKEDASMDDVVE--------AAKasnAHNFISQLpngyetqvgergvqmSG 500
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNVALplelaGTPKAEIKARVTellelvglSDK---ADRYPAQL---------------SG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 501 GQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
.
gi 15229473 578 S 578
Cdd:PRK11153 224 T 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
994-1233 |
3.17e-29 |
|
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: 118.09 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHI 1073
Cdd:cd03288 21 KIHDLCVRYENNLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPTLFAGTIRENIiygGVSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKN 1153
Cdd:cd03288 98 SIILQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1154 PSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKgPTGIYFSLV 1233
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ-EDGVFASLV 253
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
359-573 |
3.70e-29 |
|
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: 116.09 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI--DKLQVKWLRSQ 436
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFA-TTIKENILFG-----KEDAsmDDVVEAAK--------ASNAHNFISQLpngyetqvgergvqmSGGQ 502
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLApikvkGMSK--AEAEERALellekvglADKADAYPAQL---------------SGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 503 KQRIAIARAIIKSPTILLLDEATSALDSEserVVQEALEN----ASIGRTTILIAHRLSTIRN-ADVISVVKNGHI 573
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
995-1213 |
4.14e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.31 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRD---IRSYHLRSLRR 1071
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTLFAG-TIRENIIYG----GVSDKideaeiieaAKAANAHDFIT--SLTEGYDTYCgdrgVQLSGGQKQRI 1144
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALPlrvtGKSRK---------EIRRRVREVLDlvGLSDKAKALP----HELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1145 AIARAVLKNPSVLLLDEATSALD-SQSERVVqDALERV-MVGrTSVVIA-HRLSTIQNCDA-IAVLDKGKLVE 1213
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDpETSWEIM-ELLEEInRRG-TTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1004-1216 |
4.62e-29 |
|
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: 116.07 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1004 YPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsYHLRSLRRHIALVSQEPTLF 1083
Cdd:cd03263 10 YKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AG-TIRENI-IYG---GVSDKIdeaeiieAAKAANAHDFITSLTEGYDTYCGDrgvqLSGGQKQRIAIARAVLKNPSVLL 1158
Cdd:cd03263 88 DElTVREHLrFYArlkGLPKSE-------IKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1159 LDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
996-1220 |
4.76e-29 |
|
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: 116.90 E-value: 4.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 996 EFLDVDFSYPTrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSY---HLRSLRRH 1072
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEPTLFAG-TIRENIIYGGVsdkideaeiieaakaaNAHDFITSL-----------------TEGYDTYCGDRGV 1134
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRL----------------GRRSTWRSLfglfpkeekqralaaleRVGLLDKAYQRAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1135 QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTI-QNCDAIAVLDKGKL 1211
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
....*....
gi 15229473 1212 VERGTHSSL 1220
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
359-596 |
6.43e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.96 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYP--SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI-----DKlQVK 431
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDK-YIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 432 WLRSQMGLVSQ--EPALFATTIKENILFGKEDASMDdvVEAAKaSNAHNFISQLpnGYETQVGERG-VQMSGGQKQRIAI 508
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVK-NYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALENASI--GRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELMEn 585
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK- 235
|
250
....*....|.
gi 15229473 586 iDGQYSTLVHL 596
Cdd:PRK13646 236 -DKKKLADWHI 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
359-567 |
7.54e-29 |
|
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: 115.27 E-value: 7.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKST---VISLLQRfydPLAGEILIDGVSIDKLQVKWlRS 435
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllrILAGLLP---PSAGEVLWNGEPIRDAREDY-RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALFAT-TIKENILF----GKEDASMDDVVEAAK----ASNAHNFISQLpngyetqvgergvqmSGGQKQRI 506
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEavglAGLADLPVRQL---------------SAGQKRRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 507 AIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIA-HRLSTIRNADVISV 567
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
359-584 |
7.85e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.42 E-value: 7.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:PRK13635 6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEP--ALFATTIKENILFGKEDASM--DDVVE----AAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIAR 510
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENIGVprEEMVErvdqALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 511 AIIKSPTILLLDEATSALDSESErvvQEALE-----NASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELME 584
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
360-583 |
8.86e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 115.62 E-value: 8.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRLETsiFDdfcLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVkwlrSQ--M 437
Cdd:COG3840 3 RLDDLTYRYGDFPLR--FD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErpV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEPALFA-TTIKENILFG--------KEDASmdDVVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAI 508
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIGLGlrpglkltAEQRA--QVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALD----SESERVVQEAleNASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELM 583
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDEL--CRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
359-582 |
1.68e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.37 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEP--ALFATTIKENILFGKEDASMD------DVVEAAKASNAHNFISQLPngyetqvgergVQMSGGQKQRIAIAR 510
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPheemkeRVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 511 AIIKSPTILLLDEATSALDSESE----RVVQEALEnaSIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRD--DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
378-585 |
1.78e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 117.91 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRSQMGLVSQEPalFAT----- 449
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDP--YASlnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFG------KEDASMDDVVEAA------KASNAHNFisqlPNgyetqvgergvQMSGGQKQRIAIARAIIKSPT 517
Cdd:COG4608 113 TVGDIIAEPlrihglASKAERRERVAELlelvglRPEHADRY----PH-----------EFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 518 ILLLDEATSALD-SESERVV------QEALenasiGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:COG4608 178 LIVCDEPVSALDvSIQAQVLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
996-1211 |
3.06e-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: 113.78 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 996 EFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKIDGRdirsyHLRSLRR 1071
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLLK----PTSGSIRVFGK-----PLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTL---FAGTIRENIIYGGVSDK--IDEAEIIEAAKAANAHDF--ITSLtegydtycGDRGV-QLSGGQKQR 1143
Cdd:cd03235 69 RIGYVPQRRSIdrdFPISVRDVVLMGLYGHKglFRRLSKADKAKVDEALERvgLSEL--------ADRQIgELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1144 IAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV-MVGRTSVVIAHRLSTIQN-CDAIAVLDKGKL 1211
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
359-596 |
5.96e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 5.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLqvkwlRSQMG 438
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPAL---FATTIKENIL------------FGKEDAsmDDVVEAAKASNAHNFISQlpngyetQVGErgvqMSGGQK 503
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLmgrygrrglfrrPSRADR--EAVDEALERVGLEDLADR-------PIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 504 QRIAIARAIIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIR-NADVISVVkNGHIVETGSHDE 581
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPEE 224
|
250
....*....|....*..
gi 15229473 582 LM--ENIDGQYSTLVHL 596
Cdd:COG1121 225 VLtpENLSRAYGGPVAL 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
358-585 |
7.62e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 113.20 E-value: 7.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQM 437
Cdd:cd03296 2 SIEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEPALFA-TTIKENILFG-KEDASMDDVVEAAKASNAHNFI-----SQLPNGYETQvgergvqMSGGQKQRIAIAR 510
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYPAQ-------LSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRrlHDELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
35-289 |
1.05e-27 |
|
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: 114.57 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 35 MGLGLIGAVGDGFTTPLVLLITSKLMNNIGGssfNTDtfMQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQTARMR 114
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIP---AGD--LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 115 EKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLV 194
Cdd:cd07346 76 RDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 195 IPGLMYGRALISISRKIREEYNE-AGFVAEqAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIGSNG-I 272
Cdd:cd07346 154 LILRYFRRRIRKASREVRESLAElSAFLQE-SLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGlL 232
|
250
....*....|....*..
gi 15229473 273 TFAMWGFMSWYGSRMVM 289
Cdd:cd07346 233 TALGTALVLLYGGYLVL 249
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1014-1223 |
1.33e-27 |
|
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: 112.43 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyhLRSLRRHIALVSQEPTLFAG-TIRENII 1092
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFPHmTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1093 YGGVSDKIDEAEIIEAAKAANAHDFITSLTegydtycgDRGVQ-LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE 1171
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLL--------NRKPEtLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1172 RVVQDALERVM--VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:cd03299 166 EKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
995-1211 |
1.48e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.49 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKIDGRDIRSyhlrsLR 1070
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTllkaILGLLP----PTSGTVRLFGKPPRR-----AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1071 RHIALVSQEPTL---FAGTIRENI---IYGGVS-----DKIDEAEIIEAAKAANAHDFItsltegydtycgDRGV-QLSG 1138
Cdd:COG1121 75 RRIGYVPQRAEVdwdFPITVRDVVlmgRYGRRGlfrrpSRADREAVDEALERVGLEDLA------------DRPIgELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALER-VMVGRTSVVIAHRLSTI-QNCDAIAVLDKGKL 1211
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
93-289 |
1.78e-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: 113.73 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 93 VVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFdlHVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSY 172
Cdd:cd18576 51 VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFF--HERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 173 IVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGS 252
Cdd:cd18576 129 VLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15229473 253 VKLGIKQGLAKGITIGSngITFAMWG---FMSWYGSRMVM 289
Cdd:cd18576 209 VKLALKRARIRALFSSF--IIFLLFGaivAVLWYGGRLVL 246
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
999-1225 |
1.96e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.77 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPdviifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyHLRSLRRHIALVSQ 1078
Cdd:COG3840 6 DLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EPTLFAG-TIRENIiYGGVSD--KIDEaeiieaakaaNAHDFITSLTEGYD-TYCGDR--GvQLSGGQKQRIAIARAVLK 1152
Cdd:COG3840 79 ENNLFPHlTVAQNI-GLGLRPglKLTA----------EQRAQVEQALERVGlAGLLDRlpG-QLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1153 NPSVLLLDEATSALDSqservvqdALERVMV----------GRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLL 1221
Cdd:COG3840 147 KRPILLLDEPFSALDP--------ALRQEMLdlvdelcrerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
....
gi 15229473 1222 SKGP 1225
Cdd:COG3840 219 DGEP 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
995-1212 |
2.10e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 112.46 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI---RSYHLRSLRR 1071
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTLFAG-TIRENIIYGGVsdkideaeiieaakaaNAHDFITSLTEGYDT-----------------YCGDRG 1133
Cdd:COG3638 81 RIGMIFQQFNLVPRlSVLTNVLAGRL----------------GRTSTWRSLLGLFPPedreralealervgladKAYQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1134 VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRLSTIQN-CDAIAVLDKGK 1210
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
..
gi 15229473 1211 LV 1212
Cdd:COG3638 225 VV 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
377-577 |
2.37e-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: 111.23 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 377 FDDFCLRVP---SGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGV----SIDKLQVKWLRSQMGLVSQEPALFA- 448
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 449 TTIKENILFG---KEDASMDDVVEAakasnahnfISQLPNgyETQVGERGV-QMSGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:cd03297 90 LNVRENLAFGlkrKRNREDRISVDE---------LLDLLG--LDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 525 TSALDSESERVVQEALEN--ASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETG 577
Cdd:cd03297 159 FSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1009-1216 |
2.67e-27 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 111.56 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrsYHLRSLRRHIALVSQEPTLFAG-TI 1087
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIYGGVSDKIDEAEIIEAAKAanAHDFITslTEGYdtycGDRGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAE--ALDLVQ--LEGY----ANRKPsQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1167 DSQSERVVQDALERV--MVGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGT 1216
Cdd:cd03300 162 DLKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
357-582 |
5.17e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.01 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPsrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQ 436
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALF-ATTIKENILFG----KED-ASMDD-VVEAAKasnahnfISQLpngyeTQVGERGV-QMSGGQKQRIAI 508
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPkAEIDRrVREAAE-------LLGL-----EDLLDRKPkQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESeRV--------VQEALenasiGRTTILIAHRLS---TIrnADVISVVKNGHIVETG 577
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVG 216
|
....*
gi 15229473 578 SHDEL 582
Cdd:COG3839 217 TPEEL 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
359-588 |
6.04e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 6.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:PRK13648 8 IVFKNVSFQYQSD-ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEP--ALFATTIKENILFGKEDASM--DDVVE-AAKASNAHNFISQlpNGYETQvgergvQMSGGQKQRIAIARAII 513
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAVpyDEMHRrVSEALKQVDMLER--ADYEPN------ALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 514 KSPTILLLDEATSALDSESE----RVVQEALENASIgrTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENIDG 588
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARqnllDLVRKVKSEHNI--TIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
359-587 |
6.83e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.06 E-value: 6.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVY--PSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKW--LR 434
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 435 SQMGLVSQEP--ALFATTIKENILFG------KEDASMDDVVEAAKasnahnfISQLPngYETQVGERGVQMSGGQKQRI 506
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGpinlglSEEEIENRVKRAMN-------IVGLD--YEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 507 AIARAIIKSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELM 583
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVF 233
|
....
gi 15229473 584 ENID 587
Cdd:PRK13637 234 KEVE 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
359-585 |
1.47e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYP--SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSID----KLQVKW 432
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 433 LRSQMGLVSQ--EPALFATTIKENILFGKED--ASMDDVVEAAKasnahNFISQLpnGYETQVGERG-VQMSGGQKQRIA 507
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKV--GLSEDLISKSpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 508 IARAIIKSPTILLLDEATSALDSES-ERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1006-1207 |
1.48e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 108.34 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1006 TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKIDGRDIRSyHLRSLRRHIALVSQEPT 1081
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRD-AREDYRRRLAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1082 LFAG-TIRENI-----IYGGVSDKIDeaeiieaakaanAHDFITS--LTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKN 1153
Cdd:COG4133 86 LKPElTVRENLrfwaaLYGLRADREA------------IDEALEAvgLAGLADLPVR----QLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1154 PSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIA-HRLSTIQNCDAIAVLD 1207
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGD 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
352-585 |
1.68e-26 |
|
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: 109.35 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 352 LEKIRGEVEFKNVKFvypsrletsifddfclRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVK 431
Cdd:cd03299 6 LSKDWKEFKLKNVSL----------------EVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 432 wlRSQMGLVSQEPALFA-TTIKENILFG----KEDASMDD--VVEAAKASNahnfISQLPNGYETQvgergvqMSGGQKQ 504
Cdd:cd03299 70 --KRDISYVPQNYALFPhMTVYKNIAYGlkkrKVDKKEIErkVLEIAEMLG----IDHLLNRKPET-------LSGGEQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 505 RIAIARAIIKSPTILLLDEATSALDSESERVVQEALENA--SIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDE 581
Cdd:cd03299 137 RVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
....
gi 15229473 582 LMEN 585
Cdd:cd03299 217 VFKK 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
995-1224 |
1.86e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTrPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEP-TLFAGTIRENIIYGGVSDKideaeiieAAKAANAHDFITSLTEGYD--TYCGDRGVQLSGGQKQRIAIARAVL 1151
Cdd:PRK13648 87 IVFQNPdNQFVGSIVKYDVAFGLENH--------AVPYDEMHRRVSEALKQVDmlERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1152 KNPSVLLLDEATSALDSQSERVVQDALERVMVGR--TSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKG 1224
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
704-940 |
3.46e-26 |
|
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: 109.94 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 704 SHDEIKEKTRIYALSFVGLAVLSFLinisQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDAN 783
Cdd:cd18572 31 SREAFYRAVLLLLLLSVLSGLFSGL----RGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 784 VVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALV-MIAVQPVIIVC-FYTRRVllKSMSKKAIKAQDESSKLAAEAV 861
Cdd:cd18572 105 KVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLaFITVPVIALITkVYGRYY--RKLSKEIQDALAEANQVAEEAL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 862 SNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYITAKALFeTFMI 940
Cdd:cd18572 183 SNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLV-TFML 260
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1015-1216 |
3.93e-26 |
|
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: 108.20 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRslRRHIALVSQEPTLFAG-TIRENIIY 1093
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRHmTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1094 GgVSDKIDEAEIIEAAKAANAHDFI--TSLTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE 1171
Cdd:cd03296 98 G-LRVKPRSERPPEAEIRAKVHELLklVQLDWLADRYPA----QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229473 1172 RVVQDALERVM--VGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGT 1216
Cdd:cd03296 173 KELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
995-1191 |
4.19e-26 |
|
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: 107.49 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRS---LRR 1071
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTLFAG-TIRENIIYGGVSdkIDEAEIIEAAKAANAHDFItSLTEGYDTYcgdrGVQLSGGQKQRIAIARAV 1150
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEV--TGVPPREIRKRVPAALELV-GLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIA 1191
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
677-943 |
4.37e-26 |
|
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: 109.82 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 677 ISATLFGAIQPAYAYSLGSMVsvyfltshDEIKEKTRIYALSFVGLAV--LSFLINIS---QHYNFAYMGEYLTKRIRER 751
Cdd:cd18552 6 LGMILVAATTAALAWLLKPLL--------DDIFVEKDLEALLLVPLAIigLFLLRGLAsylQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 752 MLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVC 831
Cdd:cd18552 78 LFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 832 FytrRVLLKSMSKKAIKAQDESSKLAA---EAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSL 908
Cdd:cd18552 156 I---RRIGKRLRKISRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260 270
....*....|....*....|....*....|....*
gi 15229473 909 TSCTWALDFWYGGRLIQDGYITAKALFeTFMILVS 943
Cdd:cd18552 233 GAIAIALVLWYGGYQVISGELTPGEFI-SFITALL 266
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1012-1215 |
6.20e-26 |
|
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: 106.48 E-value: 6.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLI--ERFYDPLKGIVKIDGRDIrsyHLRSLRRHIALVSQE----PTLfag 1085
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDdilhPTL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 TIRENIIYggvSDKIdeaeiieaakaanahdfitsltegydtycgdRGvqLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:cd03213 98 TVRETLMF---AAKL-------------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1166 LDSQSERVVQDALER-VMVGRTSVVIAHRLST--IQNCDAIAVLDKGKLVERG 1215
Cdd:cd03213 142 LDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
378-585 |
6.48e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 113.63 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTV-ISLLQrfYDPLAGEILIDGVSIDKL---QVKWLRSQMGLVSQEPalFAT---- 449
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLgLALLR--LIPSEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDP--FGSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 -----TIKENILF---GKEDASMDDVVEAA------KASNAHNFISQLpngyetqvgergvqmSGGQKQRIAIARAIIKS 515
Cdd:COG4172 379 mtvgqIIAEGLRVhgpGLSAAERRARVAEAleevglDPAARHRYPHEF---------------SGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 516 PTILLLDEATSALDseseRVVQealenASI-----------GRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELM 583
Cdd:COG4172 444 PKLLVLDEPTSALD----VSVQ-----AQIldllrdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 15229473 584 EN 585
Cdd:COG4172 515 DA 516
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
379-590 |
6.57e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.66 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 379 DFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRS----QMGLVSQEPALFA-TTIKE 453
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 454 NILFGKEDASmddVVEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESE 533
Cdd:PRK10070 126 NTAFGMELAG---INAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 534 RVVQEALE--NASIGRTTILIAHRL-STIRNADVISVVKNGHIVETGSHDELMENIDGQY 590
Cdd:PRK10070 201 TEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
358-574 |
8.69e-26 |
|
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: 106.10 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSRLETS---IFDDFCLRVPSGKTVALVGGSGSGKSTVISLL--QRFYDPLAGEILIDGVSIDKlqvKW 432
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 433 LRSQMGLVSQEPALFAT-TIKENILFgkedasmddvveAAKAsnahnfisqlpngyetqvgeRGVqmSGGQKQRIAIARA 511
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAKL--------------------RGL--SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 512 IIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLST--IRNADVISVVKNGHIV 574
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
687-934 |
8.73e-26 |
|
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: 108.88 E-value: 8.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 687 PAYAYSLGSMVSVYFLTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDr 766
Cdd:cd18780 16 PYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 767 dENSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCF--YTRRVllKSMSK 844
Cdd:cd18780 95 -VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAviYGKYV--RKLSK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 845 KAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESP----RRESIRQSWFAGFGLAMSQsltsCTWALDFWYG 920
Cdd:cd18780 172 KFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESyllgKKLARASGGFNGFMGAAAQ----LAIVLVLWYG 247
|
250
....*....|....
gi 15229473 921 GRLIQDGYITAKAL 934
Cdd:cd18780 248 GRLVIDGELTTGLL 261
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
999-1215 |
9.61e-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: 106.51 E-value: 9.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRpdvIIFKNFSIKIEEGkSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyHLRSLRRHIALVSQ 1078
Cdd:cd03264 5 NLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EPTLFAG-TIRENIIY----GGVSDKIDEAEIIEAAKAANahdfitsLTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKN 1153
Cdd:cd03264 80 EFGVYPNfTVREFLDYiawlKGIPSKEVKARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1154 PSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
359-609 |
1.23e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.90 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEP--ALFATTIKENILFGKEDASMDD------VVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIAR 510
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLDKdeverrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 511 AIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIA-HRLS-TIRNADVISVVKNGHIVETG-----SHDELM 583
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250 260 270
....*....|....*....|....*....|
gi 15229473 584 ENIDGQYSTLV----HLQQIEKQDINVSVK 609
Cdd:PRK13647 232 EQAGLRLPLVAqifeDLPELGQSKLPLTVK 261
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
39-297 |
1.67e-25 |
|
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: 108.17 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 39 LIGAVGDGFttplVLLITSKLMNNIGgssfnTDTFMQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYL 118
Cdd:cd18784 6 LAAAVGEIF----IPYYTGQVIDGIV-----IEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 119 RAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIV---GLPFIVLLvi 195
Cdd:cd18784 77 RSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVtliGLPLIAIV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 196 pGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIGSNGITF- 274
Cdd:cd18784 153 -SKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTEl 231
|
250 260
....*....|....*....|...
gi 15229473 275 AMWGFMSWYGSRMVMYHGAQGGT 297
Cdd:cd18784 232 ALTVSTLYYGGHLVITGQISGGN 254
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
360-577 |
2.07e-25 |
|
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: 105.31 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLqvkwlRSQMGL 439
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQEPAL---FATTIKENILFG------------KEDasMDDVVEAAKASNAHNFISQlpngyetQVGErgvqMSGGQKQ 504
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGlyghkglfrrlsKAD--KAKVDEALERVGLSELADR-------QIGE----LSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 505 RIAIARAIIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIRNA--DVISVvkNGHIVETG 577
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfdRVLLL--NRTVVASG 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
359-577 |
3.07e-25 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 105.03 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQMG 438
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFA-TTIKENILFG------KEDASMDDVVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARA 511
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 512 IIKSPTILLLDEATSALD--------SESERVVQEalenasIGRTTILIAH-RLSTIRNADVISVVKNGHIVETG 577
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDaklrvqmrAELKRLQQR------LGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
359-571 |
3.34e-25 |
|
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: 105.11 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETsiFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQ-- 436
Cdd:cd03290 1 VQVTNGYFSWGSGLAT--LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 --MGLVSQEPALFATTIKENILFG----KEDASMddVVEAAKASNAhnfISQLPNGYETQVGERGVQMSGGQKQRIAIAR 510
Cdd:cd03290 79 ysVAYAAQKPWLLNATVEENITFGspfnKQRYKA--VTDACSLQPD---IDLLPFGDQTEIGERGINLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 511 AIIKSPTILLLDEATSALDSE-SERVVQEALEN--ASIGRTTILIAHRLSTIRNADVISVVKNG 571
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
999-1224 |
3.79e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 106.64 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYP--TRPDViifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALV 1076
Cdd:PRK13635 10 HISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1077 SQEP-TLFAG-TIRENIIYG----GVSDKIDEAEIIEAAKAANAHDFITsltegydtycgDRGVQLSGGQKQRIAIARAV 1150
Cdd:PRK13635 87 FQNPdNQFVGaTVQDDVAFGleniGVPREEMVERVDQALRQVGMEDFLN-----------REPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALeRVMV---GRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKG 1224
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETV-RQLKeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
995-1216 |
3.96e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.88 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyHLRSLRRHIA 1074
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAG-TIRENIIYGGVSDKIdeaeiieaakaanAHDFITSLT---------EGYdtycGDRGV-QLSGGQKQR 1143
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGLRMQKT-------------PAAEITPRVmealrmvqlEEF----AQRKPhQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1144 IAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAH-RLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
382-585 |
4.36e-25 |
|
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: 104.82 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVkWLRSQMGL--VSQEPALFAT-TIKENILFG 458
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-HERARAGIgyVPEGRRIFPElTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 459 -------KEDASMDDVVEAakasnahnfisqLPNGYETQvGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALdse 531
Cdd:cd03224 100 ayarrraKRKARLERVYEL------------FPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL--- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 532 SERVVQE---ALEN-ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:cd03224 164 APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
379-655 |
7.05e-25 |
|
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: 107.89 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 379 DFCL----RVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGV----SIDKLQVKWLRSQMGLVSQEPALFA-T 449
Cdd:TIGR02142 11 DFSLdadfTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFPhL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDASMDDvveaaKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALD 529
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSE-----RRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 530 SESERVVQEALEN--ASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELMEniDGQYSTLVHLQQ-------I 599
Cdd:TIGR02142 164 DPRKYEILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWA--SPDLPWLAREDQgsliegvV 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 600 EKQD--------------INVSVKIGPISDPSKdIRNSSRVSTLSRS----SSANSVTgPSTIKNLSEDNKPQL 655
Cdd:TIGR02142 242 AEHDqhygltalrlggghLWVPENLGPTGARLR-LRVPARDVSLALQkpeaTSIRNIL-PARVVEIEDSDIGRV 313
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
691-961 |
8.60e-25 |
|
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: 106.06 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 691 YSLGSMVSVYFLTSHD--EIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRde 768
Cdd:cd18573 17 FAIGKLIDVASKESGDieIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 769 NSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVC--FYTRRVllKSMSKKA 846
Cdd:cd18573 95 NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGavFYGRYV--RKLSKQV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 847 IKAQDESSKLAAEAVSNVRTITAFSSQERIM----KMLEKAQESPRRESI-RQSWFAGFGLAMSQSLTSCtwaldFWYGG 921
Cdd:cd18573 173 QDALADATKVAEERLSNIRTVRAFAAERKEVeryaKKVDEVFDLAKKEALaSGLFFGSTGFSGNLSLLSV-----LYYGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15229473 922 RLIQDGYITAKALFETFMILVSTGRVIADAGSMTTDLAKG 961
Cdd:cd18573 248 SLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKG 287
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
375-576 |
1.09e-24 |
|
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: 104.05 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 375 SIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRSQ-MGLVSQEPALFAT- 449
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARhVGFVFQSFQLLPTl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDASMDDVVEAAKASNAhnfisqlpngyetQVG--ERG----VQMSGGQKQRIAIARAIIKSPTILLLDE 523
Cdd:COG4181 106 TALENVMLPLELAGRRDARARARALLE-------------RVGlgHRLdhypAQLSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 524 ATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRNADVISVVKNGHIVET 576
Cdd:COG4181 173 PTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1014-1216 |
1.18e-24 |
|
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: 104.06 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI--RSYHLRSlRRHIALVSQEPTLFAG-TIREN 1090
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIA-RLGIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 IIYGGVSDKIDEAEIIEAAKAANAH--------DFITsLTEGYDTYCGDrgvqLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREAreraeellERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1163 TSALDSQSERVVQDALERVMV-GRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:cd03219 171 AAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
995-1226 |
1.42e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.02 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHL--RSLRRH 1072
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdeRLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEPTLFAG-TIRENIIYGgvsdKIDEAEIIEAAKAANAHDFITS--LTEGYDTYCGdrgvQLSGGQKQRIAIARA 1149
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFG----PLRVRGASKEEAEKQARELLAKvgLAERAHHYPS----ELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1150 VLKNPSVLLLDEATSALDSQSE----RVVQDALERVMvgrTSVVIAHRLSTIQNCDA-IAVLDKGKLVERGTHSSLLSKG 1224
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGM---TMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIKNP 227
|
..
gi 15229473 1225 PT 1226
Cdd:PRK09493 228 PS 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
995-1224 |
1.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.25 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYP--TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI----RSYHLRS 1068
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1069 LRRHIALVSQ--EPTLFAGTIRENIIYGGVSDKIDEAEIIEAakaanAHDFITSLteGYDtycgdRGV------QLSGGQ 1140
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNY-----AHRLLMDL--GFS-----RDVmsqspfQMSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1141 KQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERGTH 1217
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSP 230
|
....*..
gi 15229473 1218 SSLLSKG 1224
Cdd:PRK13646 231 KELFKDK 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
998-1222 |
1.75e-24 |
|
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: 106.72 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 998 LDVDFSyptrpdviifknfsikIEEGKSTAIVGPSGSGKSTIIGLI---ERfydPLKGIVKIDGRDI----RSYHLRSLR 1070
Cdd:COG4148 16 LDVDFT----------------LPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLqdsaRGIFLPPHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1071 RHIALVSQEPTLFAG-TIRENIIYG-----GVSDKIDeaeiieaakaanaHDFITSLtegydtyCG-----DRGV-QLSG 1138
Cdd:COG4148 77 RRIGYVFQEARLFPHlSVRGNLLYGrkrapRAERRIS-------------FDEVVEL-------LGighllDRRPaTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVmvgRTSVVI-----AHRLSTIQN-CDAIAVLDKGKLV 1212
Cdd:COG4148 137 GERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERL---RDELDIpilyvSHSLDEVARlADHVVLLEQGRVV 213
|
250
....*....|
gi 15229473 1213 ERGTHSSLLS 1222
Cdd:COG4148 214 ASGPLAEVLS 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1017-1215 |
1.82e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.97 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1017 SIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYH---LRSLRRHIALVSQEPtlFAG-----TIR 1088
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YASlnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1089 ENI-----IYGGVSDKideaeiieaakaaNAHDFITSLTE--GYDTYCGDR-GVQLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:COG4608 116 DIIaeplrIHGLASKA-------------ERRERVAELLElvGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1161 EATSALD----SQserVV------QDALervmvGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:COG4608 183 EPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIA 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
357-594 |
2.18e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.41 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPSRLETsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPL-VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFATTIKENILFGKEdASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 517 T-ILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENIDGQYSTLV 594
Cdd:PTZ00243 1465 SgFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
382-585 |
2.34e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.68 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSID--------KLQVKWLRSQMGLVSQEPALFA-TTIK 452
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslsqqKGLIRQLRQHVGFVFQNFNLFPhRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 453 ENILFGK---EDASMDDVVEAAKASNAHNFISqlpnGYETQVGERgvqMSGGQKQRIAIARAIIKSPTILLLDEATSALD 529
Cdd:PRK11264 104 ENIIEGPvivKGEPKEEATARARELLAKVGLA----GKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 530 SEserVVQEALEN----ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK11264 177 PE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
359-584 |
2.47e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.57 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQMG 438
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFA-TTIKENILFG------KEDASMDDVVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARA 511
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrmqktPAAEITPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 512 IIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAH-RLSTIRNADVISVVKNGHIVETGSHDELME 584
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
995-1215 |
2.48e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 102.19 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyHLRSLRRHIA 1074
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTLFAG-TIRENIIYGGVS----DKIDEAEIIEAAKAANAHDFITSLTEgydtycgdrgvQLSGGQKQRIAIARA 1149
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSPglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1150 VLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTIQNCDAIAV-LDKGKLVERG 1215
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
993-1216 |
2.73e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.93 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 993 GQVEFLDVDFSYPtrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrsYHLRSLRRH 1072
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEPTLF-AGTIRENIIYG----GVS-DKIDEAEIIEaakaanAHdfITSLTEgydtyCGDRGV-QLSGGQKQRIA 1145
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPkAEIDRRVREA------AE--LLGLED-----LLDRKPkQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1146 IARAVLKNPSVLLLDEATSALDSQSeRV--------VQDALervmvGRTSVVIAH------RLStiqncDAIAVLDKGKL 1211
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHdqveamTLA-----DRIAVMNDGRI 212
|
....*
gi 15229473 1212 VERGT 1216
Cdd:COG3839 213 QQVGT 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
359-582 |
2.74e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 102.58 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETSIfDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKlQVKWLRSQMG 438
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFAT-TIKENILF-----GKEDASMDDVVEAAK-----ASNAHNFISQLpngyetqvgergvqmSGGQKQRIA 507
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLrvlglTDKANKRARTL---------------SGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 508 IARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
359-610 |
3.65e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.01 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETS---IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKW-LR 434
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 435 SQMGLVSQEP--ALFATTIKENILFGKEDASMDD------VVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRI 506
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPeeirerVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 507 AIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRNADVISVVKNGHIVETG------S 578
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGtpkeifK 233
|
250 260 270
....*....|....*....|....*....|....*
gi 15229473 579 HDELMENID---GQYSTLVHlqQIEKQDINVSVKI 610
Cdd:PRK13633 234 EVEMMKKIGldvPQVTELAY--ELKKEGVDIPSDI 266
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
385-585 |
3.77e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 385 PSGKTvALVGGSGSGKSTVISLLQRFYD-----PLAGEILIDGVSI-----DKLQvkwLRSQMGLVSQEPALFATTIKEN 454
Cdd:PRK14239 30 PNEIT-ALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysprtDTVD---LRKEIGMVFQQPNPFPMSIYEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFG------KEDASMDDVVEAA-KASNAHNFIsqlpngyETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSA 527
Cdd:PRK14239 106 VVYGlrlkgiKDKQVLDEAVEKSlKGASIWDEV-------KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 528 LDSESERVVQEALENASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
999-1212 |
6.00e-24 |
|
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: 101.18 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrsyHLRSLRRHIALVSQ 1078
Cdd:cd03226 4 NISFSYKKGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EPT--LFAGTIRENIIYGgvsdkideaeiieaakAANAHDFITSLTEGYDTYC----GDRGVQ-LSGGQKQRIAIARAVL 1151
Cdd:cd03226 79 DVDyqLFTDSVREELLLG----------------LKELDAGNEQAETVLKDLDlyalKERHPLsLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1152 KNPSVLLLDEATSALDSQSERVVQDALERVM-VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLV 1212
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1014-1215 |
6.30e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYD-----PLKGIVKIDGRDIrsYHLRS----LRRHIALVSQEPTLFA 1084
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNI--YSPRTdtvdLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1085 GTIRENIIYG----GVSDK--IDEAEIIEAAKaanahdfiTSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLL 1158
Cdd:PRK14239 100 MSIYENVVYGlrlkGIKDKqvLDEAVEKSLKG--------ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1159 LDEATSALDSQSERVVQDALERVMVGRTSVVIAHRL---STIQncDAIAVLDKGKLVERG 1215
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRIS--DRTGFFLDGDLIEYN 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
970-1225 |
8.94e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 970 AVLDR----YTSIDPEDPDGYETERIT----GQVEFLDVDFsypTRPDV-IIFKNFSIKIEEGKSTAIVGPSGSGKSTIi 1040
Cdd:COG4178 330 ATVDRlagfEEALEAADALPEAASRIEtsedGALALEDLTL---RTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTL- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1041 glierfydpLKGIVKI----DGRdIRsyhlRSLRRHIALVSQEPTLFAGTIRENIIYGGVSDKIDEAEIIEAAKAANAHD 1116
Cdd:COG4178 406 ---------LRAIAGLwpygSGR-IA----RPAGARVLFLPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGH 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1117 FITSLTEGydtycGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLST 1196
Cdd:COG4178 472 LAERLDEE-----ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTL 546
|
250 260
....*....|....*....|....*....
gi 15229473 1197 IQNCDaiAVLDkgkLVERGTHSSLLSKGP 1225
Cdd:COG4178 547 AAFHD--RVLE---LTGDGSWQLLPAEAP 570
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
370-1223 |
1.10e-23 |
|
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: 108.84 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 370 SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGvsidklqvkwlrsQMGLVSQEPALFAT 449
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGkedASMDDV--VEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSA 527
Cdd:TIGR01271 502 TIKDNIIFG---LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 528 LDSESERVVQEA-LENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELmENIDGQYST----LVHLQQIEKQ 602
Cdd:TIGR01271 579 LDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL-QAKRPDFSSlllgLEAFDNFSAE 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 603 DIN---------VSV----------------------------KIGPISDPSKDIRNSSRVSTLSRSSSAN----SVTGP 641
Cdd:TIGR01271 658 RRNsiltetlrrVSIdgdstvfsgpetikqsfkqpppefaekrKQSIILNPIASARKFSFVQMGPQKAQATtiedAVREP 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 642 STIK-------NLSEDNKPQLPSFKRLLAMnLPEWKQALYGCISATLFG-----AIQPAY--------AYSLGSMVSVY- 700
Cdd:TIGR01271 738 SERKfslvpedEQGEESLPRGNQYHHGLQH-QAQRRQSVLQLMTHSNRGenrreQLQTSFrkkssitqQNELASELDIYs 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 701 -------FLTSHDEIKE------------------------------KTRIYAL-------------SFVGLAVLS---- 726
Cdd:TIGR01271 817 rrlskdsVYEISEEINEedlkecfaderenvfetttwntylryittnRNLVFVLifclviflaevaaSLLGLWLITdnps 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 727 ---------------------FLINISQHY----------NFAYMGEY-----------LTKRIRERMLSKVLTFEVGWF 764
Cdd:TIGR01271 897 apnyvdqqhanasspdvqkpvIITPTSAYYifyiyvgtadSVLALGFFrglplvhtlltVSKRLHEQMLHSVLQAPMAVL 976
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 765 DRDEnsSGAICSRLAKDANVVRSL----VGDRMALVVQTVSAVtiaftmgLVIAWRLALVMIAVQPVIIVCFYTRRVLLK 840
Cdd:TIGR01271 977 NTMK--AGRILNRFTKDMAIIDDMlpltLFDFIQLTLIVLGAI-------FVVSVLQPYIFIAAIPVAVIFIMLRAYFLR 1047
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 841 SMSKKAIKAQDESSKLAAEAVSNVR---TITAFSSQERIMKMLEKAQESPrresiRQSWFagfglamsQSLTSCTWaldF 917
Cdd:TIGR01271 1048 TSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLH-----TANWF--------LYLSTLRW---F 1111
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 918 WYGGRLIQDGYITAKALFETFMILVSTGRV---IADAGSMTTDL---AKGSDAVGSVFAVLDR---YTSIDPEDPDG--- 985
Cdd:TIGR01271 1112 QMRIDIIFVFFFIAVTFIAIGTNQDGEGEVgiiLTLAMNILSTLqwaVNSSIDVDGLMRSVSRvfkFIDLPQEEPRPsgg 1191
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 986 -----------YETERIT------GQVEFLDVDFSYpTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYD 1048
Cdd:TIGR01271 1192 ggkyqlstvlvIENPHAQkcwpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS 1270
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1049 PlKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAGTIRENI-IYGGVSDKideaEIIEAAKAANAHDFITSLTEGYDT 1127
Cdd:TIGR01271 1271 T-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQWSDE----EIWKVAEEVGLKSVIEQFPDKLDF 1345
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1128 YCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLD 1207
Cdd:TIGR01271 1346 VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIE 1425
|
1050
....*....|....*.
gi 15229473 1208 KGKLVERGTHSSLLSK 1223
Cdd:TIGR01271 1426 GSSVKQYDSIQKLLNE 1441
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
378-591 |
1.25e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.53 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVsiDKLQVKWLRSQMGLVSQEPALFA-TTIKENIL 456
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLSHVPPYQRPINMMFQSYALFPhMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 457 FG-KED----ASMDD-VVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSPTILLLDEATSALDS 530
Cdd:PRK11607 114 FGlKQDklpkAEIASrVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 531 E-SERV---VQEALENasIGRTTILIAH-RLSTIRNADVISVVKNGHIVETGSHDELMENIDGQYS 591
Cdd:PRK11607 183 KlRDRMqleVVDILER--VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
715-955 |
1.42e-23 |
|
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: 102.18 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 715 YALSFVGL----AVLSFLinisQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVVRSLVG 790
Cdd:cd18576 38 IALLLLGLfllqAVFSFF----RIYLFARVGERVVADLRKDLYRHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 791 DRMA-LVVQTVSAVtIAFTMGLVIAWRLALVMIAVQPVIIVC--FYTRRvlLKSMSKKAIKAQDESSKLAAEAVSNVRTI 867
Cdd:cd18576 112 TTLAeFLRQILTLI-GGVVLLFFISWKLTLLMLATVPVVVLVavLFGRR--IRKLSKKVQDELAEANTIVEETLQGIRVV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 868 TAFSSQ----ERIMKMLEKAQESPRRESIRQSWFAGFglamSQSLTSCTWALDFWYGGRLIQDGYITAKALFeTFMILvs 943
Cdd:cd18576 189 KAFTREdyeiERYRKALERVVKLALKRARIRALFSSF----IIFLLFGAIVAVLWYGGRLVLAGELTAGDLV-AFLLY-- 261
|
250
....*....|..
gi 15229473 944 TGRVIADAGSMT 955
Cdd:cd18576 262 TLFIAGSIGSLA 273
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
359-577 |
1.52e-23 |
|
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: 99.96 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTvALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKlQVKWLRSQMG 438
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFAT-TIKE---------NILFGKEDASMDDVVEAAkasNAHNFISQLPNGYetqvgergvqmSGGQKQRIAI 508
Cdd:cd03264 76 YLPQEFGVYPNfTVREfldyiawlkGIPSKEVKARVDEVLELV---NLGDRAKKKIGSL-----------SGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1012-1225 |
1.69e-23 |
|
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: 108.46 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRdirsyhlrslrrhIALVSQEPTLFAGTIRENI 1091
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1092 IYGGVSDKIdeaEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE 1171
Cdd:TIGR01271 508 IFGLSYDEY---RYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1172 R-VVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGP 1225
Cdd:TIGR01271 585 KeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP 639
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
359-580 |
1.76e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDG------VSIDKLQVKW 432
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 433 LRSQMGLVSQE----PALfatTIKENILfgkeDASMDdVVEAAKASnAHNFISQLPNGYE-TQVGER-GVQMSGGQKQRI 506
Cdd:PRK11124 80 LRRNVGMVFQQynlwPHL---TVQQNLI----EAPCR-VLGLSKDQ-ALARAEKLLERLRlKPYADRfPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 507 AIARAIIKSPTILLLDEATSALDSE-SERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHD 580
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1017-1216 |
1.80e-23 |
|
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: 102.82 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1017 SIKIEEGKSTAIVGPSGSGKST----IIGLIERFYDpLKGIVKIDGRDIRSY---HLRSLR-RHIALVSQEPT-----LF 1083
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTlaraILGLLPPPGI-TSGEILFDGEDLLKLsekELRKIRgREIQMIFQDPMtslnpVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 agTIRENI-----IYGGVSDKideaeiieaakaaNAHDFITSLTE-----GYDTYCGDRGVQLSGGQKQRIAIARAVLKN 1153
Cdd:COG0444 104 --TVGDQIaeplrIHGGLSKA-------------EARERAIELLErvglpDPERRLDRYPHELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1154 PSVLLLDEATSALD--SQSE-----RVVQDALervmvgRTSVV-IAHRLSTI-QNCDAIAVLDKGKLVERGT 1216
Cdd:COG0444 169 PKLLIADEPTTALDvtIQAQilnllKDLQREL------GLAILfITHDLGVVaEIADRVAVMYAGRIVEEGP 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1008-1215 |
1.94e-23 |
|
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: 99.64 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyhLRSLRRHIALVSQEPTLFAG-T 1086
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAMVFQNYALYPHmT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1087 IRENIIYG----GVS-DKIDEAeiieaakaanahdfITSLTE--GYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:cd03301 89 VYDNIAFGlklrKVPkDEIDER--------------VREVAEllQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1160 DEATSALDSQSERVVQDALERVM--VGRTSVVIAH-RLSTIQNCDAIAVLDKGKLVERG 1215
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1009-1216 |
1.97e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAG-TI 1087
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIYG-----------GVSDkideaeiieaakaanaHDFITSLTE--GYDTYCGDRGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:PRK11231 94 RELVAYGrspwlslwgrlSAED----------------NARVNQAMEqtRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1155 SVLLLDEATSALD--SQSE-----RVVQDAlervmvGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGT 1216
Cdd:PRK11231 158 PVVLLDEPTTYLDinHQVElmrlmRELNTQ------GKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGT 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
359-587 |
2.55e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.36 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPS--RLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI----DKLQVKW 432
Cdd:PRK13649 3 INLQNVSYTYQAgtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 433 LRSQMGLVSQ--EPALFATTIKENILFGKED--ASMDDVVEAAKASNAHNFISqlpngyETQVGERGVQMSGGQKQRIAI 508
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALENA-SIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMENI 586
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQDV 236
|
.
gi 15229473 587 D 587
Cdd:PRK13649 237 D 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1012-1225 |
3.02e-23 |
|
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: 101.09 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRdirsyhlrslrrhIALVSQEPTLFAGTIRENI 1091
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1092 IYGgVSdkIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE 1171
Cdd:cd03291 119 IFG-VS--YDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1172 R-VVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGP 1225
Cdd:cd03291 196 KeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
362-554 |
3.62e-23 |
|
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: 98.87 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 362 KNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKlqvKWLRSQMGLVS 441
Cdd:cd03226 3 ENISFSYKK--GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 442 QEP--ALFATTIKENILFGKEDASMD--DVVEAAKASNAHNFISQLPngyetqvgergVQMSGGQKQRIAIARAIIKSPT 517
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 15229473 518 ILLLDEATSALDSESERVVQEA-LENASIGRTTILIAH 554
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELiRELAAQGKAVIVITH 184
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
359-622 |
3.93e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI--DKLQVKWLRSQ 436
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEP--ALFATTIKENILFG------KEDASMDDVVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAI 508
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIA-HRLSTI-RNADVISVVKNGHIVETG------SHD 580
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGtpkevfSDI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15229473 581 ELMENIDGQYSTLVHLQQIEKQDINVSVKIG-PISDPSKDIRN 622
Cdd:PRK13639 229 ETIRKANLRLPRVAHLIEILNKEDNLPIKMGyTIGEARRNIKE 271
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
995-1222 |
4.01e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.94 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEP--TLFAGTIRENIIYG----GVSDKIDEAEIIEAAKAANAHDFITSltegydtycgdRGVQLSGGQKQRIAIAR 1148
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGmenqGIPREEMIKRVDEALLAVNMLDFKTR-----------EPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1149 AVLKNPSVLLLDEATSALD----SQSERVVQDALERVMVgrTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
359-582 |
4.13e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEP--ALFATTIKENILFGKEDAS------MDDVVEAAKASNAHNFISQLPngyetqvgergVQMSGGQKQRIAIAR 510
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGipreemIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 511 AIIKSPTILLLDEATSALD----SESERVVQEALENASIgrTTILIAHRLSTIRNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1008-1212 |
4.22e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 97.11 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRH-IALVSQeptlfagt 1086
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1087 ireniiyggvsdkideaeiieaakaanahdfitsltegydtycgdrgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1167 dSQSERvvqDALERVMV-----GRTSVVIAHRLSTIQN-CDAIAVLDKGKLV 1212
Cdd:cd03216 114 -TPAEV---ERLFKVIRrlraqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
379-577 |
5.24e-23 |
|
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: 98.33 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 379 DFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQMGLVSQEPALFA-TTIKENILF 457
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 458 G-----KEDASMDDVVEAAKASNA-HNFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSE 531
Cdd:cd03298 94 GlspglKLTAEDRQAIEVALARVGlAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15229473 532 SERVVQEALEN--ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:cd03298 163 LRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
995-1221 |
5.27e-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: 99.77 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGI-VKIDGRDIRSYHLRSLRRHI 1073
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPTL-FAGTIR-ENIIYGGVSDKIDEAEIIEAAKAANAHDFITSLteGYDTYCGDRGVQLSGGQKQRIAIARAVL 1151
Cdd:COG1119 81 GLVSPALQLrFPRDETvLDVVLSGFFDSIGLYREPTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1152 KNPSVLLLDEATSALD-SQSERVVQdALERVMV--GRTSVVIAHRLSTIQNC-DAIAVLDKGKLVERGTHSSLL 1221
Cdd:COG1119 159 KDPELLILDEPTAGLDlGARELLLA-LLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1014-1222 |
6.04e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI---RSYHLRSLRRH-IALVSQEPTLFAG-TIR 1088
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKkIAMVFQSFALMPHmTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1089 ENIIYGgvsdkIDEAEIIEAAKAANAHDFITSLteGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDS 1168
Cdd:PRK10070 125 DNTAFG-----MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1169 QSERVVQDALERVMVG--RTSVVIAHRL-STIQNCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK10070 198 LIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
378-582 |
7.03e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.94 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDklqvkwLRS-----QMG--LVSQEPALFAT- 449
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR------FRSprdaqAAGiaIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDAS---MDDVVEAAKASNAhnfISQL-----PNgyeTQVGErgvqMSGGQKQRIAIARAIIKSPTILLL 521
Cdd:COG1129 95 SVAENIFLGREPRRgglIDWRAMRRRAREL---LARLgldidPD---TPVGD----LSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 522 DEATSAL-DSESER---VVQEaLenASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:COG1129 165 DEPTASLtEREVERlfrIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1012-1222 |
7.88e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.05 E-value: 7.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVK-----IDG-RDIRSYH--LRSLRRHIALVSQEPTLF 1083
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTaRSLSQQKglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AG-TIRENIIYGGVSDKideaEIIEAAKAANAHDFITS--LTEGYDTYcgdrGVQLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:PRK11264 98 PHrTVLENIIEGPVIVK----GEPKEEATARARELLAKvgLAGKETSY----PRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1161 EATSALDSQSERVV-----QDALERvmvgRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK11264 170 EPTSALDPELVGEVlntirQLAQEK----RTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
378-585 |
8.51e-23 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 98.66 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwLRSQMGLVS--QEPALFAT-TIKEN 454
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFG-----KEDASMDDVVEAAKASN--AHNFISQ--LPNGYETQVGErgvqMSGGQKQRIAIARAIIKSPTILLLDEAT 525
Cdd:cd03219 96 VMVAaqartGSGLLLARARREEREARerAEELLERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 526 SAL-DSESERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:cd03219 172 AGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-585 |
8.51e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.22 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 356 RGEVEFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYD-----PLAGEILIDGVSIDKLQV 430
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 431 KWLRSQMGLVSQEPALFAT-TIKENILFG-------KEDASMDDVVEAAKASnahnfiSQLPNGYETQVGERGVQMSGGQ 502
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNlSIFENVALGlklnrlvKSKKELQERVRWALEK------AQLWDEVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 503 KQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAH-RLSTIRNADVISVVKNGHIVETGSHDE 581
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....
gi 15229473 582 LMEN 585
Cdd:PRK14247 232 VFTN 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
359-585 |
9.07e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGE---ILIDGVSIDKLQVKWLRS 435
Cdd:PRK13640 6 VEFKHVSFTYPDS-KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEP--ALFATTIKENILFGKEDASmddVVEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAII 513
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRA---VPRPEMIKIVRDVLADV--GMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 514 KSPTILLLDEATSALDSESE----RVVQEALENASIgrTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKeqilKLIRKLKKKNNL--TVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1015-1215 |
9.38e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 9.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyHLRSLRRHIALVSQEPTLFAG-TIRENIIY 1093
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1094 GGVSDKIdeaeiieaakaanAHDFITSLTEGYDT------YCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK11607 115 GLKQDKL-------------PKAEIASRVNEMLGlvhmqeFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1168 SQ-SERV---VQDALERvmVGRTSVVIAH-RLSTIQNCDAIAVLDKGKLVERG 1215
Cdd:PRK11607 182 KKlRDRMqleVVDILER--VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1017-1222 |
1.38e-22 |
|
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: 97.50 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1017 SIKIEEGKSTAIVGPSGSGKST----IIGLIerfyDPLKGIVKIDGRDIRSY--HLRsLRRHIALVSQEPTLFAG-TIRE 1089
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTllktIMGLL----PPRSGSIRFDGRDITGLppHER-ARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NIIYGGVSDKIDeaeiieaakaanahDFITSLTEGYDTY------CGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:cd03224 95 NLLLGAYARRRA--------------KRKARLERVYELFprlkerRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1164 SALDSQSERVVQDALERVMVGRTSVVI----AHRLSTIqnCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
382-576 |
1.43e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 95.57 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGvsidklqvkwlrsqmglvsqepalfattikenilfgkED 461
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-------------------------------------KE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 462 ASMDDVVEAAKAsnahnfisqlpngyetqvgerGV----QMSGGQKQRIAIARAIIKSPTILLLDEATSAL-DSESERVV 536
Cdd:cd03216 64 VSFASPRDARRA---------------------GIamvyQLSVGERQMVEIARALARNARLLILDEPTAALtPAEVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15229473 537 QEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVET 576
Cdd:cd03216 123 KVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
358-580 |
1.61e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSID---KL---QVK 431
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPsekAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 432 WLRSQMGLVSQE----PALfatTIKENIL--------FGKEDAsMDDVVEAAKASNAHNFISQLPNgyetqvgergvQMS 499
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIeapckvlgLSKEQA-REKAMKLLARLRLTDKADRFPL-----------HLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 500 GGQKQRIAIARAIIKSPTILLLDEATSALDSE-SERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQG 223
|
...
gi 15229473 578 SHD 580
Cdd:COG4161 224 DAS 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1015-1216 |
1.74e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSY----HLRSLRRHIALVSQ--EPTLFAGTIR 1088
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQIRKKVGLVFQfpESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1089 ENIIYG----GVSDKideaeiieaAKAANAHDFITSLteGYDTYCGDRG-VQLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:PRK13649 105 KDVAFGpqnfGVSQE---------EAEALAREKLALV--GISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1164 SALDSQSERVVQDALERV-MVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
380-583 |
1.74e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 380 FCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGV-----SIDKLQVKWLrsqmglvSQEPALFA-TTIKE 453
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSRRPVSML-------FQENNLFShLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 454 NILFG-----KEDASMDDVVEA-AKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSPTILLLDEATSA 527
Cdd:PRK10771 91 NIGLGlnpglKLNAAQREKLHAiARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 528 LD----SESERVVQEALENASIgrTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELM 583
Cdd:PRK10771 160 LDpalrQEMLTLVSQVCQERQL--TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
377-587 |
1.82e-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: 100.56 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 377 FDDFCLRV----PSGKTVALVGGSGSGKSTVISL---LQRfydPLAGEILIDG-VSIDKLQVKWL---RSQMGLVSQEPA 445
Cdd:COG4148 11 RGGFTLDVdftlPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGeVLQDSARGIFLpphRRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 446 LFAT-TIKENILFG-------KEDASMDDVVEaakasnahnfisqlpngyetQVG-----ERGV-QMSGGQKQRIAIARA 511
Cdd:COG4148 88 LFPHlSVRGNLLYGrkrapraERRISFDEVVE--------------------LLGighllDRRPaTLSGGERQRVAIGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 512 IIKSPTILLLDEATSALDSES--------ERVVQEAlenasigRTTIL-IAHRLSTI-RNADVISVVKNGHIVETGSHDE 581
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARkaeilpylERLRDEL-------DIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAE 220
|
....*.
gi 15229473 582 LMENID 587
Cdd:COG4148 221 VLSRPD 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1026-1224 |
1.94e-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: 100.57 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1026 TAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRS----YHLRSLRRHIALVSQEPTLFAG-TIRENIIYGgvsdki 1100
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGNLRYG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1101 deAEIIEAAKAANAHDFITSLTeGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALER 1180
Cdd:TIGR02142 100 --MKRARPSERRISFERVIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLER 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15229473 1181 VM--VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLSKG 1224
Cdd:TIGR02142 177 LHaeFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
719-942 |
2.17e-22 |
|
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: 98.66 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 719 FVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRmalVVQ 798
Cdd:cd18551 42 LVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSG---LPQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 799 TVSAVTI---AFTMGLVIAWRLALVMIAVQPVIIVCFYtrrVLLKSMSKKAIKAQDESSKLAA---EAVSNVRTITAFSS 872
Cdd:cd18551 117 LVTGVLTvvgAVVLMFLLDWVLTLVTLAVVPLAFLIIL---PLGRRIRKASKRAQDALGELSAaleRALSAIRTVKASNA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 873 QERIMKMLEKAQESPRRESIRQS-WFAGFGLAMSQSLTSCTWALdFWYGGRLIQDGYITAKALFeTFMILV 942
Cdd:cd18551 194 EERETKRGGEAAERLYRAGLKAAkIEALIGPLMGLAVQLALLVV-LGVGGARVASGALTVGTLV-AFLLYL 262
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
994-1239 |
3.42e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTII----GLIERFYDPL--KGIV---KIDGRDIRSY 1064
Cdd:PRK13631 23 RVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnGLIKSKYGTIqvGDIYigdKKNNHELITN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1065 HL-------RSLRRHIALVSQEP--TLFAGTIRENIIYGGVSDKIDEAEIIEAakaanAHDFITSLTEGYDtYCGDRGVQ 1135
Cdd:PRK13631 103 PYskkiknfKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKL-----AKFYLNKMGLDDS-YLERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1136 LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSER-VVQDALERVMVGRTSVVIAHRLSTI-QNCDAIAVLDKGKLVE 1213
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILK 256
|
250 260
....*....|....*....|....*.
gi 15229473 1214 RGThssllskgPTGIYFSLVSLQTTS 1239
Cdd:PRK13631 257 TGT--------PYEIFTDQHIINSTS 274
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
999-1222 |
3.58e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDpLKGIVKIDGR------DI--RSYHLRSLR 1070
Cdd:PRK14258 12 NLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1071 RHIALVSQEPTLFAGTIRENIIYG----GVSDKIDEaeiieaakaanaHDFITSLTEGYDTY------CGDRGVQLSGGQ 1140
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGvkivGWRPKLEI------------DDIVESALKDADLWdeikhkIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1141 KQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALE--RVMVGRTSVVIAHRLSTIQNCDAIAVLDKG------KLV 1212
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLV 235
|
250
....*....|
gi 15229473 1213 ERGTHSSLLS 1222
Cdd:PRK14258 236 EFGLTKKIFN 245
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-585 |
3.97e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 352 LEKIRGEVEFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDpLAGEILIDG--------V 423
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 424 SIDKLQVKWLRSQMGLVSQEPALFATTIKENILFG------KEDASMDDVVEAAKASnahnfiSQLPNGYETQVGERGVQ 497
Cdd:PRK14258 77 YERRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 498 MSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGR--TTILIAHRLSTI-RNADVISVVKN---- 570
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQVsRLSDFTAFFKGnenr 230
|
250
....*....|....*.
gi 15229473 571 -GHIVETGSHDELMEN 585
Cdd:PRK14258 231 iGQLVEFGLTKKIFNS 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
994-1216 |
4.33e-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: 102.07 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYP------TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIerfydPLKGIVKIDGRDIRS 1063
Cdd:COG4172 277 EARDLKVWFPIKrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1064 YH---LRSLRRHIALVSQEPtlFAG-----TIRENIIYGGVSDKIDEAEIIEAAKAANAhdfitsLTE-GYDTYCGDRGV 1134
Cdd:COG4172 352 LSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGLRVHGPGLSAAERRARVAEA------LEEvGLDPAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1135 -QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDsqseRVVQ----DAL-----ERvmvGRTSVVIAHRLSTIQN-CDAI 1203
Cdd:COG4172 424 hEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqilDLLrdlqrEH---GLAYLFISHDLAVVRAlAHRV 496
|
250
....*....|...
gi 15229473 1204 AVLDKGKLVERGT 1216
Cdd:COG4172 497 MVMKDGKVVEQGP 509
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
357-587 |
4.62e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.77 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYPSR--LETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI----DKL-Q 429
Cdd:PRK13645 5 KDIILDNVSYTYAKKtpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 430 VKWLRSQMGLVSQEP--ALFATTIKENILFGKEDASmDDVVEAAKASNAHNFISQLPNGYetqVGERGVQMSGGQKQRIA 507
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 508 IARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELME 584
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErlNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240
|
...
gi 15229473 585 NID 587
Cdd:PRK13645 241 NQE 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1004-1234 |
4.65e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 103.71 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1004 YPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDgrdirsyhlrslrRHIALVSQEPTLF 1083
Cdd:PTZ00243 668 FELEPKVLL-RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AGTIRENIIYggvSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:PTZ00243 734 NATVRGNILF---FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1164 SALDSQ-SERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSkgpTGIYFSLVS 1234
Cdd:PTZ00243 811 SALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR---TSLYATLAA 879
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-582 |
5.25e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.04 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 363 NVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRF---YDP---LAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFA-TTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKS 515
Cdd:PRK14246 92 VGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 516 PTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
714-960 |
6.20e-22 |
|
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: 97.50 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 714 IYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRM 793
Cdd:cd18542 40 LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDK--ARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 794 ALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCFYtrrVLLKSMSKKAIKAQDESSKL---AAEAVSNVRTITAF 870
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSY---VFFKKVRPAFEEIREQEGELntvLQENLTGVRVVKAF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 871 SSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYITAKAL--FETFMILVS----- 943
Cdd:cd18542 195 AREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELvaFISYLWMLIwpvrq 274
|
250
....*....|....*..
gi 15229473 944 TGRVIADAGSMTTDLAK 960
Cdd:cd18542 275 LGRLINDMSRASASAER 291
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
994-1215 |
7.51e-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: 95.51 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrSYHLRSLRRHI 1073
Cdd:cd03266 3 TADALTKRFRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPTLFAG-TIRENIIYGGvsdkideaeIIEAAKAANAHDFITSLTE--GYDTYCGDRGVQLSGGQKQRIAIARAV 1150
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFA---------GLYGLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALERVM-VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
999-1206 |
7.54e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 7.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQ 1078
Cdd:PRK10247 12 NVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EPTLFAGTIRENII--YGGVSDKIDEAEIIEAAKAANAHDfiTSLTEGYDtycgdrgvQLSGGQKQRIAIARAVLKNPSV 1156
Cdd:PRK10247 89 TPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLERFALPD--TILTKNIA--------ELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1157 LLLDEATSALDSQSERVVQDALERVMVGRTSVVI--AHRLSTIQNCDAIAVL 1206
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITL 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1008-1209 |
7.94e-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: 95.48 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIV----KIDGRDIRSYHLRSLRRHIALVSQEPTLF 1083
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AGTIRENIIYGGVSDKideAEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:cd03290 92 NATVEENITFGSPFNK---QRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15229473 1164 SALDSQ-SERVVQDALERVMVG--RTSVVIAHRLSTIQNCDAIAVLDKG 1209
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
359-587 |
9.09e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.11 E-value: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYP--SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPL-----AGEILIDGVSIDKlQVK 431
Cdd:PRK13643 2 IKFEKVNYTYQpnSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTegkvtVGDIVVSSTSKQK-EIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 432 WLRSQMGLVSQEP--ALFATTIKENILFGKEDASMDDVVEAAKASNAHNFIsqlpnGYETQVGERG-VQMSGGQKQRIAI 508
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSpFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALENA-SIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMENI 586
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEV 235
|
.
gi 15229473 587 D 587
Cdd:PRK13643 236 D 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
995-1223 |
1.07e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIIfKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDP---LKGIVKIDGRDIRSYHLRSLRR 1071
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPAL-NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEP-TLFAG-TIRENIIYG----GVSDKIDEAEIIEAAKAANAHDFITSltegydtycgdRGVQLSGGQKQRIA 1145
Cdd:PRK13640 85 KVGIVFQNPdNQFVGaTVGDDVAFGlenrAVPRPEMIKIVRDVLADVGMLDYIDS-----------EPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1146 IARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
33-289 |
1.13e-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: 96.78 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 33 LLMGLGLIGAVGDGFTTplvllitsklmnnigGSSFNTDTFMqsisknsVALLYVACGSWVVCFLEGYCWTRTGERQTAR 112
Cdd:cd18575 13 LALGQGLRLLIDQGFAA---------------GNTALLNRAF-------LLLLAVALVLALASALRFYLVSWLGERVVAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 113 MREKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIVL 192
Cdd:cd18575 71 LRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 193 LVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIGSN-G 271
Cdd:cd18575 149 VVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALViF 228
|
250
....*....|....*...
gi 15229473 272 ITFAMWGFMSWYGSRMVM 289
Cdd:cd18575 229 LVFGAIVFVLWLGAHDVL 246
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
766-1224 |
1.41e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.98 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 766 RDENSSGAICSRLAKDANVVRslvgdRMALVVQTVSAVTIAFTMGLVIAWR-LALVMIAVQPVIIVCFYTRRVLLKSM-- 842
Cdd:PLN03232 392 RKNFASGKVTNMITTDANALQ-----QIAEQLHGLWSAPFRIIVSMVLLYQqLGVASLFGSLILFLLIPLQTLIVRKMrk 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 843 -SKKAIKAQDESSKLAAEAVSNVRTITAFSsqerimkmLEKAQESpRRESIRQ---SWF------AGFGLAMSQSL---- 908
Cdd:PLN03232 467 lTKEGLQWTDKRVGIINEILASMDTVKCYA--------WEKSFES-RIQGIRNeelSWFrkaqllSAFNSFILNSIpvvv 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 909 TSCTWALDFWYGGRLIQDGYITAKALFETFMILVST-GRVIADAGSMTTDLAKGSDAVGSVFAVLDRYTSIDPEDPdgye 987
Cdd:PLN03232 538 TLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMlPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAP---- 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 988 teritgQVEFLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIdgrdirsyhlr 1067
Cdd:PLN03232 614 ------AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV----------- 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1068 sLRRHIALVSQEPTLFAGTIRENIIYGgvSDKIDEAEIIEAAKAANAHDFitSLTEGYD-TYCGDRGVQLSGGQKQRIAI 1146
Cdd:PLN03232 677 -IRGSVAYVPQVSWIFNATVRENILFG--SDFESERYWRAIDVTALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSM 751
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1147 ARAVLKNPSVLLLDEATSALDSQSERVVQDA-LERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKG 1224
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG 830
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1002-1225 |
2.27e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 101.35 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1002 FSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLK-GIVKIDGRdirsyhlrslrrhIALVSQEP 1080
Cdd:PLN03130 622 FSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------VAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 TLFAGTIRENIIYGGVSDK------IDEAEIieaakaanAHDFitSLTEGYD-TYCGDRGVQLSGGQKQRIAIARAVLKN 1153
Cdd:PLN03130 689 WIFNATVRDNILFGSPFDPeryeraIDVTAL--------QHDL--DLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1154 PSVLLLDEATSALDSQSERVVQDA-LERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKGP 1225
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP 831
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
677-931 |
2.32e-21 |
|
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: 95.92 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 677 ISATLFGAIQPayaYSLGSMVSVYFLTSHDEIKEkTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKV 756
Cdd:cd18544 9 LLATALELLGP---LLIKRAIDDYIVPGQGDLQG-LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 757 LTFEVGWFDRdeNSSGAICSRLAKD--------ANVVRSLVGDrmalvvqTVSAVTIAFTMgLVIAWRLALVMIAVQPVI 828
Cdd:cd18544 85 QRLPLSFFDR--TPVGRLVTRVTNDtealnelfTSGLVTLIGD-------LLLLIGILIAM-FLLNWRLALISLLVLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 829 IVCFYtrrvLLKSMSKKAIkaQDESSKLA------AEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGL 902
Cdd:cd18544 155 LLATY----LFRKKSRKAY--REVREKLSrlnaflQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFR 228
|
250 260
....*....|....*....|....*....
gi 15229473 903 AMSQSLTSCTWALDFWYGGRLIQDGYITA 931
Cdd:cd18544 229 PLVELLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
358-587 |
2.83e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSR--LETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI----DKLQVK 431
Cdd:PRK13634 2 DITFQKVEHRYQYKtpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 432 WLRSQMGLVSQ--EPALFATTIKENILFGKEDASMDDVVEAAKASNAHNFIsqlpnGYETQVGERG-VQMSGGQKQRIAI 508
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELV-----GLPEELLARSpFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
..
gi 15229473 586 ID 587
Cdd:PRK13634 237 PD 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
999-1222 |
3.60e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.05 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSY-HLRSLRRHIALVS 1077
Cdd:PRK13644 6 NVSYSYPDGTPAL--ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1078 QEP-TLFAG-TIRENIIYG---------GVSDKIDEaeiieaakaanahdfitSLTE-GYDTYCGDRGVQLSGGQKQRIA 1145
Cdd:PRK13644 84 QNPeTQFVGrTVEEDLAFGpenlclppiEIRKRVDR-----------------ALAEiGLEKYRHRSPKTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1146 IARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM-VGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1009-1222 |
3.71e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.34 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGR------DIRSYHLRSLRRHIALVSQEPTL 1082
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1083 FAG-TIRENIIY----GGVSDKIDEAEIIEAAKAAnahdfITSLTEGYDTYcGDRGVQLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:PRK14246 102 FPHlSIYDNIAYplksHGIKEKREIKKIVEECLRK-----VGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1158 LLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
378-582 |
4.19e-21 |
|
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: 93.20 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKlQVKWLRSQMGLVSQEPALfattikENILF 457
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV------DDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 458 GKEDASMDDVVEAAKASNAHNFISQLPNGYE-TQVGERGVQ-MSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERV 535
Cdd:cd03265 90 GWENLYIHARLYGVPGAERRERIDELLDFVGlLEAADRLVKtYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15229473 536 VQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:cd03265 170 VWEYIEklKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
997-1224 |
5.54e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 997 FLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALV 1076
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1077 SQEPTL-FAGTIRENIIYG--------GVSDKIDEAEIIEAAKAANAHDFItsltegydtycgDRGV-QLSGGQKQRIAI 1146
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGrtphrsrfDTWTETDRAAVERAMERTGVAQFA------------DRPVtSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1147 ARAVLKNPSVLLLDEATSALD-SQSERVVQDALERVMVGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGTHSSLLSKG 1224
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1012-1216 |
5.87e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.68 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTL-FAGTIREn 1090
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 IIYGGVSDkideaeiieaAKAANAHDfiTSLTEGYDTYCG-----DRGV-QLSGGQKQRIAIARaVL-------KNPSVL 1157
Cdd:PRK13548 96 VVAMGRAP----------HGLSRAED--DALVAAALAQVDlahlaGRDYpQLSGGEQQRVQLAR-VLaqlwepdGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1158 LLDEATSALD-SQSERVVQDALERVMVGRTSV-VIAHRLS-TIQNCDAIAVLDKGKLVERGT 1216
Cdd:PRK13548 163 LLDEPTSALDlAHQHHVLRLARQLAHERGLAViVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1014-1215 |
5.99e-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: 92.28 E-value: 5.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyHLRSLRRHIALVSQEPTLFAG-TIRENII 1092
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALIEAPGFYPNlTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1093 YG----GVSDKIdeaeiieaakaanahdfITSLTE--GYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:cd03268 95 LLarllGIRKKR-----------------IDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1167 DSQSERVVQDALERVM-VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:cd03268 158 DPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
382-578 |
6.16e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLA-----GEILIDGVSIDKLQVK--WLRSQMGLVSQEPALFATTIKEN 454
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFGKE----DASMDDVVEAAKASNAhnfisqLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDS 530
Cdd:PRK14243 111 IAYGARingyKGDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229473 531 ESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGS 578
Cdd:PRK14243 185 ISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
359-582 |
6.32e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.94 E-value: 6.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQMG 438
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFA-TTIKENILFG-------KEDASmDDVVEAAKASNAHNFisqlpngyetqvGERGV-QMSGGQKQRIAIA 509
Cdd:PRK11432 82 MVFQSYALFPhMSLGENVGYGlkmlgvpKEERK-QRVKEALELVDLAGF------------EDRYVdQISGGQQQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 510 RAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRelQQQFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
989-1222 |
6.41e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 989 ERITGQVEFLDVDFSYPTRPDV---------IIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGI-----V 1054
Cdd:PRK14271 4 ERLGGQSGAADVDAAAPAMAAVnltlgfagkTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1055 KIDGRDIRSYH-LRSLRRHIALVSQEPTLFAGTIRENIIYGGVSDKIdeAEIIEAAKAANAHDFITSLTEGYDTYCGDRG 1133
Cdd:PRK14271 84 LLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL--VPRKEFRGVAQARLTEVGLWDAVKDRLSDSP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1134 VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLV 1212
Cdd:PRK14271 162 FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLV 241
|
250
....*....|
gi 15229473 1213 ERGTHSSLLS 1222
Cdd:PRK14271 242 EEGPTEQLFS 251
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
359-600 |
7.00e-21 |
|
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: 93.23 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAG---EIL---IDGVSIdklqvkW 432
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDV------W 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 433 -LRSQMGLVSqePALFA-----TTIKENILFGKEDaSMD--DVVEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQ 504
Cdd:COG1119 75 eLRKRIGLVS--PALQLrfprdETVLDVVLSGFFD-SIGlyREPTDEQRERARELLELL--GLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 505 RIAIARAIIKSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLSTIrnADVIS---VVKNGHIVETGSH 579
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEI--PPGIThvlLLKDGRVVAAGPK 227
|
250 260
....*....|....*....|...
gi 15229473 580 DELM--ENIDGQYSTLVHLQQIE 600
Cdd:COG1119 228 EEVLtsENLSEAFGLPVEVERRD 250
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1009-1215 |
7.50e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.44 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIG----LIERFYDP-LKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLF 1083
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AG-TIRENIIYGGVSDKIDEAEIIEAAKAANAHDfITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:PRK14247 95 PNlSIFENVALGLKLNRLVKSKKELQERVRWALE-KAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1163 TSALDSQSERVVQDALERVMVGRTSVVIAH------RLStiqncDAIAVLDKGKLVERG 1215
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
357-583 |
8.02e-21 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 93.77 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 357 GEVEFKNVKFVYpSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDpLAGEILIDGVSIDKLQVKWLRSQ 436
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEPALFATTIKENI-LFGKEdaSMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKS 515
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 516 PTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELM 583
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
995-1216 |
8.50e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 8.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSY-PTRP-DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIR----SYHLRS 1068
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1069 LRRHIALVSQ--EPTLFAGTIRENIIYG----GVSDKideaeiieaAKAANAHDFITSLteGYDTYCGDRG-VQLSGGQK 1141
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpknfGFSED---------EAKEKALKWLKKV--GLSEDLISKSpFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1142 QRIAIARAVLKNPSVLLLDEATSALDSQS-ERVVQDALERVMVGRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERGT 1216
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHAS 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1010-1213 |
9.67e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 92.50 E-value: 9.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1010 VIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLI---ERfydPLKGIVKIDGRDIRSY------HLRslRRHIALVSQE- 1079
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALdedaraRLR--ARHVGFVFQSf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1080 ---PTLfagTIRENII----YGGVSDKIDEaeiieaakaanAHDFITS--LTEGYDTYCGdrgvQLSGGQKQRIAIARAV 1150
Cdd:COG4181 100 qllPTL---TALENVMlpleLAGRRDARAR-----------ARALLERvgLGHRLDHYPA----QLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAHRLSTIQNCDAIAVLDKGKLVE 1213
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
345-556 |
1.19e-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: 99.21 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 345 DNPDGHKLEKIRGEVEFKNVKFVYPSRlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPlAGEILIDGVS 424
Cdd:TIGR01271 1204 ENPHAQKCWPSGGQMDVQGLTAKYTEA-GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVS 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 425 IDKLQVKWLRSQMGLVSQEPALFATTIKENiLFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQ 504
Cdd:TIGR01271 1282 WNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQ 1360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 505 RIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTILIAHRL 556
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
378-585 |
1.22e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 92.79 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVkWLRSQMGLVS--QEPALFAT-TIKEN 454
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFG--------------------KEDASMDDVVEAAkasnahnfISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIK 514
Cdd:COG0411 100 VLVAaharlgrgllaallrlprarREEREARERAEEL--------LERV--GLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 515 SPTILLLDEATSAL-DSESERVVQ--EALeNASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:COG0411 170 EPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRAD 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
386-585 |
1.34e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.26 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 386 SGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI---DKLQVKWLRSQMGLVSQEPalFAT--------TIKEN 454
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP--YGSlnprkkvgQILEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFGKEDASmddvvEAAKASNAHNFISQLpnGYETQVGERGVQM-SGGQKQRIAIARAIIKSPTILLLDEATSALD-SES 532
Cdd:PRK11308 118 PLLINTSLS-----AAERREKALAMMAKV--GLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQ 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 533 ERV------VQEALenasiGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK11308 191 AQVlnlmmdLQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
995-1224 |
1.35e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.55 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSY-PTRP-DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI----RSYHLRS 1068
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1069 LRRHIALVSQ--EPTLFAGTIRENIIYG----GVSDKideaeiieaAKAANAHDFI--TSLTEGYDtycgDRG-VQLSGG 1139
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpmnfGVSEE---------DAKQKAREMIelVGLPEELL----ARSpFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1140 QKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*...
gi 15229473 1217 HSSLLSKG 1224
Cdd:PRK13634 230 PREIFADP 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
359-607 |
1.38e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.13 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI-DKLQVKWLRSQM 437
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEP--ALFATTIKENILFGKEDASMDDVVEAAKASNAHNFIsqlpnGYETQVGERGVQMSGGQKQRIAIARAIIKS 515
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 516 PTILLLDEATSALDSESERVVQEALENA-SIGRTTILIAHRLSTIRNADVISVVKNGHIVETGSHDELMENIDGQY---- 590
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTlglt 234
|
250
....*....|....*....
gi 15229473 591 -STLVHL-QQIEKQDINVS 607
Cdd:PRK13644 235 pPSLIELaENLKMHGVVIP 253
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
378-577 |
1.73e-20 |
|
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: 91.28 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDG--VSIDKLQVkwlRSQMGLVSQEPALFA-TTIKEN 454
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdVVKEPAEA---RRRLGFVSDSTGLYDrLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 I-----LFGKEDASMDDVVEaakasnahNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALD 529
Cdd:cd03266 99 LeyfagLYGLKGDELTARLE--------ELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15229473 530 SESERVVQEALEN-ASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETG 577
Cdd:cd03266 169 VMATRALREFIRQlRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1001-1223 |
2.02e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.88 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1001 DFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEP 1080
Cdd:PRK13647 9 DLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 --TLFAGTIRENIIYGGVSDKIDEaeiieaakaanahDFITSLTE------GYDTYCGDRGVQLSGGQKQRIAIARAVLK 1152
Cdd:PRK13647 89 ddQVFSSTVWDDVAFGPVNMGLDK-------------DEVERRVEealkavRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1153 NPSVLLLDEATSALDSQSERVVQDALERV-MVGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
373-567 |
2.10e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.31 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIK 452
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 453 ENILFG--------KEDASMDDVVEAAkasnahnfisqLPngyETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:PRK10247 99 DNLIFPwqirnqqpDPAIFLDDLERFA-----------LP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15229473 525 TSALDSESERVVQEalenasigrttilIAHRLSTIRNADVISV 567
Cdd:PRK10247 165 TSALDESNKHNVNE-------------IIHRYVREQNIAVLWV 194
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1014-1216 |
2.30e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.15 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGiVKIDGRDIrsYHLRSL----------RRHIALVSQEPTLF 1083
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVT--FHGKNLyapdvdpvevRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AGTIRENIIYG----GVSDKIDEAEIIEAAKaanahdfiTSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:PRK14243 104 PKSIYDNIAYGarinGYKGDMDELVERSLRQ--------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1160 DEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
379-582 |
2.32e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 379 DFCLRvpSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwLRSQMG--LVSQEPALFAT-TIKENI 455
Cdd:PRK15439 31 DFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGiyLVPQEPLLFPNlSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 456 LFG--KEDASMDDVVEAAKASNAHNFISQLPNGYEtqVGERgvqmsggqkQRIAIARAIIKSPTILLLDEATSALD-SES 532
Cdd:PRK15439 108 LFGlpKRQASMQKMKQLLAALGCQLDLDSSAGSLE--VADR---------QIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 533 ERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
702-930 |
2.38e-20 |
|
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: 92.86 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 702 LTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKD 781
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 782 ANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCFYtrrVLLKSMSKKAIKAQDESSKLAA--- 858
Cdd:cd18541 107 LNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVY---RLGKKIHKRFRKVQEAFSDLSDrvq 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 859 EAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYIT 930
Cdd:cd18541 184 ESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTIT 255
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1014-1216 |
2.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI--RSYHLRSLRRHIALVSQEP--TLFAGTIRE 1089
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NIIYG----GVSD-KIDEAEIIEAAkaanahdfITSLTegYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:PRK13637 104 DIAFGpinlGLSEeEIENRVKRAMN--------IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1165 ALDSQSErvvQDALERVM-----VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:PRK13637 174 GLDPKGR---DEILNKIKelhkeYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
374-582 |
3.27e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 374 TSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQMGLVSQEPALFA-TTIK 452
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 453 ENILFG------KEDASMDDVveAAKASNAHNFI--SQLPNGYETqvgergvQMSGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:PRK10851 93 DNIAFGltvlprRERPNAAAI--KAKVTQLLEMVqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 525 TSALDSESERVVQEALEN--ASIGRTTILIAH-RLSTIRNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQlhEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
377-554 |
3.69e-20 |
|
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: 90.57 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 377 FDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEIL-------IDGVSIDKLQVKWLRSQ-MGLVSQ------ 442
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwVDLAQASPREILALRRRtIGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 443 ---------EPALfattikenilfgkeDASMDDvvEAAKASnAHNFISQLpngyetQVGERGVQM-----SGGQKQRIAI 508
Cdd:COG4778 107 rvsaldvvaEPLL--------------ERGVDR--EEARAR-ARELLARL------NLPERLWDLppatfSGGEQQRVNI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALENASIGRTTIL-IAH 554
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
378-577 |
3.74e-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: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWlrSQMGLVSQEPALFAT-TIKENI- 455
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPNlTARENLr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 456 ----LFGKEDASMDDVVEAAkasnahnfisqlpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSE 531
Cdd:cd03268 95 llarLLGIRKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229473 532 SERVVQEALEN-ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:cd03268 161 GIKELRELILSlRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-585 |
4.27e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 375 SIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAG-----EILIDGVSI-DKLQVKWLRSQMGLVSQEPALFA 448
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 449 TTIKENILFGKEDASMDDVVEAAKASNAHNFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSAL 528
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 529 DSESERVVQEALENASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
359-582 |
4.38e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLEtsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMG 438
Cdd:PRK13652 4 IETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEP--ALFATTIKENILFGKEDASMDDVVEAAKASNAHNFIsqlpnGYETQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 517 TILLLDEATSALDSESERVVQEALENASI--GRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
995-1224 |
4.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.72 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIA 1074
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEP-TLFAG-TIRENIIYG----GVSDKIDEAEIIEAAKAANAHDFITSltegydtycgdRGVQLSGGQKQRIAIAR 1148
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAFGlenkGIPHEEMKERVNEALELVGMQDFKER-----------EPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1149 AVLKNPSVLLLDEATSALDSQSE----RVVQDALERvmVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSKG 1224
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1012-1227 |
4.82e-20 |
|
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: 91.41 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrsYHL-----RSLRRHIALVSQE-PTLF-- 1083
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL--YQLdrkqrRAFRRDVQLVFQDsPSAVnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AGTIREnIIYGGVSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYcgdrGVQLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:TIGR02769 104 RMTVRQ-IIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKL----PRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1164 SALDSQSERVVQDALE--RVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLS-KGPTG 1227
Cdd:TIGR02769 179 SNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSfKHPAG 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
995-1218 |
4.87e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDG------RDIRSYHLRS 1068
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1069 LRRHIALVSQE----PTLfagTIRENIIYG-----GVSDKIdeaeiieaaKAANAHDFITSL--TEGYDTYcgdrGVQLS 1137
Cdd:COG4161 80 LRQKVGMVFQQynlwPHL---TVMENLIEApckvlGLSKEQ---------AREKAMKLLARLrlTDKADRF----PLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1138 GGQKQRIAIARAVLKNPSVLLLDEATSALDSQ-SERVVQDALERVMVGRTSVVIAHRLSTIQNCDA-IAVLDKGKLVERG 1215
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASqVVYMEKGRIIEQG 223
|
...
gi 15229473 1216 THS 1218
Cdd:COG4161 224 DAS 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1015-1216 |
4.93e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 91.25 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI--RSYHLRSlRRHIALVSQEPTLFAG-TIRENI 1091
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItgLPPHRIA-RLGIARTFQNPRLFPElTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1092 I--------YGGVSDKIDEAEIIEAAKAANAH-----DFItSLTEGYDTYCGDrgvqLSGGQKQRIAIARAVLKNPSVLL 1158
Cdd:COG0411 101 LvaaharlgRGLLAALLRLPRARREEREARERaeellERV-GLADRADEPAGN----LSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1159 LDEATSALDSQ-SERVVqDALERV--MVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:COG0411 176 LDEPAAGLNPEeTEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
376-529 |
5.98e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDP---LAGEILIDGVSIDKLQVkwLRSQMGLVSQEPALFA-TTI 451
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDLLFPhLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 452 KENILFG---------KEDASMDDVVEAAKASNAHNFISQLpngyetqvgergvqmSGGQKQRIAIARAIIKSPTILLLD 522
Cdd:COG4136 94 GENLAFAlpptigraqRRARVEQALEEAGLAGFADRDPATL---------------SGGQRARVALLRALLAEPRALLLD 158
|
....*..
gi 15229473 523 EATSALD 529
Cdd:COG4136 159 EPFSKLD 165
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
35-299 |
6.51e-20 |
|
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: 91.71 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 35 MGLGLIGAVGDGFTTPLVLLITSKLMNNIGgssfntdtfmqsISKNSVALLYVACGswVVC---------FLEGYCWTRT 105
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIF------------VEKDLEALLLVPLA--IIGlfllrglasYLQTYLMAYV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 106 GERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIV 185
Cdd:cd18552 67 GQRVVRDLRNDLFDKLLRLPLSFFDRN--SSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 186 GLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGI 265
Cdd:cd18552 145 ALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARAL 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15229473 266 ------TIGSNGITFAMwgfmsWYGSRMVMYHGAQGGTVF 299
Cdd:cd18552 225 ssplmeLLGAIAIALVL-----WYGGYQVISGELTPGEFI 259
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
359-613 |
6.70e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.22 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETSI--FDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILI-DGVSIDKLQV----- 430
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgDIYIGDKKNNhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 431 ----------KWLRSQMGLVSQEP--ALFATTIKENILFGKedasmddVVEAAKASNAHnfisQLPNGYETQVG------ 492
Cdd:PRK13631 102 npyskkiknfKELRRRVSMVFQFPeyQLFKDTIEKDIMFGP-------VALGVKKSEAK----KLAKFYLNKMGlddsyl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 493 ERG-VQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESER-VVQEALENASIGRTTILIAHRLSTIRN-ADVISVVK 569
Cdd:PRK13631 171 ERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMD 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15229473 570 NGHIVETGSHDELMENIDGQYSTLVHLQQIeKQDINVSVKIGPI 613
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQHIINSTSIQVPRV-IQVINDLIKKDPK 293
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
382-585 |
7.53e-20 |
|
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: 90.04 E-value: 7.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVkWLRSQMGL--VSQEPALFAT-TIKENILFG 458
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFPSlTVEENLLLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 459 ----KEDASMDDVVEAAkasnahnfisqlpngYET--QVGER----GVQMSGGQKQRIAIARAIIKSPTILLLDEATSAL 528
Cdd:COG0410 103 ayarRDRAEVRADLERV---------------YELfpRLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 529 dseSERVVQEALEnaSIGR-----TTILI----AHRLSTIrnADVISVVKNGHIVETGSHDELMEN 585
Cdd:COG0410 168 ---APLIVEEIFE--IIRRlnregVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLAD 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
359-586 |
8.40e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKlQVKWLRSQMG 438
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPAL-FATTIKENIL-FGKEDASMDDVVEAAKASNAHnfISQLPNGYETQVGErgvqMSGGQKQRIAIARAIIKSP 516
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLvFGRYFGMSTREIEAVIPSLLE--FARLESKADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 517 TILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTI-RNADVISVVKNGH-IVETGSHDELMENI 586
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRkIAEGRPHALIDEHI 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-585 |
8.91e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.29 E-value: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYD-----PLAGEILIDGVSI-----DKLQVkwlRSQMGLVSQEPALFA-TT 450
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIyspdvDPIEV---RREVGMVFQYPNPFPhLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 451 IKENILFG-------KEDASMDDVVEAAKASNAhnfisqLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDE 523
Cdd:PRK14267 102 IYDNVAIGvklnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 524 ATSALDSESERVVQEALENASIGRTTILIAHR-LSTIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
376-576 |
1.04e-19 |
|
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: 90.25 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRSQMGLVSQE-PALF--AT 449
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVnpRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENIlfGKEDASMDDVVEAAKASNAHNFISQLpnGYETQVGER-GVQMSGGQKQRIAIARAIIKSPTILLLDEATSAL 528
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKARIAELLDMV--GLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 529 DSESERVVQEALE--NASIGRTTILIAHRLSTI-RNADVISVVKNGHIVET 576
Cdd:TIGR02769 182 DMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
359-577 |
1.11e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 88.88 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPsrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQvkwlRSQMG 438
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALF-ATTIKENILF-------GKEDA--SMDDVVEAAKASNahnfisqlpngYETQVGErgvQMSGGQKQRIAI 508
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlaqlkglKKEEArrRIDEWLERLELSE-----------YANKRVE---ELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEAL-ENASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETG 577
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
373-585 |
1.16e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.03 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI-------------DKLQVKWLRSQMGL 439
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQEPALFA-TTIKENILfgkeDASMDdVVEAAKASNAHNFISQLPN-GY-ETQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:PRK10619 97 VFQHFNLWShMTVLENVM----EAPIQ-VLGLSKQEARERAVKYLAKvGIdERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 517 TILLLDEATSALD----SESERVVQEALENasiGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK10619 172 EVLLFDEPTSALDpelvGEVLRIMQQLAEE---GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
995-1222 |
1.26e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.52 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrSYHLRSL---RR 1071
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEP--TLFAGTIRENIIYGGVSDKIDEAEIIEaakaaNAHDFITSLT-EGYDTYCGDrgvQLSGGQKQRIAIAR 1148
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEK-----RVKEALKAVGmEGFENKPPH---HLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1149 AVLKNPSVLLLDEATSALD----SQSERVVQDALERvmvGRTSVVIAHRLSTIQ-NCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKE---GITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
373-573 |
1.43e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLqvkwlRSQMGLVSQEPALFA-TTI 451
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 452 KENILFGKEDASMDDVVEAAKASnahnfisqlpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSE 531
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15229473 532 SERVVQEALEN--ASIGRTTILIAHRLS-TIRNADVISVVKNGHI 573
Cdd:PRK11247 168 TRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1015-1219 |
1.63e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDG------RDIRSYHLRSLRRHIALVSQEPTLFAG-TI 1087
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPHlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIYG-----GVSDKIdeaeiieaaKAANAHDFITSL--TEGYDTYcgdrGVQLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:PRK11124 100 QQNLIEApcrvlGLSKDQ---------ALARAEKLLERLrlKPYADRF----PLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1161 EATSALDSQ-SERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAV-LDKGKLVERGTHSS 1219
Cdd:PRK11124 167 EPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVyMENGHIVEQGDASC 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1001-1216 |
2.00e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1001 DFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEP 1080
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 --TLFAGTIRENIIYGGVSDKIDEAEIieaakaanAHDFITSL-TEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:PRK13652 88 ddQIFSPTVEQDIAFGPINLGLDEETV--------AHRVSSALhMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1158 LLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERGT 1216
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGT 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
370-577 |
2.37e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.83 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 370 SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPAL-FA 448
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 449 TTIKENI---------LFGKEDASMDDVVEAAkasnahnfisqLPNGYETQVGERGV-QMSGGQKQRIAIARAIIKSPTI 518
Cdd:PRK09536 92 FDVRQVVemgrtphrsRFDTWTETDRAAVERA-----------MERTGVAQFADRPVtSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 519 LLLDEATSALDSESE-RVVQEALENASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETG 577
Cdd:PRK09536 161 LLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
993-1223 |
3.17e-19 |
|
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: 89.14 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 993 GQVEFLDVDFSYpTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDpLKGIVKIDGRDIRSYHLRSLRRH 1072
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEPTLFAGTIRENI-IYGGVSDKideaEIIEAAKAANAHDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVL 1151
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWSDE----EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1152 KNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1015-1220 |
5.24e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyhlRSLR-RHIALVSQEPTLFAG-TIRENII 1092
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQqRDICMVFQSYALFPHmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1093 YG----GVSdkideaEIIEAAKAANAHDFITslTEGYdtycGDRGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK11432 101 YGlkmlGVP------KEERKQRVKEALELVD--LAGF----EDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1168 SQSERVVQDALERVM--VGRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGTHSSL 1220
Cdd:PRK11432 169 ANLRRSMREKIRELQqqFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
359-587 |
5.42e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.28 E-value: 5.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFvypSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWL---RS 435
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 QMGLVSQEPALFA-TTIKENILFGKEDasmddvveaakasnaHnfiSQLPNG--YET------QVGERGV------QMSG 500
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPLRE---------------H---TQLPAPllHSTvmmkleAVGLRGAaklmpsELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 501 GQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISelNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHG 226
|
250
....*....|
gi 15229473 578 SHDELMENID 587
Cdd:PRK11831 227 SAQALQANPD 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1014-1216 |
5.91e-19 |
|
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: 87.04 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyHLRSLRRHIALVSQEPTLFAG-TIRENI- 1091
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1092 ----IYGGVSDKIDEAEIIEAakaanahDFItSLTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:cd03265 96 iharLYGVPGAERRERIDELL-------DFV-GLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1168 SQSERVVQDALERvMVGRTSVVI---AHRLSTI-QNCDAIAVLDKGKLVERGT 1216
Cdd:cd03265 164 PQTRAHVWEYIEK-LKEEFGMTIlltTHYMEEAeQLCDRVAIIDHGRIIAEGT 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
360-554 |
6.36e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.00 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRLE-TSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSI-----DKlqvkwl 433
Cdd:COG4525 5 TVRHVSVRYPGGGQpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgaDR------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 434 rsqmGLVSQEPALFA-TTIKENILFGKEDASMDdvvEAAKASNAHNFISQLpnGYEtQVGERGV-QMSGGQKQRIAIARA 511
Cdd:COG4525 79 ----GVVFQKDALLPwLNVLDNVAFGLRLRGVP---KAERRARAEELLALV--GLA-DFARRRIwQLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15229473 512 IIKSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAH 554
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
373-583 |
7.49e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPalfatTIK 452
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHH-----LTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 453 ENI---------------LFGKEDASMDDVVEAAKAsnahnfisqlpngyETQVGE----RGVQMSGGQKQRIAIARAII 513
Cdd:PRK11231 89 EGItvrelvaygrspwlsLWGRLSAEDNARVNQAME--------------QTRINHladrRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 514 KSPTILLLDEATSALD----SESERVVQEaLENAsiGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELM 583
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDinhqVELMRLMRE-LNTQ--GKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1012-1222 |
7.80e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 87.72 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIR-------------SYHLRSLRRHIALVSQ 1078
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EPTLFAG-TIRENIIYGgvsdKIDEAEIIEAAKAANAHDFITSLteGYDTYCGDR-GVQLSGGQKQRIAIARAVLKNPSV 1156
Cdd:PRK10619 100 HFNLWSHmTVLENVMEA----PIQVLGLSKQEARERAVKYLAKV--GIDERAQGKyPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1157 LLLDEATSALD----SQSERVVQDALERvmvGRTSVVIAHRLSTIQNCDA-IAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK10619 174 LLFDEPTSALDpelvGEVLRIMQQLAEE---GKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
359-582 |
7.90e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSID--KLQVKWLRSQ 436
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 MGLVSQEP--ALFATTIKENILFGKEDASM--DDVVEAAKASNAHNFISQLPNGyETQVgergvqMSGGQKQRIAIARAI 512
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-PTHC------LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 513 IKSPTILLLDEATSALD----SESERVVQEALENASIgrtTILIA-HRLSTIR-NADVISVVKNGHIVETGSHDEL 582
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGL---TIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
378-585 |
8.30e-19 |
|
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: 91.67 E-value: 8.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKS-TVISLLQRFYDPLA---GEILIDGVSIDKLQVKWLR----SQMGLVSQEP--ALf 447
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLGLSERELRrirgNRIAMIFQEPmtSL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 448 attikeNILF--GKEdasmddVVEA--------AKASNAHnfISQLPNgyetQVG----ERGV-----QMSGGQKQRIAI 508
Cdd:COG4172 106 ------NPLHtiGKQ------IAEVlrlhrglsGAAARAR--ALELLE----RVGipdpERRLdayphQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 509 ARAIIKSPTILLLDEATSALDseserV-VQ-EALE-----NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHD 580
Cdd:COG4172 168 AMALANEPDLLIADEPTTALD-----VtVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTA 242
|
....*
gi 15229473 581 ELMEN 585
Cdd:COG4172 243 ELFAA 247
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1002-1215 |
8.45e-19 |
|
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: 86.82 E-value: 8.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1002 FSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRdirsyhLRSLrrhIAL-VSQEP 1080
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSL---LGLgGGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 TLfagTIRENIIYG----GVSDK-IDEAEiieaakaanahDFITSLTEGYDtyCGDRGV-QLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03220 98 EL---TGRENIYLNgrllGLSRKeIDEKI-----------DEIIEFSELGD--FIDLPVkTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1155 SVLLLDEATSALDSQSERVVQDAL-ERVMVGRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERG 1215
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
360-574 |
8.57e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.09 E-value: 8.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSRLET-SIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWL----R 434
Cdd:PRK10535 6 ELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 435 SQMGLVSQEPALFA-TTIKENIlfgKEDASMDDVVEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAII 513
Cdd:PRK10535 86 EHFGFIFQRYHLLShLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 514 KSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIRNADVISVVKNGHIV 574
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1016-1167 |
9.46e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.56 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1016 FSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDirsyHLRS--LRRHIALVSQEPTLFAG-TIRENII 1092
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTppSRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1093 YG---GVsdKIDEAEIIEAAKAANA---HDFITSLTEgydtycgdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:PRK10771 94 LGlnpGL--KLNAAQREKLHAIARQmgiEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
.
gi 15229473 1167 D 1167
Cdd:PRK10771 161 D 161
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1006-1167 |
9.76e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.00 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1006 TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDP---LKGIVKIDGRDIRsyHLRSLRRHIALVSQEPTL 1082
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT--ALPAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1083 FAG-TIRENIIYG---GVSdkideaeiieaakAANAHDFI-TSLTEGYDTYCGDRGV-QLSGGQKQRIAIARAVLKNPSV 1156
Cdd:COG4136 88 FPHlSVGENLAFAlppTIG-------------RAQRRARVeQALEEAGLAGFADRDPaTLSGGQRARVALLRALLAEPRA 154
|
170
....*....|.
gi 15229473 1157 LLLDEATSALD 1167
Cdd:COG4136 155 LLLDEPFSKLD 165
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
995-1223 |
9.90e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.98 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGR--DIRSYHLRSLRRH 1072
Cdd:PRK13636 6 LKVEELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1073 IALVSQEP--TLFAGTIRENIIYGGVSDKIDEAEIIEAAKAANAHDFITSLTEGyDTYCgdrgvqLSGGQKQRIAIARAV 1150
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-PTHC------LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1151 LKNPSVLLLDEATSALD----SQSERVVQDALERvmVGRTSVVIAHRLSTIQ-NCDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
32-260 |
1.12e-18 |
|
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: 87.87 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 32 WLLMGLGLIGAVGdGFTTPLVlliTSKLMNNIGGSSFNTDTFmqsisknsVALLYVACGSWVVCFLEGYCWTRTGERQTA 111
Cdd:cd18551 2 ILALLLSLLGTAA-SLAQPLL---VKNLIDALSAGGSSGGLL--------ALLVALFLLQAVLSALSSYLLGRTGERVVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIV---GLP 188
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRR--RSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVtlaVVP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 189 FIVLLVIPglmYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQG 260
Cdd:cd18551 148 LAFLIILP---LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAA 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
358-587 |
1.50e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.83 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSRLETSI--FDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEI----------------- 418
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 419 -LIDGVSIDKL------QVKWLRSQMGLVSQ--EPALFATTIKENILFGKedASMDDVVEAAKaSNAHNFISQ--LPNGY 487
Cdd:PRK13651 82 kVLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGP--VSMGVSKEEAK-KRAAKYIELvgLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 488 etqVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENA-SIGRTTILIAHRLSTI--RNADV 564
Cdd:PRK13651 159 ---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRT 235
|
250 260
....*....|....*....|...
gi 15229473 565 IsVVKNGHIVETGSHDELMENID 587
Cdd:PRK13651 236 I-FFKDGKIIKDGDTYDILSDNK 257
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1009-1222 |
2.36e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 85.80 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIerfyDPLKGIVKIDGRDI--RSYHLRSlRRHIALVSQEPTL 1082
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLL----PPRSGSIRFDGEDItgLPPHRIA-RLGIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1083 FAG-TIRENIIYGGvsdkideaeiieaAKAANAHDFITSLTEGYDTY------CGDRGVQLSGGQKQRIAIARAVLKNPS 1155
Cdd:COG0410 90 FPSlTVEENLLLGA-------------YARRDRAEVRADLERVYELFprlkerRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1156 VLLLDEATSALdsqSERVVQ---DALERVMVGRTSVVI----AHRLSTIqnCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:COG0410 157 LLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
373-585 |
2.44e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 85.65 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWL-RSQMGLVSQEPALFAT-T 450
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 451 IKENILFGkedasmddvVEAAKASNAH--NFISQLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSAL 528
Cdd:TIGR03410 92 VEENLLTG---------LAALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 529 D----SESERVVQEAleNASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:TIGR03410 163 QpsiiKDIGRVIRRL--RAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDED 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1012-1216 |
2.58e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.22 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSlrRHIALVSQEPTLFAG-TIREN 1090
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 IIYG---------GVSDKIDEAEIIEAAKAANAHdfitsLTEGYDTycgdrgvQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:PRK10851 95 IAFGltvlprrerPNAAAIKAKVTQLLEMVQLAH-----LADRYPA-------QLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1162 ATSALDSQservVQDALERVM------VGRTSVVIAH-RLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:PRK10851 163 PFGALDAQ----VRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1018-1216 |
3.34e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.83 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1018 IKIEEGKSTAIVGPSGSGKSTII----GLI------ERFYDPLKGIVKIDGRDIRSyhLRSLRRHIALVSQEPTLFAG-T 1086
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLrhlsGLItgdksaGSHIELLGRTVQREGRLARD--IRKSRANTGYIFQQFNLVNRlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1087 IRENIIYGGVSDKIDEAEIIEAAKAANAHDFITSLTE-GYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PRK09984 103 VLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1166 LDSQSERVVQDALERVMV--GRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGT 1216
Cdd:PRK09984 183 LDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1001-1193 |
3.40e-18 |
|
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: 82.97 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1001 DFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRdirsyhlrslrRHIALVSQEP 1080
Cdd:cd03223 5 NLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 TLFAGTIRENIIYggVSDKIdeaeiieaakaanahdfitsltegydtycgdrgvqLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:cd03223 74 YLPLGTLREQLIY--PWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|...
gi 15229473 1161 EATSALDSQSERVVQDALERVMVgrTSVVIAHR 1193
Cdd:cd03223 117 EATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
349-582 |
3.91e-18 |
|
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: 86.06 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 349 GHKLEKIRGEV-------EFKNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILID 421
Cdd:cd03291 18 GELLEKAKQENndrkhssDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 422 GVSIDKLQVKWLrsqmglvsqepalFATTIKENILFGkedASMDDV--VEAAKASNAHNFISQLPNGYETQVGERGVQMS 499
Cdd:cd03291 98 GRISFSSQFSWI-------------MPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 500 GGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEA-LENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETGS 578
Cdd:cd03291 162 GGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241
|
....
gi 15229473 579 HDEL 582
Cdd:cd03291 242 FSEL 245
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
376-555 |
3.98e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKST---VISLLQRFYD-----PLAGEILidgvsidklqvkwlrsqmgLVSQEPALF 447
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTllrAIAGLWPYGSgriarPAGARVL-------------------FLPQRPYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 448 ATTIKENILFGKEDASMDD--VVEAAKASNAHNFISQLpngyeTQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEAT 525
Cdd:COG4178 439 LGTLREALLYPATAEAFSDaeLREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|
gi 15229473 526 SALDSESERVVQEALENASIGRTTILIAHR 555
Cdd:COG4178 514 SALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
720-934 |
4.51e-18 |
|
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: 86.00 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 720 VGLAVLSFLinisQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQT 799
Cdd:cd18575 47 LVLALASAL----RFYLVSWLGERVVADLRKAVFAHLLRLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSSLSIALRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 800 VSAVTIAFTMGLVIAWRLALVMIAVQPVIIV--CFYTRRVllKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIM 877
Cdd:cd18575 121 LLLLIGGLVMLFITSPKLTLLVLLVIPLVVLpiILFGRRV--RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAER 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 878 KMLEKAQESPRRESIR----QSWFagFGLAMSQSLTSCTWALdfWYGGRLIQDGYITAKAL 934
Cdd:cd18575 199 QRFATAVEAAFAAALRriraRALL--TALVIFLVFGAIVFVL--WLGAHDVLAGRMSAGEL 255
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
991-1212 |
4.62e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.78 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 991 ITGQVEFLDVDFSYPT-RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYH---L 1066
Cdd:PRK10535 1 MTALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1067 RSLRR-HIALVSQEPTLFAG-TIRENI----IYGGVSDKideaeiieaAKAANAHDFITSLteGYDTYCGDRGVQLSGGQ 1140
Cdd:PRK10535 81 AQLRReHFGFIFQRYHLLSHlTAAQNVevpaVYAGLERK---------QRLLRAQELLQRL--GLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1141 KQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM-VGRTSVVIAHRLSTIQNCDAIAVLDKGKLV 1212
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-556 |
4.74e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVK--FVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVkWLRSQ 436
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 M-GLVSQEPAL---FATTIKENIL------------FGKEDASMDDVVEAakasnahnfISQLPNGYE----TQVGergv 496
Cdd:COG1101 81 YiGRVFQDPMMgtaPSMTIEENLAlayrrgkrrglrRGLTKKRRELFREL---------LATLGLGLEnrldTKVG---- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 497 QMSGGQKQRIAIARAIIKSPTILLLDEATSALD---SE-----SERVVQEAlenasiGRTTILIAHRL 556
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAAlvlelTEKIVEEN------NLTTLMVTHNM 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
376-585 |
4.93e-18 |
|
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: 84.52 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwLRSQMGL--VSQEPALFAT-TIK 452
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLGIgyLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 453 ENILFGKEDASMDDvveAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALD--- 529
Cdd:cd03218 94 ENILAVLEIRGLSK---KEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpia 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 530 -SESERVVQEaLENASIGrttILIA-HRLS-TIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:cd03218 169 vQDIQKIIKI-LKDRGIG---VLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1014-1192 |
6.08e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 84.44 E-value: 6.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLrrhiaLVSQEPTLFAG-TIRENIi 1092
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1093 YGGVSDKIDEAEIIEAAKAANAHDFITSLTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSER 1172
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|..
gi 15229473 1173 VVQDALERVM--VGRTSVVIAH 1192
Cdd:TIGR01184 152 NLQEELMQIWeeHRVTVLMVTH 173
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
359-584 |
7.25e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.01 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKlQVKWLRSQMG 438
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQ----EPALfatTIKENIL-----FGKEDASMDDVV----EAAKasnahnfisqLPNGYETQVGErgvqMSGGQKQR 505
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgryFGLSAAAARALVppllEFAK----------LENKADAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 506 IAIARAIIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELM 583
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
.
gi 15229473 584 E 584
Cdd:PRK13537 227 E 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
379-580 |
1.15e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.39 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 379 DFCLRvpSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRSQMGLVSQEPALFAT-TIKEN 454
Cdd:PRK10908 22 TFHMR--PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDHHLLMDrTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 -----ILFGkedASMDDVVEAAKAS--------NAHNFisqlpngyetqvgerGVQMSGGQKQRIAIARAIIKSPTILLL 521
Cdd:PRK10908 100 vaiplIIAG---ASGDDIRRRVSAAldkvglldKAKNF---------------PIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 522 DEATSALDSE-SERVVQEALENASIGRTTILIAHRLSTI--RNADVISvVKNGHIveTGSHD 580
Cdd:PRK10908 162 DEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsrRSYRMLT-LSDGHL--HGGVG 220
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
714-930 |
1.28e-17 |
|
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: 84.83 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 714 IYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLV-GDR 792
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDS--RPVGKILSRVINDVNSLSDLLsNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 793 MALVVQTVSAVTIAFTMgLVIAWRLALVMIAVQPVIIVcfyTRRVLLKSMSKKAIKAQDESSKLAA---EAVSNVRTITA 869
Cdd:cd18545 119 INLIPDLLTLVGIVIIM-FSLNVRLALVTLAVLPLLVL---VVFLLRRRARKAWQRVRKKISNLNAylhESISGIRVIQS 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 870 FSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYIT 930
Cdd:cd18545 195 FAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAIT 255
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
376-576 |
1.35e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.35 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRSQMGLVSQ---------- 442
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQdsisavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 443 -------EPALFATTIKEnilfGKEDASMDDVVEAAKASNAHnfISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKS 515
Cdd:PRK10419 107 tvreiirEPLRHLLSLDK----AERLARASEMLRAVDLDDSV--LDKRPP-----------QLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 516 PTILLLDEATSALDseseRVVQ-------EALENASiGRTTILIAHRLSTI-RNADVISVVKNGHIVET 576
Cdd:PRK10419 170 PKLLILDEAVSNLD----LVLQagvirllKKLQQQF-GTACLFITHDLRLVeRFCQRVMVMDNGQIVET 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
378-585 |
2.21e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.76 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL-QVKWL--RSQMGLVSQEP-------ALF 447
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkDDEWRavRSDIQMIFQDPlaslnprMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 448 ATTIKENILFGKEDASMDDVVEAAKASNAH-----NFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSPTILLLD 522
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 523 EATSALD-SESERVVQ--EALEnASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK15079 187 EPVSALDvSIQAQVVNllQQLQ-REMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
716-962 |
2.41e-17 |
|
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: 84.49 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 716 ALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDrmAL 795
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRLTGDVGAIQDLLVS--GV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 796 VVQTVSAVTIAFTMG--LVIAWRLALVMIAVQPV--IIVCFYTRRVllKSMSKKAIKAQDESSKLAAEAVSNVRTITAFS 871
Cdd:cd18564 133 LPLLTNLLTLVGMLGvmFWLDWQLALIALAVAPLllLAARRFSRRI--KEASREQRRREGALASVAQESLSAIRVVQAFG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 872 SQERIMKMLEKAQESPRRESIRQS-WFAGFGLAMSQSLTSCTwALDFWYGGRLIQDGYITAKAL--FETFmiLVSTGRVI 948
Cdd:cd18564 211 REEHEERRFARENRKSLRAGLRAArLQALLSPVVDVLVAVGT-ALVLWFGAWLVLAGRLTPGDLlvFLAY--LKNLYKPV 287
|
250
....*....|....
gi 15229473 949 ADAGSMTTDLAKGS 962
Cdd:cd18564 288 RDLAKLTGRIAKAS 301
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
999-1168 |
2.43e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.37 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYP-TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyhlRSLRRhiALVS 1077
Cdd:COG4525 8 HVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG---PGADR--GVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1078 QEPTLFAG-TIRENIIYG----GVSdKIDEAEIieaakaanAHDFITSLteGYDTYCGDRGVQLSGGQKQRIAIARAVLK 1152
Cdd:COG4525 83 QKDALLPWlNVLDNVAFGlrlrGVP-KAERRAR--------AEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170
....*....|....*.
gi 15229473 1153 NPSVLLLDEATSALDS 1168
Cdd:COG4525 152 DPRFLLMDEPFGALDA 167
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1012-1220 |
3.91e-17 |
|
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: 81.80 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIerfyDPLKGIVKIDGRDI--RSYHLRSlRRHIALVSQEPTLFAG 1085
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLL----PVKSGSIRLDGEDItkLPPHERA-RAGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 -TIRENIIYG-----GVSDKIDeaeiieaakaanahDFITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:TIGR03410 90 lTVEENLLTGlaalpRRSRKIP--------------DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1160 DEATSALDSQserVVQDaLERV------MVGRTSVVIAHRLSTIQNC-DAIAVLDKGKLVERGTHSSL 1220
Cdd:TIGR03410 156 DEPTEGIQPS---IIKD-IGRVirrlraEGGMAILLVEQYLDFARELaDRYYVMERGRVVASGAGDEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1009-1215 |
3.91e-17 |
|
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: 81.56 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHlrslRRHIALVSQEPTLFAG-TI 1087
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPKmKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIY----GGVSDKideaeiieaakaaNAHDFITSLTEGYD--TYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:cd03269 88 IDQLVYlaqlKGLKKE-------------EARRRIDEWLERLElsEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1162 ATSALDSQSERVVQDAL-ERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:cd03269 155 PFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1007-1212 |
4.13e-17 |
|
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: 81.93 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1007 RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLK---GIVKIDGRDIRSYhlrSLRRHIALVSQEPTLF 1083
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPD---QFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AG-TIRENIIY-----------GGVSDKIDEaeiieaakaanahdfITSLTEGYDTYCGDRGVQ-LSGGQKQRIAIARAV 1150
Cdd:cd03234 94 PGlTVRETLTYtailrlprkssDAIRKKRVE---------------DVLLRDLALTRIGGNLVKgISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALERVMV-GRTSVVIAH--RLSTIQNCDAIAVLDKGKLV 1212
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1012-1215 |
6.44e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.81 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYD-----PLKGIVKIDGRDIRSYHLRSL--RRHIALVSQEPTLFA 1084
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1085 G-TIRENIIYGGVSDKIDEAEIIEAAKAANAHDfITSLTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:PRK14267 99 HlTIYDNVAIGVKLNGLVKSKKELDERVEWALK-KAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1164 SALDSQSERVVQDALERVMVGRTSVVIAH------RLStiqncDAIAVLDKGKLVERG 1215
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRVS-----DYVAFLYLGKLIEVG 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
995-1217 |
7.15e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPtrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyHLRSLRRHIA 1074
Cdd:PRK13536 42 IDLAGVSKSYG---DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQEPTL-FAGTIRENII----YGGVSDKideaeiieaakaaNAHDFITSLTE--GYDTYCGDRGVQLSGGQKQRIAIA 1147
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLvfgrYFGMSTR-------------EIEAVIPSLLEfaRLESKADARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1148 RAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV-GRTSVVIAHRLSTIQN-CDAIAVLDKG-KLVERGTH 1217
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1014-1213 |
7.63e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.07 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGR--DIRSYHlRSLRRHIALVSQEPTLFAG-TIREN 1090
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPR-DAQAAGIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 I-------IYGGVSDKideaeiieaAKAANAHDFITSLteGYD----TYCGDrgvqLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:COG1129 100 IflgreprRGGLIDWR---------AMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1160 DEATSALdSQSE-----RVVQDALERvmvGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVE 1213
Cdd:COG1129 165 DEPTASL-TEREverlfRIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
992-1222 |
7.83e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 992 TGQVEFLDVDFSYPTRP--DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGL-----IERFYDPLKGIVKIDGRDIRSY 1064
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1065 HLRSLRRHIALVSQEP--TLFAGTIRENIIYGGVSDKIDEAEIIEAAKAanahdfITSLTEGYDTYCGDRGVQLSGGQKQ 1142
Cdd:PRK13645 84 EVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPE------LLKLVQLPEDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1143 RIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERGTHSS 1219
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFE 237
|
...
gi 15229473 1220 LLS 1222
Cdd:PRK13645 238 IFS 240
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
80-289 |
9.91e-17 |
|
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: 82.56 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 80 NSVALLYVACGSWVVC--------FLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQ 151
Cdd:cd18564 48 DPLALLLLAAAALVGIallrglasYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRR--RTGDLLSRLTGDVGAIQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 152 DVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGL---PFIVLLVIPglmYGRALISISRKIREEYNEAGFVAEQAISS 228
Cdd:cd18564 126 DLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALavaPLLLLAARR---FSRRIKEASREQRRREGALASVAQESLSA 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 229 VRTVYAFSGERKTISKFSTALQGSVKLGIKQ-GLAKGITIGSNGITFAMWGFMSWYGSRMVM 289
Cdd:cd18564 203 IRVVQAFGREEHEERRFARENRKSLRAGLRAaRLQALLSPVVDVLVAVGTALVLWFGAWLVL 264
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
378-582 |
1.18e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDG--VSID------KLQVkwlrsqmGLVSQEPALFAT 449
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsprdaiALGI-------GMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 -TIKENILFGKEDA-----SMDDVVEAAKA-SNAHNF-------ISQLPngyetqVGERgvqmsggqkQRIAIARAIIKS 515
Cdd:COG3845 95 lTVAENIVLGLEPTkggrlDRKAARARIRElSERYGLdvdpdakVEDLS------VGEQ---------QRVEILKALYRG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 516 PTILLLDEATSAL-DSESERVVqEALEN-ASIGRTTILIAHRLSTIR-NADVISVVKNGHIVETG-----SHDEL 582
Cdd:COG3845 160 ARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMaIADRVTVLRRGKVVGTVdtaetSEEEL 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
371-557 |
1.43e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 371 RLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKW---LRSQ-MGLVSQEPAL 446
Cdd:PRK11629 19 SVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 447 FAT-TIKENIlfgkedaSMDDVVEAAKASNAHNFISQL--PNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDE 523
Cdd:PRK11629 99 LPDfTALENV-------AMPLLIGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 15229473 524 ATSALDSESERVVQEALE--NASIGRTTILIAHRLS 557
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGelNRLQGTAFLVVTHDLQ 207
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
362-584 |
1.45e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 362 KNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVS 441
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 442 QE-PALFATTIKENIL------------FGKEDasMDDVVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAI 508
Cdd:PRK10575 92 QQlPAAEGMTVRELVAigrypwhgalgrFGAAD--REKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 509 ARAIIKSPTILLLDEATSALDSESERVVQEALENASIGR--TTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELME 584
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
378-554 |
1.47e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.90 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSidklqVKWLRSQMGLVSQEPALFA-TTIKENIL 456
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQNEGLLPwRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 457 FGKEDASMDdvvEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVV 536
Cdd:PRK11248 93 FGLQLAGVE---KMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|
gi 15229473 537 QEALEN--ASIGRTTILIAH 554
Cdd:PRK11248 168 QTLLLKlwQETGKQVLLITH 187
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1003-1206 |
1.47e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1003 SYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKidgrdirsyhlRSLRRHIALVSQ---E 1079
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-----------RAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1080 PTLFAGTIRENIIYG--------GVSDKIDEAEIIEAAKAANAHDFitsltegydtycGDRGVQ-LSGGQKQRIAIARAV 1150
Cdd:NF040873 67 PDSLPLTVRDLVAMGrwarrglwRRLTRDDRAAVDDALERVGLADL------------AGRQLGeLSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDAL-ERVMVGRTSVVIAHRLSTIQNCDAIAVL 1206
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
370-553 |
1.55e-16 |
|
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: 79.32 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 370 SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRsQMGLVSQEPALFAT 449
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 -TIKENILFGKED-ASMDDVVEAAKASNAHNFISQLPNGyetqvgergvQMSGGQKQRIAIARAIIKSPTILLLDEATSA 527
Cdd:TIGR01189 88 lSALENLHFWAAIhGGAQRTIEDALAAVGLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 15229473 528 LDSESERVVQEALEnASIGRTTILIA 553
Cdd:TIGR01189 158 LDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
376-587 |
1.56e-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: 79.49 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRF--YDPLAGEILIDGVSIDKLQVKwLRSQMG--LVSQEPalfatti 451
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGifLAFQYP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 452 kenilfgkedasmddvVEAAKASNAhNFIsqlpngyetqvgeRGVQM--SGGQKQRIAIARAIIKSPTILLLDEATSALD 529
Cdd:cd03217 87 ----------------PEIPGVKNA-DFL-------------RYVNEgfSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 530 SESERVVQEALEN-ASIGRTTILIAH--RLSTIRNADVISVVKNGHIVETGShDELMENID 587
Cdd:cd03217 137 IDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALEIE 196
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
96-289 |
1.59e-16 |
|
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: 81.71 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 96 FLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLhvTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVG 175
Cdd:cd18542 57 YLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDK--ARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 176 FILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKL 255
Cdd:cd18542 135 FSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDL 214
|
170 180 190
....*....|....*....|....*....|....*
gi 15229473 256 GIKQGLAKGITIG-SNGITFAMWGFMSWYGSRMVM 289
Cdd:cd18542 215 NIKLAKLLAKYWPlMDFLSGLQIVLVLWVGGYLVI 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1017-1216 |
1.65e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.32 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1017 SIKIEEGKSTAIVGPSGSGKSTI---IGLIERfydPLKGIVKIDGRDIRSY---HLRSLRRHIALVSQEPtlFA------ 1084
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNP--YGslnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1085 --GTIREN--IIYGGVSDKideaeiieaAKAANAHDFITSL---TEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:PRK11308 110 kvGQILEEplLINTSLSAA---------ERREKALAMMAKVglrPEHYDRYPH----MFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1158 LLDEATSALD----SQSERVVQDaLERVMvGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:PRK11308 177 VADEPVSALDvsvqAQVLNLMMD-LQQEL-GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
736-944 |
1.70e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 81.44 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 736 NFAY------MGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVgdrMALVVQTVSAVTIafTM 809
Cdd:cd18574 59 TFAYisllsvVGERVAARLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSSF---KQCVSQGLRSVTQ--TV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 810 GLVIAW-----RLALVMIAVQPVIIVC--FYTRrvLLKSMSKKAiKAQDE-SSKLAAEAVSNVRTITAFSSQERIMKMLE 881
Cdd:cd18574 132 GCVVSLylispKLTLLLLVIVPVVVLVgtLYGS--FLRKLSRRA-QAQVAkATGVADEALGNIRTVRAFAMEDRELELYE 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 882 KAQESPRRESIRqswfAGFGLAMSQSLTSctWALD------FWYGGRLIQDGYITAKALFeTFMILVST 944
Cdd:cd18574 209 EEVEKAAKLNEK----LGLGIGIFQGLSN--LALNgivlgvLYYGGSLVSRGELTAGDLM-SFLVATQT 270
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
378-582 |
1.93e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKS-TVISLLQRFYDP----LAGEILIDGVSI---DKLQVKWLR-SQMGLVSQEPALFA 448
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 449 T---TIKENIL--------FGKEDA--SMDDVVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKS 515
Cdd:PRK15134 106 NplhTLEKQLYevlslhrgMRREAArgEILNCLDRVGIRQAAKRLTDYPH-----------QLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 516 PTILLLDEATSALD-SESERVVQEALE-NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:PRK15134 175 PELLIADEPTTALDvSVQAQILQLLRElQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
994-1222 |
2.08e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.65 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPT----RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKIDGR--DIRS 1063
Cdd:COG4167 6 EVRNLSKTFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTlakmLAGIIE----PTSGEILINGHklEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1064 YHLRSlrRHIALVSQEPT------LFAGTIRE-----NiiyggvsdkideaeiieaakaanahdfiTSLTEG------YD 1126
Cdd:COG4167 82 YKYRC--KHIRMIFQDPNtslnprLNIGQILEeplrlN----------------------------TDLTAEereeriFA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1127 TYcgdRGV------------QLSGGQKQRIAIARAVLKNPSVLLLDEATSALD----SQSERVVQDALERvmVGRTSVVI 1190
Cdd:COG4167 132 TL---RLVgllpehanfyphMLSSGQKQRVALARALILQPKIIIADEALAALDmsvrSQIINLMLELQEK--LGISYIYV 206
|
250 260 270
....*....|....*....|....*....|...
gi 15229473 1191 AHRLSTIQNC-DAIAVLDKGKLVERGTHSSLLS 1222
Cdd:COG4167 207 SQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
103-265 |
2.21e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 81.05 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 103 TRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDsfvIQDVLSeklpNF-------LMSASTFVGSYIVG 175
Cdd:cd18574 67 SVVGERVAARLRNDLFSSLLRQDIAFFDTH--RTGELVNRLTAD---VQEFKS----SFkqcvsqgLRSVTQTVGCVVSL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 176 FILLWRLAI---VGLPFIVLLvipGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGS 252
Cdd:cd18574 138 YLISPKLTLlllVIVPVVVLV---GTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKA 214
|
170
....*....|...
gi 15229473 253 VKLGIKQGLAKGI 265
Cdd:cd18574 215 AKLNEKLGLGIGI 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
999-1211 |
2.95e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDgRDIRsyhlrslrrhIALVSQ 1078
Cdd:COG0488 3 NLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EPTLFAG-TIRENIIYG-----GVSDKIDEAEIIEAAKAANAHDfITSLTEGYDTYCG---------------------D 1131
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGdaelrALEAELEELEAKLAEPDEDLER-LAELQEEFEALGGweaearaeeilsglgfpeedlD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1132 RGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQServvQDALERVMVGRTS--VVIAH-R--LSTIqnCDAIAV 1205
Cdd:COG0488 148 RPVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGtvLVVSHdRyfLDRV--ATRILE 221
|
....*.
gi 15229473 1206 LDKGKL 1211
Cdd:COG0488 222 LDRGKL 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
359-582 |
3.03e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVkfvYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQMG 438
Cdd:PRK11000 4 VTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFA-TTIKENILFGKEDASMDDVvEAAKASNAHNFISQLPNGYETQVGErgvqMSGGQKQRIAIARAIIKSPT 517
Cdd:PRK11000 79 MVFQSYALYPhLSVAENMSFGLKLAGAKKE-EINQRVNQVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 518 ILLLDEATSALDSESErvVQEALENAS----IGRTTILIAH-RLSTIRNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK11000 154 VFLLDEPLSNLDAALR--VQMRIEISRlhkrLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1006-1213 |
3.04e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1006 TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI----RSYHlRSLRRHIALVSQEPt 1081
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQR-KAFRRDIQMVFQDS- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1082 LFA----GTIRENIiyggvsdkideaeiieaakaANAHDFITSLTE--------------GYDTYCGDR-GVQLSGGQKQ 1142
Cdd:PRK10419 99 ISAvnprKTVREII--------------------REPLRHLLSLDKaerlarasemlravDLDDSVLDKrPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1143 RIAIARAVLKNPSVLLLDEATSALDsqseRVVQ----DALERVM--VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVE 1213
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLD----LVLQagviRLLKKLQqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
83-289 |
3.07e-16 |
|
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: 80.63 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 83 ALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFL 162
Cdd:cd18563 48 GLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKR--QTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 163 MSASTFVGSYIVGFILLWRLAIVGL---PFIVLLVIpglMYGRALISISRKI-REEYNEAGFVAEqAISSVRTVYAFSGE 238
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLALLVLipvPLVVWGSY---FFWKKIRRLFHRQwRRWSRLNSVLND-TLPGIRVVKAFGQE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 239 RKTISKFSTALQGSVKLGIKqglakgitigSNGITFAMWGFMS-----------WYGSRMVM 289
Cdd:cd18563 202 KREIKRFDEANQELLDANIR----------AEKLWATFFPLLTfltslgtlivwYFGGRQVL 253
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
715-930 |
3.15e-16 |
|
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: 80.60 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 715 YALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMA 794
Cdd:cd18550 41 LALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTR--TRTGEIQSRLNNDVGGAQSVVTGTLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 795 LVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCfyTRRV--LLKSMSKKAIKAQDESSKLAAE--AVSNVRTITAF 870
Cdd:cd18550 119 SVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLP--TRRVgrRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLF 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 871 SSQERIMKMLEKAQESPRRESIRQS-WFAGFGLAMSqSLTSCTWALDFWYGGRLIQDGYIT 930
Cdd:cd18550 197 GREDDEAARFARRSRELRDLGVRQAlAGRWFFAALG-LFTAIGPALVYWVGGLLVIGGGLT 256
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
999-1221 |
3.53e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRpdvIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQ 1078
Cdd:PRK10575 16 NVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 E-PTLFAGTIRENIIYG-----------GVSD--KIDEAEIIEAAKAAnAHDFITSLtegydtycgdrgvqlSGGQKQRI 1144
Cdd:PRK10575 93 QlPAAEGMTVRELVAIGrypwhgalgrfGAADreKVEEAISLVGLKPL-AHRLVDSL---------------SGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1145 AIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIA--HRLS-TIQNCDAIAVLDKGKLVERGTHSSLL 1221
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
995-1210 |
3.72e-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: 76.72 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIdGRDIRSYHLRslrrhia 1074
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVKIGYFE------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 lvsqeptlfagtireniiyggvsdkideaeiieaakaanahdfitsltegydtycgdrgvQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03221 70 ------------------------------------------------------------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1155 SVLLLDEATSALDSQServvQDALERVMVG--RTSVVIAHRLSTIQN-CDAIAVLDKGK 1210
Cdd:cd03221 90 NLLLLDEPTNHLDLES----IEALEEALKEypGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
995-1223 |
4.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.16 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSY-PTRP--DVIIFkNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDgrDI------RSYH 1065
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1066 LRSLRRHIALVSQEP--TLFAGTIRENIIYG----GVSDKideaeiIEAAKAANAHDFITSLTEGYDTycgdRGVQLSGG 1139
Cdd:PRK13643 79 IKPVRKKVGVVFQFPesQLFEETVLKDVAFGpqnfGIPKE------KAEKIAAEKLEMVGLADEFWEK----SPFELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1140 QKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV-MVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTH 1217
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*.
gi 15229473 1218 SSLLSK 1223
Cdd:PRK13643 229 SDVFQE 234
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
714-930 |
4.37e-16 |
|
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: 80.25 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 714 IYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRM 793
Cdd:cd18563 44 LLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDK--RQTGSLMSRVTSDTDRLQDFLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 794 -ALVVQTVSAVTIAFTMgLVIAWRLALVMIAVQPVIIVCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSS 872
Cdd:cd18563 122 pDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQ 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 873 QERIMKMLEKAQESPRRESIR-QSWFAGFGLAMSQSLTSCTWALdFWYGGRLIQDGYIT 930
Cdd:cd18563 201 EKREIKRFDEANQELLDANIRaEKLWATFFPLLTFLTSLGTLIV-WYFGGRQVLSGTMT 258
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1011-1216 |
4.38e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.13 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1011 IIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSY-HLRSLRRHIALVSQEP--TLFAGTI 1087
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAGMVFQNPdnQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIYG----GVSDKIDEAEIIEAAKAANAHDFitsltEGYDTYCgdrgvqLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:PRK13633 104 EEDVAFGpenlGIPPEEIRERVDESLKKVGMYEY-----RRHAPHL------LSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1164 SALDSQSERVVQDALERV--MVGRTSVVIAHRLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
382-598 |
4.46e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTvisLLQRfydpLAGeiLIDGVSIDKLQVKWL-----------------RSQMGLVSQEP 444
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKST---LLRH----LSG--LITGDKSAGSHIELLgrtvqregrlardirksRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 445 ALF-ATTIKENILFG------------------KEDASMDDVVEAAKASNAHNFISQLpngyetqvgergvqmSGGQKQR 505
Cdd:PRK09984 96 NLVnRLSVLENVLIGalgstpfwrtcfswftreQKQRALQALTRVGMVHFAHQRVSTL---------------SGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 506 IAIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
250
....*....|....*..
gi 15229473 583 -MENIDGQYSTLVHLQQ 598
Cdd:PRK09984 241 dNERFDHLYRSINRVEE 257
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
373-587 |
4.59e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.34 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKST---VISLLQRfYDPLAGEILIDGVSIDKLQVKwLRSQMGL-VS-QEP--- 444
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPvei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 445 -----ALFATTIKENILFGKEDA--SMDDVVEAAKASN-AHNFIsqlpngyetqvgERGVQ--MSGGQKQRIAIARAIIK 514
Cdd:COG0396 90 pgvsvSNFLRTALNARRGEELSAreFLKLLKEKMKELGlDEDFL------------DRYVNegFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 515 SPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAH--RLSTIRNADVISVVKNGHIVETGSHdELMENID 587
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELALELE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
378-586 |
4.68e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.93 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILI----DGVSIDKLQVKwLRSQ----MGLVSQEPALFA- 448
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 449 TTIKENIL------FGKEDASMDDVVEAAKA----SNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSPTI 518
Cdd:TIGR03269 380 RTVLDNLTeaigleLPDELARMKAVITLKMVgfdeEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 519 LLLDEATSALDSESERVVQEALENA--SIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMENI 586
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAreEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
998-1212 |
4.95e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.36 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 998 LDVDFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI--RSYHLRSlrRHIAL 1075
Cdd:COG1101 7 LSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYKRA--KYIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1076 VSQEPTlfAGT-----IREN--IIYG---------GVSDKideaeiieaakaaNAHDFITSLTE---GYDTYCGDRGVQL 1136
Cdd:COG1101 85 VFQDPM--MGTapsmtIEENlaLAYRrgkrrglrrGLTKK-------------RRELFRELLATlglGLENRLDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVmVGR---TSVVIAHRLStiqncDAIA------VLD 1207
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNME-----QALDygnrliMMH 223
|
....*
gi 15229473 1208 KGKLV 1212
Cdd:COG1101 224 EGRII 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
386-582 |
5.14e-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: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 386 SGKTVALVGGSGSGKSTVISLLQrFYDP----LAGEILIDGVSIDKLQVKwLRSqmGLVSQEPALFAT-TIKENILF--- 457
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPIDAKEMR-AIS--AYVQQDDLFIPTlTVREHLMFqah 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 458 ---------GKEDASMDDVVEAAKASNAHNFISQLPNgyetqvgeRGVQMSGGQKQRIAIARAIIKSPTILLLDEATSAL 528
Cdd:TIGR00955 126 lrmprrvtkKEKRERVDEVLQALGLRKCANTRIGVPG--------RVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 529 DSES-ERVVQEALENASIGRTTILIAHRLST--IRNADVISVVKNGHIVETGSHDEL 582
Cdd:TIGR00955 198 DSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
359-577 |
5.46e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 78.34 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLETS-------------------IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEIL 419
Cdd:cd03220 1 IELENVSKSYPTYKGGSsslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 420 IDGvsidklQVKWLrsqMGL-VSQEPALfatTIKENILF--------GKE-DASMDDVVEaakasnahnfISQLPNGYET 489
Cdd:cd03220 81 VRG------RVSSL---LGLgGGFNPEL---TGRENIYLngrllglsRKEiDEKIDEIIE----------FSELGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 490 QVGErgvqMSGGQKQRIAIARAIIKSPTILLLDEATSALDSE----SERVVQEALENasiGRTTILIAHRLSTIRN-ADV 564
Cdd:cd03220 139 PVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQ---GKTVILVSHDPSSIKRlCDR 211
|
250
....*....|...
gi 15229473 565 ISVVKNGHIVETG 577
Cdd:cd03220 212 ALVLEKGKIRFDG 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
376-577 |
6.80e-16 |
|
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: 78.08 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKST---VISLLQRFYDPLAGEILIDGVSIDKLQVKwlrSQMGLVSQEPALFAT-TI 451
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRKPDQFQ---KCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 452 KENILF-----------GKEDASMDDVV---EAAKASNAHNFISQLpngyetqvgergvqmSGGQKQRIAIARAIIKSPT 517
Cdd:cd03234 99 RETLTYtailrlprkssDAIRKKRVEDVllrDLALTRIGGNLVKGI---------------SGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 518 ILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAH--RLSTIRNADVISVVKNGHIVETG 577
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
370-554 |
9.21e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.15 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 370 SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSqMGLVSQEPALFAT 449
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG-LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 -TIKENILFGKEDASmDDVVEAAKAsnahnfisqlpngyetQVGERGV------QMSGGQKQRIAIARAIIKSPTILLLD 522
Cdd:cd03231 88 lSVLENLRFWHADHS-DEQVEEALA----------------RVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|...
gi 15229473 523 EATSALDSESERVVQEAL-ENASIGRTTILIAH 554
Cdd:cd03231 151 EPTTALDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1006-1191 |
9.68e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1006 TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHI----ALvsqEPT 1081
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLghrnAM---KPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1082 LfagTIRENI-----IYGGVSDKIDEaeiieaakaanAHDF-----ITSLTEGYdtycgdrgvqLSGGQKQRIAIARAVL 1151
Cdd:PRK13539 88 L---TVAENLefwaaFLGGEELDIAA-----------ALEAvglapLAHLPFGY----------LSAGQKRRVALARLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15229473 1152 KNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIA 1191
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
373-554 |
1.12e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRSQ-MGLVSQEPALFA 448
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 449 T-TIKENI-----LFGKEDASMDDvveaakasNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLD 522
Cdd:PRK10584 102 TlNALENVelpalLRGESSRQSRN--------GAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190
....*....|....*....|....*....|....
gi 15229473 523 EATSALDSES-ERVVQEALE-NASIGRTTILIAH 554
Cdd:PRK10584 172 EPTGNLDRQTgDKIADLLFSlNREHGTTLILVTH 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
361-532 |
1.26e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 361 FKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGvsidklqvkwlRSQMGLV 440
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 441 SQEPALFAT-TIKENILFGKED------------ASMDDVVEA-AKASNAHNFISQLpNGYE------------------ 488
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAElraleaeleeleAKLAEPDEDlERLAELQEEFEAL-GGWEaearaeeilsglgfpeed 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15229473 489 --TQVGErgvqMSGGQKQRIAIARAIIKSPTILLLDEATSALDSES 532
Cdd:COG0488 146 ldRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
387-585 |
1.40e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 78.34 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 387 GKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWL-----------------RSQMGLVSQEPALFAT 449
Cdd:COG4167 39 GQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRckhirmifqdpntslnpRLNIGQILEEPLRLNT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENilfgkedASMDDVVEAAKasnahnfisqlpngyetQVG------ERGVQM-SGGQKQRIAIARAIIKSPTILLLD 522
Cdd:COG4167 119 DLTAE-------EREERIFATLR-----------------LVGllpehaNFYPHMlSSGQKQRVALARALILQPKIIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 523 EATSALD-SESERVVQEALE-NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:COG4167 175 EALAALDmSVRSQIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
378-585 |
1.54e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYdP---LAGEILIDGvsiDKLQVKWLR--SQMGLV--SQEPALFAT- 449
Cdd:PRK13549 22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEG---EELQASNIRdtERAGIAiiHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDAS---MDDvveAAKASNAHNFISQL-----PNgyeTQVGERGvqmsGGQKQRIAIARAIIKSPTILLL 521
Cdd:PRK13549 98 SVLENIFLGNEITPggiMDY---DAMYLRAQKLLAQLkldinPA---TPVGNLG----LGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 522 DEATSALdSESE-RVVQEALEN-ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK13549 168 DEPTASL-TESEtAVLLDIIRDlKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTED 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
979-1233 |
1.60e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.37 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 979 DPEDPDG-----YETErITGQVEFLDVD-----FSYPTRPDViifKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYD 1048
Cdd:TIGR01257 906 DPEHPEGindsfFERE-LPGLVPGVCVKnlvkiFEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1049 PLKGIVKIDGRDIRSyHLRSLRRHIALVSQEPTLFAG-TIRENIIYGGvsdKIDEAEIIEAAKAANAHDFITSLTEGYDT 1127
Cdd:TIGR01257 982 PTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFYA---QLKGRSWEEAQLEMEAMLEDTGLHHKRNE 1057
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1128 YCGDrgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNC-DAIAVL 1206
Cdd:TIGR01257 1058 EAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAII 1133
|
250 260
....*....|....*....|....*..
gi 15229473 1207 DKGKLVERGTHSSLLSKGPTGIYFSLV 1233
Cdd:TIGR01257 1134 SQGRLYCSGTPLFLKNCFGTGFYLTLV 1160
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
375-594 |
1.67e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 375 SIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFA-TTIKE 453
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 454 NILFG------------KEDAsmDDVVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSPTILLL 521
Cdd:PRK10253 101 LVARGryphqplftrwrKEDE--EAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 522 DEATSALDSESERVVQEALE--NASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDE-----LMENIDGQYSTL 593
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSelNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEivtaeLIERIYGLRCMI 247
|
.
gi 15229473 594 V 594
Cdd:PRK10253 248 I 248
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
380-578 |
1.82e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 380 FCLRvpSGKTVALVGGSGSGKSTVISLLQRFYdPLAGEILIDGVSIDKLQVKWL---RSQMGLVSQEP--AL-----FAT 449
Cdd:PRK15134 307 FTLR--PGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLnprlnVLQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDASM----DDVVEAAK-----ASNAHNFISQLpngyetqvgergvqmSGGQKQRIAIARAIIKSPTILL 520
Cdd:PRK15134 384 IIEEGLRVHQPTLSAaqreQQVIAVMEevgldPETRHRYPAEF---------------SGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 521 LDEATSALDseseRVVQ-------EALENASiGRTTILIAHRLSTIRNA--DVIsVVKNGHIVETGS 578
Cdd:PRK15134 449 LDEPTSSLD----KTVQaqilallKSLQQKH-QLAYLFISHDLHVVRALchQVI-VLRQGEVVEQGD 509
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1011-1222 |
1.90e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.72 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1011 IIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEPTLFAG-TIRE 1089
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NIIYGGVSD--------KIDEAEIIEAAKAANahdfITSL-TEGYDTycgdrgvqLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:PRK10253 101 LVARGRYPHqplftrwrKEDEEAVTKAMQATG----ITHLaDQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1161 EATSALDSQSERVVQDALERV--MVGRTSVVIAHRLStiQNC---DAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLN--QACryaSHLIALREGKIVAQGAPKEIVT 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
376-578 |
2.12e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQvKWLRSQM-GLVSQEPAL-FATTIKE 453
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELARRrAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 454 NILFG--------KEDasmDDVVEAAKASN-----AHNFISQLpngyetqvgergvqmSGGQKQRIAIARAII------K 514
Cdd:PRK13548 96 VVAMGraphglsrAED---DALVAAALAQVdlahlAGRDYPQL---------------SGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 515 SPTILLLDEATSALD-SESERVVQEALENA-SIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGS 578
Cdd:PRK13548 158 PPRWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
378-554 |
2.18e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 76.74 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQvkwlRSQMgLVSQEPALFA-TTIKENIL 456
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRM-VVFQNYSLLPwLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 457 FGKeDASMDDVVEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVV 536
Cdd:TIGR01184 77 LAV-DRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|
gi 15229473 537 QEALEN--ASIGRTTILIAH 554
Cdd:TIGR01184 154 QEELMQiwEEHRVTVLMVTH 173
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1013-1192 |
2.43e-15 |
|
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: 76.70 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKG------------IVKIDGRDIrsYHLRslRRHIALVSQ-- 1078
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsilvrhdggwvdLAQASPREI--LALR--RRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 -------------EPTLFAGTIREniiyggvsdkideaeiieaAKAANAHDFITSL------------Tegydtycgdrg 1133
Cdd:COG4778 103 rviprvsaldvvaEPLLERGVDRE-------------------EARARARELLARLnlperlwdlppaT----------- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1134 vqLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTSVV-IAH 1192
Cdd:COG4778 153 --FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1003-1216 |
2.53e-15 |
|
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: 76.81 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1003 SYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHL-RSLRRHIALVSQEPT 1081
Cdd:cd03218 9 RYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1082 LFAG-TIRENII----YGGVSDKIdeaeiieaakaanAHDFITSLTEGYD-TYCGDR-GVQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03218 86 IFRKlTVEENILavleIRGLSKKE-------------REEKLEELLEEFHiTHLRKSkASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1155 SVLLLDEATSALDSQS----ERVVQDALERVMvgrtSVVIA-HRLS-TIQNCDAIAVLDKGKLVERGT 1216
Cdd:cd03218 153 KFLLLDEPFAGVDPIAvqdiQKIIKILKDRGI----GVLITdHNVReTLSITDRAYIIYEGKVLAEGT 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
994-1223 |
3.61e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.85 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSyptrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERF--YDPLKGIV----------------- 1054
Cdd:TIGR03269 2 EVKNLTKKFD-----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1055 ----------------KIDGRDIRSYHLRSLRRHIALVSQEPTLFAG--TIRENIIyggvsDKIDEAEIIEAAKAANAHD 1116
Cdd:TIGR03269 77 kvgepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVL-----EALEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1117 FITSLTEGYDTYCGDRgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRL 1194
Cdd:TIGR03269 152 LIEMVQLSHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWP 229
|
250 260 270
....*....|....*....|....*....|
gi 15229473 1195 STIQNCDAIAV-LDKGKLVERGTHSSLLSK 1223
Cdd:TIGR03269 230 EVIEDLSDKAIwLENGEIKEEGTPDEVVAV 259
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
368-563 |
3.74e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 368 YPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGvsidklqvkwlRSQMGLVSQ---EP 444
Cdd:NF040873 2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 445 ALFATTIKENI---------LFGKEDASMDDVVEAA-KASNAHNFISQlpngyetQVGErgvqMSGGQKQRIAIARAIIK 514
Cdd:NF040873 68 DSLPLTVRDLVamgrwarrgLWRRLTRDDRAAVDDAlERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15229473 515 SPTILLLDEATSALDSESERVVQEAL-ENASIGRTTILIAHRLSTIRNAD 563
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1007-1216 |
4.07e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1007 RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIErFYDP----LKGIVKIDGRDIRSyhlRSLRRHIALVSQE--- 1079
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPIDA---KEMRAISAYVQQDdlf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1080 -PTLfagTIRENIIYGG----------------VSDKIDEaeiieaakaanahdfiTSLTEGYDTYCGDRGVQ--LSGGQ 1140
Cdd:TIGR00955 111 iPTL---TVREHLMFQAhlrmprrvtkkekrerVDEVLQA----------------LGLRKCANTRIGVPGRVkgLSGGE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1141 KQRIAIARAVLKNPSVLLLDEATSALDSQS-ERVVQDALERVMVGRTSVVIAHRLST--IQNCDAIAVLDKGKLVERGT 1216
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
83-299 |
4.49e-15 |
|
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: 77.43 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 83 ALLYVAC--GSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLhvTSTSDVITSVSSDSFVIQDVLSEKLPN 160
Cdd:cd18544 44 ALLYLGLllLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLVT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 161 FLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEA-GFVAEQaISSVRTVYAFSGER 239
Cdd:cd18544 122 LIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLnAFLQES-ISGMSVIQLFNREK 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 240 KTISKFSTALQGSVKLGIKQglakgITIGSngITFAMWGFMS--------WYGSRMVMYHGAQGGTVF 299
Cdd:cd18544 201 REFEEFDEINQEYRKANLKS-----IKLFA--LFRPLVELLSslalalvlWYGGGQVLSGAVTLGVLY 261
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1012-1215 |
4.63e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.26 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERF--YDPLKGIVKIDGRDIR--SYHLRSlRRHIALVSQEPtlfagti 1087
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITdlPPEERA-RLGIFLAFQYP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 renIIYGGVSDKideaeiieaakaanahDFITSLTEGydtycgdrgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:cd03217 87 ---PEIPGVKNA----------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1168 SQSERVVQDALERVM-VGRTSVVIAH--RLSTIQNCDAIAVLDKGKLVERG 1215
Cdd:cd03217 137 IDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1003-1161 |
5.40e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.84 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1003 SYPTRPDViifKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKIDGRDIRSY--HLRSlRRHIALV 1076
Cdd:COG1137 12 SYGKRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLpmHKRA-RLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1077 SQEPTLFAG-TIRENII---------YGGVSDKIDEAEiieaakaanaHDFitSLTEGYDTycgdRGVQLSGGQKQRIAI 1146
Cdd:COG1137 84 PQEASIFRKlTVEDNILavlelrklsKKEREERLEELL----------EEF--GITHLRKS----KAYSLSGGERRRVEI 147
|
170
....*....|....*
gi 15229473 1147 ARAVLKNPSVLLLDE 1161
Cdd:COG1137 148 ARALATNPKFILLDE 162
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
972-1179 |
6.66e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 6.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 972 LDRYTSIDPEDPDGY------ETERITGQV-EFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIE 1044
Cdd:COG0488 286 LEKLEREEPPRRDKTveirfpPPERLGKKVlELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1045 RFYDPLKGIVKIdGRDIRsyhlrslrrhIALVSQEPTLFAG--TIRENIIYGGVSDKIdeaeiieaakaANAHDFITS-L 1121
Cdd:COG0488 363 GELEPDSGTVKL-GETVK----------IGYFDQHQEELDPdkTVLDELRDGAPGGTE-----------QEVRGYLGRfL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1122 TEGYD--TYCGDrgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALE 1179
Cdd:COG0488 421 FSGDDafKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD 476
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
359-555 |
6.93e-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: 73.73 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYdPLAGEilidgvSIDKLQvkwlRSQMG 438
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGSG------RIGMPE----GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFATTIKENILFgkedaSMDDVveaakasnahnfisqlpngyetqvgergvqMSGGQKQRIAIARAIIKSPTI 518
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 15229473 519 LLLDEATSALDSESERVVQEALENASIgrTTILIAHR 555
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1009-1230 |
7.34e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 76.69 E-value: 7.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyhlRSLRRHIALVSQEPTLFAG-TI 1087
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYLPEERGLYPKmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIY----GGVSDKideaeiieaakaaNAHDFITSLTEGYD--TYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:COG4152 89 GEQLVYlarlKGLSKA-------------EAKRRADEWLERLGlgDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1162 ATSALDSQSERVVQDAL-ERVMVGRTsvVI--AHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLSKGPTGIYF 1230
Cdd:COG4152 156 PFSGLDPVNVELLKDVIrELAAKGTT--VIfsSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1008-1212 |
7.75e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyhLRS----LRRHIALVSQEPTLF 1083
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSprdaIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AG-TIRENIIYG---GVSDKIDEAEiieaakaanAHDFITSLTEGY------DTYCGDrgvqLSGGQKQRIAIARAVLKN 1153
Cdd:COG3845 93 PNlTVAENIVLGlepTKGGRLDRKA---------ARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1154 PSVLLLDEATSALDSQsErvVQDALE--RVMV--GRTSVVIAHRLSTI-QNCDAIAVLDKGKLV 1212
Cdd:COG3845 160 ARILILDEPTAVLTPQ-E--ADELFEilRRLAaeGKSIIFITHKLREVmAIADRVTVLRRGKVV 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
378-582 |
8.55e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.51 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDP----LAGEILIDGVSIDKLQvkwLRSQM-GLVSQEP-ALF---- 447
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCA---LRGRKiATIMQNPrSAFnplh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 448 --ATTIKENIL-FGKE--DASMDDVVEAAKASNAHNFISQLPngyetqvgergVQMSGGQKQRIAIARAIIKSPTILLLD 522
Cdd:PRK10418 97 tmHTHARETCLaLGKPadDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 523 EATSALDSESERVVQEALEN--ASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1016-1216 |
9.31e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.26 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1016 FSIKIEEGKSTAIVGPSGSGKST----IIGLIerfydPLKGIVKIDGRDIRSYHLRSLRRHIA-LVSQEPTLFAGTIREn 1090
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTllarMAGLL-----PGQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 iiY-------GGVSDKIDEaeiieaakaanAHDFITSLTEGYDTYcgDRGV-QLSGGQKQRIAIARAVLK-----NPS-- 1155
Cdd:COG4138 89 --YlalhqpaGASSEAVEQ-----------LLAQLAEALGLEDKL--SRPLtQLSGGEWQRVRLAAVLLQvwptiNPEgq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1156 VLLLDEATSALD-SQservvQDALERVMV-----GRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGT 1216
Cdd:COG4138 154 LLLLDEPMNSLDvAQ-----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1014-1220 |
1.21e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.28 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTII-----------GLIERFYDPLKGIVKIDGRDIRSYHL-------------RSL 1069
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtGTIEWIFKDEKNKKKTKEKEKVLEKLviqktrfkkikkiKEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1070 RRHIALVSQ--EPTLFAGTIRENIIYGGVSDKIDEAEIIEAakaanAHDFITSLteGYD-TYCGDRGVQLSGGQKQRIAI 1146
Cdd:PRK13651 104 RRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKR-----AAKYIELV--GLDeSYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1147 ARAVLKNPSVLLLDEATSALDSQSERVVQDALERV-MVGRTSVVIAHRL-STIQNCDAIAVLDKGKLVERG-THSSL 1220
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1012-1195 |
2.26e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.08 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRS---LR-RHIALVSQEPTLFAG-T 1086
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1087 IRENI----IYGGVSDKideaeiieaAKAANAHDFITSLteGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:PRK11629 104 ALENVamplLIGKKKPA---------EINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 15229473 1163 TSALDSQSERVVQDALERVMV--GRTSVVIAHRLS 1195
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRlqGTAFLVVTHDLQ 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
992-1221 |
2.76e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 992 TGQVEFLDVDFSYPtrpDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyHLRSLRR 1071
Cdd:PRK13537 5 VAPIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1072 HIALVSQEPTL---FagTIRENII----YGGVSdkideaeiieaakAANAHDFITSLTE------GYDTYCGDrgvqLSG 1138
Cdd:PRK13537 81 RVGVVPQFDNLdpdF--TVRENLLvfgrYFGLS-------------AAAARALVPPLLEfaklenKADAKVGE----LSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV-GRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:PRK13537 142 GMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGA 221
|
....*
gi 15229473 1217 HSSLL 1221
Cdd:PRK13537 222 PHALI 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
378-576 |
3.12e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.75 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYdP---LAGEILIDGvsiDKLQVKWLRS--QMGLV--SQEPALFA-T 449
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDG---EVCRFKDIRDseALGIViiHQELALIPyL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDASM-----DDVVEAAKASNAHNFISQLPNgyeTQVGERGVqmsgGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:NF040905 94 SIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15229473 525 TSAL-DSESERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVET 576
Cdd:NF040905 167 TAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
359-572 |
3.53e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 70.94 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGvsidklqvkwlrsqmg 438
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 lvsqepalfatTIKenilfgkedasmddvveaakasnahnfISQLPngyetqvgergvQMSGGQKQRIAIARAIIKSPTI 518
Cdd:cd03221 62 -----------TVK---------------------------IGYFE------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 519 LLLDEATSALDSEServvQEALENA--SIGRTTILIAHRLSTIRN-ADVISVVKNGH 572
Cdd:cd03221 92 LLLDEPTNHLDLES----IEALEEAlkEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
378-582 |
3.74e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.76 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQvkwlRSQMGLVSQEPALFAT-TIKENIL 456
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPKmKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 457 F-------GKEDA--SMDDVVEAakasnahnFisqlpngyetQVGERG---VQ-MSGGQKQRIAIARAIIKSPTILLLDE 523
Cdd:COG4152 94 YlarlkglSKAEAkrRADEWLER--------L----------GLGDRAnkkVEeLSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 524 ATSALDSESERVVQEAL-ENASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDEL 582
Cdd:COG4152 156 PFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1026-1215 |
4.87e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.91 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1026 TAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGR---DIRS-YHLRSLRRHIALVSQEPTLFAG-TIRENIIYGgvsdki 1100
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARLFPHyKVRGNLRYG------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1101 deaeiieAAKAANAH-DFITSLTegydtycgdrGVQ---------LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQS 1170
Cdd:PRK11144 101 -------MAKSMVAQfDKIVALL----------GIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229473 1171 ERVVQDALERVM--VGRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERG 1215
Cdd:PRK11144 164 KRELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1007-1216 |
5.83e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1007 RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRdirsyhLRSLrrhIAL-VSQEPTLfag 1085
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPEL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 TIRENIIYG----GVSDK-IDEAEiieaakaanahDFITSLTEgydtyCG---DRGVQ-LSGGQKQRIAIARAVLKNPSV 1156
Cdd:COG1134 104 TGRENIYLNgrllGLSRKeIDEKF-----------DEIVEFAE-----LGdfiDQPVKtYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1157 LLLDEATSALDSQ----SERVVQDALERvmvGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:COG1134 168 LLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
359-581 |
6.14e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 6.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIdGVSIdklqvkwlrsQMG 438
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFattikenilfgKEDASMDDVVEAAKasnahnfisqlPNGYETQV----------GER-----GVqMSGGQK 503
Cdd:COG0488 382 YFDQHQEEL-----------DPDKTVLDELRDGA-----------PGGTEQEVrgylgrflfsGDDafkpvGV-LSGGEK 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 504 QRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASiGrTTILIAH-R--LSTIrnADVISVVKNGHIVE-TGSH 579
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGY 514
|
..
gi 15229473 580 DE 581
Cdd:COG0488 515 DD 516
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
349-541 |
8.19e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 349 GHKLEKIRGEVE-FKNVkfvypsrletsifdDFCLRvpSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDK 427
Cdd:PRK13539 5 GEDLACVRGGRVlFSGL--------------SFTLA--AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 428 LQVkwlRSQMGLVSQEPALFAT-TIKENILFGKE--DASMDDVVEAAKASNAHNfISQLPNGYetqvgergvqMSGGQKQ 504
Cdd:PRK13539 69 PDV---AEACHYLGHRNAMKPAlTVAENLEFWAAflGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKR 134
|
170 180 190
....*....|....*....|....*....|....*..
gi 15229473 505 RIAIARAIIKSPTILLLDEATSALDSESERVVQEALE 541
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
379-582 |
9.92e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 9.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 379 DFCLRVPSGktvaLVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSID--KLQVKWLRSQMGLVSQEP--ALFATTIKEN 454
Cdd:PRK13638 23 DFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQDPeqQIFYTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFG------KEDASMDDVVEAAKASNAHNFISQlPngyetqvgergVQ-MSGGQKQRIAIARAIIKSPTILLLDEATSA 527
Cdd:PRK13638 99 IAFSlrnlgvPEAEITRRVDEALTLVDAQHFRHQ-P-----------IQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 528 LDSES--------ERVVQEalenasiGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:PRK13638 167 LDPAGrtqmiaiiRRIVAQ-------GNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
387-591 |
1.08e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 387 GKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVKWLRSQMGLVSQEPalFAT---------TIKE- 453
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDP--YASldprqtvgdSIMEp 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 454 ----NILFGKEDAS-MDDVVEAAKASNAHNFisQLPNgyetqvgergvQMSGGQKQRIAIARAIIKSPTILLLDEATSAL 528
Cdd:PRK10261 428 lrvhGLLPGKAAAArVAWLLERVGLLPEHAW--RYPH-----------EFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 529 D-SESERVVQEALE-NASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETGSHDELMENIDGQYS 591
Cdd:PRK10261 495 DvSIRGQIINLLLDlQRDFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1009-1215 |
1.25e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.91 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRdiRSYHLRSLRRHIALVSQEPTLFAG-TI 1087
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMVFQSYALYPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIYG----GVSDK-IDEAEIIEAAKAANAHdfitsLTEgydtycgDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:PRK11000 93 AENMSFGlklaGAKKEeINQRVNQVAEVLQLAH-----LLD-------RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1163 TSALDSqSERV---VQDALERVMVGRTSVVIAH-RLSTIQNCDAIAVLDKGKLVERG 1215
Cdd:PRK11000 161 LSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1009-1216 |
1.26e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGlIERfYDPLKGIVKIDGRDI-------RSyhlrslRRHIALVS 1077
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakvLMG-HPK-YEVTSGSILLDGEDIlelspdeRA------RAGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1078 QEPTLFAG-TIRE--NIIYGGVSDKideaeiieaakAANAHDFITSLTE-----GYDTYCGDRGVQ--LSGGQKQRIAIA 1147
Cdd:COG0396 84 QYPVEIPGvSVSNflRTALNARRGE-----------ELSAREFLKLLKEkmkelGLDEDFLDRYVNegFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1148 RAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV-GRTSVVIAH--RLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
378-587 |
1.37e-13 |
|
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: 74.86 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFY--DPLAGEILIDGVSIDKLQVKWL-RSQMGLVSQEPALFAT-TIKE 453
Cdd:TIGR02633 18 DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 454 NILFGKE----DASMDDvveAAKASNAHNFISQL-----PNgyETQVGERGvqmsGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:TIGR02633 98 NIFLGNEitlpGGRMAY---NAMYLRAKNLLRELqldadNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 525 TSAL-DSESERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETgshdELMENID 587
Cdd:TIGR02633 169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVAT----KDMSTMS 229
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
715-930 |
1.52e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 72.90 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 715 YALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMA 794
Cdd:cd18540 44 FILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDK--TPVGWIMARVTSDTQRLGEIISWGLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 795 -LVVQTVSAVTIAFTMgLVIAWRLALVMIAVQPVI-IVCFYTRRVLLKSmSKKAIKAqdeSSKLAA---EAVSNVRTITA 869
Cdd:cd18540 122 dLVWGITYMIGILIVM-LILNWKLALIVLAVVPVLaVVSIYFQKKILKA-YRKVRKI---NSRITGafnEGITGAKTTKT 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 870 FSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYIT 930
Cdd:cd18540 197 LVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAIT 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
378-585 |
2.05e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.21 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVisllqrFY------DPLAGEILIDGVSIDKLQVkWLRSQMGL--VSQEPALFAT 449
Cdd:COG1137 20 KDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 -TIKENILfgkedAsmddVVEAAKASNA----------HNF-ISQLPNgyetqvgERGVQMSGGQKQRIAIARAIIKSPT 517
Cdd:COG1137 93 lTVEDNIL-----A----VLELRKLSKKereerleellEEFgITHLRK-------SKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 518 ILLLDEATSALD----SESERVVQEaLENASIGrttILIA-HR----LSTIRNADVISvvkNGHIVETGSHDELMEN 585
Cdd:COG1137 157 FILLDEPFAGVDpiavADIQKIIRH-LKERGIG---VLITdHNvretLGICDRAYIIS---EGKVLAEGTPEEILNN 226
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
715-935 |
2.07e-13 |
|
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: 72.13 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 715 YALSFVGLAVLSFLINISQHY---NFAYMGEYltkRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGd 791
Cdd:cd18543 41 LVLLLLALGVAEAVLSFLRRYlagRLSLGVEH---DLRTDLFAHLQRLDGAFHDR--WQSGQLLSRATSDLSLVQRFLA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 792 rMALVVqTVSAVTIAFTMG--LVIAWRLALV-MIAVQPVIIVCFYTRRVLLKSmskkAIKAQDESSKLAA---EAVSNVR 865
Cdd:cd18543 115 -FGPFL-LGNLLTLVVGLVvmLVLSPPLALVaLASLPPLVLVARRFRRRYFPA----SRRAQDQAGDLATvveESVTGIR 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 866 TITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYITAKALF 935
Cdd:cd18543 189 VVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLV 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
982-1215 |
2.36e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 982 DPDGYETERITGQVEFLDVD---FSYPTRPDV--------IIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIerf 1046
Cdd:PRK15134 260 EPSGDPVPLPEPASPLLDVEqlqVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1047 ydPLKGIVKIDGRDIRSYHLRSL---RRHIALVSQEP--TLFAGTIRENIIYGGVSdkideaeiiEAAKAANAHD----F 1117
Cdd:PRK15134 337 --NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNPRLNVLQIIEEGLR---------VHQPTLSAAQreqqV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1118 ITSLTE-GYDTYCGDR-GVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDsqseRVVQD---ALERVMVGR---TSVV 1189
Cdd:PRK15134 406 IAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLF 481
|
250 260
....*....|....*....|....*..
gi 15229473 1190 IAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:PRK15134 482 ISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
994-1192 |
2.44e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDfsYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyhlRSLRRhi 1073
Cdd:PRK11248 3 QISHLYAD--YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---PGAER-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1074 ALVSQEPTLFA-GTIRENIIYG----GVSdkideaeiiEAAKAANAHDFITSL-TEGYdtycGDRGV-QLSGGQKQRIAI 1146
Cdd:PRK11248 73 GVVFQNEGLLPwRNVQDNVAFGlqlaGVE---------KMQRLEIAHQMLKKVgLEGA----EKRYIwQLSGGQRQRVGI 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229473 1147 ARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM--VGRTSVVIAH 1192
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWqeTGKQVLLITH 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
994-1216 |
2.71e-13 |
|
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: 73.95 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTRpDVIIFKNFSIKIEEGKSTAIVGPSGSGKS----TIIGLIERFYDPLKGIVKIDGRDIRSY---HL 1066
Cdd:COG4172 8 SVEDLSVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLserEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1067 RSLR-RHIALVSQEPT-----LFagTIRENI-----IYGGVSDKideaeiieaakaaNAHDFITSLTE--G-------YD 1126
Cdd:COG4172 87 RRIRgNRIAMIFQEPMtslnpLH--TIGKQIaevlrLHRGLSGA-------------AARARALELLErvGipdperrLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1127 TYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDsqserV-VQ-------DALERVMvgRTSVV-IAHRLSTI 1197
Cdd:COG4172 152 AYPH----QLSGGQRQRVMIAMALANEPDLLIADEPTTALD-----VtVQaqildllKDLQREL--GMALLlITHDLGVV 220
|
250 260
....*....|....*....|
gi 15229473 1198 QN-CDAIAVLDKGKLVERGT 1216
Cdd:COG4172 221 RRfADRVAVMRQGEIVEQGP 240
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
100-288 |
2.78e-13 |
|
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: 71.73 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 100 YCWTRTgeRQTARMREKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILL 179
Cdd:cd18589 60 YNITMS--RIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 180 WRLAI---VGLPfiVLLVIPGLMyGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLG 256
Cdd:cd18589 136 PKLALltaLGLP--LLLLVPKFV-GKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLN 212
|
170 180 190
....*....|....*....|....*....|...
gi 15229473 257 IKQGLAKGITIGSNGIT-FAMWGFMSWYGSRMV 288
Cdd:cd18589 213 KKEAAAYAVSMWTSSFSgLALKVGILYYGGQLV 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
374-584 |
3.44e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.68 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 374 TSIFDDF-CLRVPS-----GKTVALVGGSGSGKSTVISLLQRF--YDPLAGEIL-------------------------- 419
Cdd:TIGR03269 7 TKKFDGKeVLKNISftieeGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 420 -------IDGVSIDKLQVKWLRSQMGLVSQEP-ALFAT-TIKENILFGKEDASMddvvEAAKA-SNAHNFISQlpngyeT 489
Cdd:TIGR03269 87 gtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTfALYGDdTVLDNVLEALEEIGY----EGKEAvGRAVDLIEM------V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 490 QVGER----GVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASI--GRTTILIAHRLSTIRN-A 562
Cdd:TIGR03269 157 QLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlS 236
|
250 260
....*....|....*....|..
gi 15229473 563 DVISVVKNGHIVETGSHDELME 584
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA 258
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1012-1215 |
4.45e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLierfydpLKGIVKIDGRDIR--SYHLRSLRRHIALVSQEPTLFA-GTIR 1088
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRL-------LAGLETPSAGELLagTAPLAEAREDTRLMFQDARLLPwKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1089 ENIIYGGVSDKIDeaeiieaakaaNAHDFITSLteGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDS 1168
Cdd:PRK11247 100 DNVGLGLKGQWRD-----------AALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15229473 1169 QSERVVQDALERVMV--GRTSVVIAHRLStiqncDAIAVLDKGKLVERG 1215
Cdd:PRK11247 167 LTRIEMQDLIESLWQqhGFTVLLVTHDVS-----EAVAMADRVLLIEEG 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1023-1212 |
4.83e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1023 GKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI---RSYHLRSLRRHIALVSQEPTLFAG-TIREN-----IIY 1093
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHHLLMDrTVYDNvaiplIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1094 GGVSDKIDEAEIIeaakaanAHDFITSLTEGYDTycgdrGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQ-SER 1172
Cdd:PRK10908 108 GASGDDIRRRVSA-------ALDKVGLLDKAKNF-----PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAlSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15229473 1173 VVQDALERVMVGRTSVVIAHRLSTIQNCD-AIAVLDKGKLV 1212
Cdd:PRK10908 176 ILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
716-941 |
5.64e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 71.03 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 716 ALSFVGLAVLSFLINISQHYnfayMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDrmaL 795
Cdd:cd18778 47 LGAYLLRALLNFLRIYLNHV----AEQKVVADLRSDLYDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIAD---G 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 796 VVQTVSAVTIAFTMG---LVIAWRLALVMIAVQPVIIVC--FYTRRVllksmSKKAIKAQDESSKLAA---EAVSNVRTI 867
Cdd:cd18778 118 IPQGITNVLTLVGVAiilFSINPKLALLTLIPIPFLALGawLYSKKV-----RPRYRKVREALGELNAllqDNLSGIREI 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 868 TAFSSQERIMKMLEKAQESPRRESIRQS-WFAGFGLAMSqSLTSCTWALDFWYGGRLIQDGYITAKALFETFMIL 941
Cdd:cd18778 193 QAFGREEEEAKRFEALSRRYRKAQLRAMkLWAIFHPLME-FLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYL 266
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
363-582 |
5.97e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 363 NVKFvYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL--QVKWLRSQ---- 436
Cdd:PRK10261 19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRsrQVIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 437 --------MGLVSQEPAL-----------FATTIKENILFGKEDASMD--DVVEAAKASNAHNFISQLPNgyetqvgerg 495
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEakRMLDQVRIPEAQTILSRYPH---------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 496 vQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESE-------RVVQEALenaSIGrtTILIAHRLSTIRN-ADVISV 567
Cdd:PRK10261 168 -QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEM---SMG--VIFITHDMGVVAEiADRVLV 241
|
250
....*....|....*
gi 15229473 568 VKNGHIVETGSHDEL 582
Cdd:PRK10261 242 MYQGEAVETGSVEQI 256
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
959-1184 |
6.54e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 73.36 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 959 AKGSDAVGSVFAVLDRYTSIDP--EDPDgYETERITGQ-------VEFLDVDFSYPTRPdvIIFKNFSIKIEEGKSTAIV 1029
Cdd:PLN03073 465 AKRASLVQSRIKALDRLGHVDAvvNDPD-YKFEFPTPDdrpgppiISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMV 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1030 GPSGSGKSTIIGLIERFYDPLKGIVkidgrdirsyhLRSLRRHIALVSQEptlfagtireniiyggvsdKIDEAEIIEAA 1109
Cdd:PLN03073 542 GPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAVFSQH-------------------HVDGLDLSSNP 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1110 KAANAHDFITSLTEGYDTYCGDRGVQ----------LSGGQKQRIAIARAVLKNPSVLLLDEATSALDsqservvQDALE 1179
Cdd:PLN03073 592 LLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-------LDAVE 664
|
....*
gi 15229473 1180 RVMVG 1184
Cdd:PLN03073 665 ALIQG 669
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
362-585 |
7.49e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 362 KNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILID--GVSIDKLQVKWLRSqMGL 439
Cdd:PRK10895 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRG-IGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 VSQEPALFAT-TIKEN---ILFGKEDASMDDVVEAAKASNAHNFISQLPNGYetqvgerGVQMSGGQKQRIAIARAIIKS 515
Cdd:PRK10895 83 LPQEASIFRRlSVYDNlmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 516 PTILLLDEATSALDSESERVVQEALENASIGRTTILIA-HRL-STIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
388-681 |
1.04e-12 |
|
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: 73.12 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 388 KTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKlQVKWLRSQMGLVSQEPALFA-TTIKENILF-----GK-- 459
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFyaqlkGRsw 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 460 EDASMDdvVEAAKASNahnfisqlpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEA 539
Cdd:TIGR01257 1036 EEAQLE--MEAMLEDT----------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 540 LENASIGRTTILIAHRLStirNADV----ISVVKNGHIVETGShDELMENI--DGQYSTLVH-LQQIEKQdinvsvkigp 612
Cdd:TIGR01257 1104 LLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT-PLFLKNCfgTGFYLTLVRkMKNIQSQ---------- 1169
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 613 isdpskdirNSSRVSTLSRSSSANSVTGPSTIKNLSEDN--KPQLPSFKRLLAMNLPEWKqaLYGCISATL 681
Cdd:TIGR01257 1170 ---------RGGCEGTCSCTSKGFSTRCPARVDEITPEQvlDGDVNELMDLVYHHVPEAK--LVECIGQEL 1229
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
744-968 |
1.20e-12 |
|
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: 70.03 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 744 LTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVVRSLVGDRMALVVQTV--SAVTIAFTMGLviAWRLALVM 821
Cdd:cd18784 67 LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLvkAIGVIVFMFKL--SWQLSLVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 822 IAVQPVIIVC--FYTRrvLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAG 899
Cdd:cd18784 143 LIGLPLIAIVskVYGD--YYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 900 fGLAMSQSLTSCTW-ALDFWYGGRLIQDGYITAKALFETFMILVSTGRVIADAGSMTTDLAKGSDAVGSV 968
Cdd:cd18784 221 -GYVWSNELTELALtVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
382-585 |
1.41e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.75 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQV-KWLRSQMGLVSQEPALFA-TTIKENILFGK 459
Cdd:PRK11614 26 LHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLAMGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 460 EDASMDDVVEAAKasnahNFISQLPNGYETQVgERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALdseSERVVQEA 539
Cdd:PRK11614 106 FFAERDQFQERIK-----WVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---APIIIQQI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 540 LENA----SIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELMEN 585
Cdd:PRK11614 177 FDTIeqlrEQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
65-288 |
1.86e-12 |
|
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: 69.29 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 65 GSSFNTDTFMQSIsknsvALLYVAC-GSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTSTSDVITSV 143
Cdd:cd18590 27 GGEYQHNAFTSAI-----GLMCLFSlGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 144 SSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAE 223
Cdd:cd18590 100 STDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAR 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 224 QAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKQGLAKGITIG-SNGITFAMWGFMSWYGSRMV 288
Cdd:cd18590 180 EAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLvRRVLQLGVQVLMLYCGRQLI 245
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
382-587 |
2.12e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL---QVkwlrSQMGLVS--QEPALFAT-TIKENI 455
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQI----ARMGVVRtfQHVRLFREmTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 456 LfgkedasmddvVEAAKASNAhNFISQLPN--GY---ETQVGERGVQ-----------------MSGGQKQRIAIARAII 513
Cdd:PRK11300 102 L-----------VAQHQQLKT-GLFSGLLKtpAFrraESEALDRAATwlervgllehanrqagnLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 514 KSPTILLLDEATSALDSESERVVQEALEN--ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMENID 587
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAElrNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1005-1212 |
2.21e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 67.29 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1005 PTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIERFYDPlKGIVKIDGRDIRSYHlRSLRRHIALVSQE- 1079
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFA-EKYPGEIIYVSEEd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1080 ---PTLfagTIRENIiyggvsdkideaeiieaakaanahDFITSLtegydtyCGD---RGVqlSGGQKQRIAIARAVLKN 1153
Cdd:cd03233 93 vhfPTL---TVRETL------------------------DFALRC-------KGNefvRGI--SGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1154 PSVLLLDEATSALDSQServvqdALERVMVGRTSVVIAhRLSTIQNC-----------DAIAVLDKGKLV 1212
Cdd:cd03233 137 ASVLCWDNSTRGLDSST------ALEILKCIRTMADVL-KTTTFVSLyqasdeiydlfDKVLVLYEGRQI 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1008-1220 |
2.34e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLR-SLRRHIALVSQE----PTL 1082
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1083 fagTIRENIIYG------GVSDKIDEAEIIEAAKAANAHDFITSLTEGYdtycgdrgvqLSGGQKQRIAIARAVLKNPSV 1156
Cdd:PRK11288 95 ---TVAENLYLGqlphkgGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY----------LSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1157 LLLDEATSALDSQ-SERvvqdaLERVMV-----GRTSVVIAHRLSTI-QNCDAIAVLDKGKLVErgTHSSL 1220
Cdd:PRK11288 162 IAFDEPTSSLSAReIEQ-----LFRVIRelraeGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
360-587 |
2.86e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 360 EFKNVKFVYPSrleTSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVsidklQVKW------L 433
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-----EMRFasttaaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 434 RSQMGLVSQE----PALfatTIKENILFGKEDASMDDVVEAAKASNAHNFISQL-----PNgyeTQVGErgvqMSGGQKQ 504
Cdd:PRK11288 78 AAGVAIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidPD---TPLKY----LSIGQRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 505 RIAIARAIIKSPTILLLDEATSALDS-ESE---RVVQEALENasiGRTTILIAHRLSTI-RNADVISVVKNGHIVETgsH 579
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVAT--F 222
|
....*...
gi 15229473 580 DElMENID 587
Cdd:PRK11288 223 DD-MAQVD 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
999-1226 |
2.89e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 999 DVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGR--DIRSYHLRSLRRHIALV 1076
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1077 SQEP--TLFAGTIRENIIYG----GVSDKIDEAEIIEAAKAANAHDFITSLTEgydtyCgdrgvqLSGGQKQRIAIARAV 1150
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQ-----C------LSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1151 LKNPSVLLLDEATSALDSQSERVVQDALERVMV-GRTSVVIAHRLSTI-QNCDAIAVLDKGKLVERGTHSSLLSKGPT 1226
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
382-578 |
2.97e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDG-VSIDKLQVKWL---RSQMGLVSQEPALFA-TTIKENIL 456
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLppeKRRIGYVFQDARLFPhYKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 457 FG---KEDASMDDVVEAAKasnahnfISQLPNGYEtqvgergVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESE 533
Cdd:PRK11144 99 YGmakSMVAQFDKIVALLG-------IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15229473 534 RVVQEALENAS--IgRTTIL-IAHRLSTI-RNADVISVVKNGHIVETGS 578
Cdd:PRK11144 165 RELLPYLERLAreI-NIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
380-583 |
3.18e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 380 FCLRvpSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWlRSQ-MGLVSQEPAlfaTTIKENILFG 458
Cdd:PRK15112 34 FTLR--EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQrIRMIFQDPS---TSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 459 KE-DASMDDVVEAAKASNAHNFISQLpngyeTQVGERGVQ-------MSGGQKQRIAIARAIIKSPTILLLDEATSALD- 529
Cdd:PRK15112 108 QIlDFPLRLNTDLEPEQREKQIIETL-----RQVGLLPDHasyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDm 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 530 SESERVVQEALE-NASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELM 583
Cdd:PRK15112 183 SMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1023-1236 |
3.34e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1023 GKSTAIVGPSGSGKSTIIGLIE-RFY-DPLKGIVKIDGRDIRsyhlRSLRRHIALVSQEPTLFAG-TIRENIIYGGVsdk 1099
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVRETLVFCSL--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1100 IDEAEIIEAAKAANAHDFITS---LTEGYDTYCGD---RGVqlSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE-R 1172
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISelgLTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyR 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1173 VVQDALERVMVGRTSVVIAHRLST--IQNCDAIAVLDKGKLVERGTHSSLLSkgptgiYFSLVSLQ 1236
Cdd:PLN03211 245 LVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA------YFESVGFS 304
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
362-538 |
3.39e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 362 KNVKFVYPSRLEtsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILI-DGVSIdklqvkwlrsqmGLV 440
Cdd:TIGR03719 8 NRVSKVVPPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV------------GYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 441 SQEPALFAT-TIKENI-------------------LFGKEDASMDDVV-EAAK------ASNAHNFISQL---------P 484
Cdd:TIGR03719 74 PQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAaEQAElqeiidAADAWDLDSQLeiamdalrcP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 485 NGyETQVGErgvqMSGGQKQRIAIARAIIKSPTILLLDEATSALDSES----ERVVQE 538
Cdd:TIGR03719 154 PW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1020-1213 |
3.64e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1020 IEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYH------LRSlrRHIALVSQE----PTLFAgtiRE 1089
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakLRA--KHVGFVFQSfmliPTLNA---LE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NI----IYGGVSDKideaeiieaAKAANAHDFITSLTEGYDTYcgDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PRK10584 108 NVelpaLLRGESSR---------QSRNGAKALLEQLGLGKRLD--HLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1166 LDSQSERVVQD---ALERVMvGRTSVVIAHRLSTIQNCDAIAVLDKGKLVE 1213
Cdd:PRK10584 177 LDRQTGDKIADllfSLNREH-GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-523 |
4.30e-12 |
|
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: 70.21 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 32 WLLMGLGLIGAVGDGFTTPLVLLITSKLmnnIGGSSFNTDTFMQSISknsVALLYVACGSWVVCFLegycwTRTGERQTA 111
Cdd:COG4615 13 WLLLLALLLGLLSGLANAGLIALINQAL---NATGAALARLLLLFAG---LLVLLLLSRLASQLLL-----TRLGQHAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 112 RMREKYLRAVLRQDvgYFDLHVTSTSDVITSVSSDSFVIQDVLSeKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIV 191
Cdd:COG4615 82 RLRLRLSRRILAAP--LERLERIGAARLLAALTEDVRTISQAFV-RLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 192 LLVIPGLMYGRALISISRKIREEYNE---------AGFvAEQAISSVRtvyafsgeRKTIskFSTALQGSVklgikQGLA 262
Cdd:COG4615 159 LGVAGYRLLVRRARRHLRRAREAEDRlfkhfrallEGF-KELKLNRRR--------RRAF--FDEDLQPTA-----ERYR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 263 KGITIGSNGITFAM-WGFMSWYGsrmvmyhgAQGGTVFAVAAAIAIGGVSLGGGLSNLKY-------------FFEAASV 328
Cdd:COG4615 223 DLRIRADTIFALANnWGNLLFFA--------LIGLILFLLPALGWADPAVLSGFVLVLLFlrgplsqlvgalpTLSRANV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 329 -GERIMEVINRVPKIDSDNPDGHKLEKIRG--EVEFKNVKFVYPSRLETSIFD----DFCLRvpSGKTVALVGGSGSGKS 401
Cdd:COG4615 295 aLRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEGFTlgpiDLTIR--RGELVFIVGGNGSGKS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 402 TVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATtikeniLFGKEDASMDDVVEAakasnahnFIS 481
Cdd:COG4615 373 TLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARARE--------LLE 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15229473 482 QLpnGYETQVGERG-----VQMSGGQKQRIAIARAIIKSPTILLLDE 523
Cdd:COG4615 439 RL--ELDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
716-934 |
4.74e-12 |
|
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: 68.28 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 716 ALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMA- 794
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHER--ETSGRIMTRMTSDIDALSELLQTGLVq 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 795 LVVQTVSAVTIAFTMgLVIAWRLALVMIAVQPVIIVC--FYTRRvllksmSKKAIKAQ-DESSKLAA---EAVSNVRTIT 868
Cdd:cd18546 120 LVVSLLTLVGIAVVL-LVLDPRLALVALAALPPLALAtrWFRRR------SSRAYRRArERIAAVNAdlqETLAGIRVVQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 869 AFSSQERIMKMLEKAQESPRRESIR----QSWFAGFglamSQSLTSCTWALDFWYGGRLIQDGYITAKAL 934
Cdd:cd18546 193 AFRRERRNAERFAELSDDYRDARLRaqrlVAIYFPG----VELLGNLATAAVLLVGAWRVAAGTLTVGVL 258
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1008-1210 |
5.99e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYdP---LKGIVKIDGRDIRSYHLR-SLRRHIALVSQEPTLF 1083
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRdTERAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AG-TIRENIIYG------GVSDkideaeiiEAAKAANAHDFITSLTEGYDTYCgdRGVQLSGGQKQRIAIARAVLKNPSV 1156
Cdd:PRK13549 95 KElSVLENIFLGneitpgGIMD--------YDAMYLRAQKLLAQLKLDINPAT--PVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1157 LLLDEATSALDSQSERV----VQDALERvmvGRTSVVIAHRLSTIQN-CDAIAVLDKGK 1210
Cdd:PRK13549 165 LILDEPTASLTESETAVlldiIRDLKAH---GIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1013-1211 |
7.56e-12 |
|
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: 65.15 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKIEEGKSTAIVGPSGSGKS----TIIGLIErfydPLKGIVKIDGRDIRSYHLRSLRRH-IALVSQEPT---LFA 1084
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTelaeALFGLRP----PASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1085 G-TIRENIIyggvsdkideaeiieaakaanahdfITSLtegydtycgdrgvqLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:cd03215 92 DlSVAENIA-------------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1164 SALD--SQSE--RVVQDALERvmvGRTSVVIahrlST-----IQNCDAIAVLDKGKL 1211
Cdd:cd03215 133 RGVDvgAKAEiyRLIRELADA---GKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
378-577 |
8.84e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwLRSQMG--LVSQEPALF-ATTIKEN 454
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIdELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFGK---EDASMDDVVEAAKASNAHNFISqLPNGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSAL-DS 530
Cdd:PRK09700 101 LYIGRhltKKVCGVNIIDWREMRVRAAMML-LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229473 531 ESERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1012-1222 |
1.29e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIERFydplKGIVKIDGRDIR--SYHLRSlRRHIALVSQEPTLFag 1085
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPRD----AGNIIIDDEDISllPLHARA-RRGIGYLPQEASIF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 tiRENIIYGGVSDKIDEAEIIEAAKAANAHDFItsLTEGYDTYCGDR-GVQLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:PRK10895 91 --RRLSVYDNLMAVLQIRDDLSAEQREDRANEL--MEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1165 ALDSQSERVVQDALERVMVGRTSVVIA-HRL-STIQNCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
994-1222 |
1.31e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPT----RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIR--SYHLR 1067
Cdd:PRK15112 6 EVRNLSKTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1068 SLRrhIALVSQEPTLfAGTIRENIiyGGVSD-----KIDEAEIIEAAKAANAHDFITSLTEGYDTYCGdrgvQLSGGQKQ 1142
Cdd:PRK15112 86 SQR--IRMIFQDPST-SLNPRQRI--SQILDfplrlNTDLEPEQREKQIIETLRQVGLLPDHASYYPH----MLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1143 RIAIARAVLKNPSVLLLDEATSALD-SQSERVVQDALE-RVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSS 1219
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
...
gi 15229473 1220 LLS 1222
Cdd:PRK15112 237 VLA 239
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1017-1220 |
1.38e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1017 SIKIEEGKSTAIVGPSGSGKST----IIGLIErfydPLKGIVKIDGRDIRSY---HLRSLRRHIALVSQEPtlFAG---- 1085
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMkddEWRAVRSDIQMIFQDP--LASlnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 -TIRENI-----IY------GGVSDKIDEAEIIEAAK--AAN--AHDFitsltegydtycgdrgvqlSGGQKQRIAIARA 1149
Cdd:PRK15079 115 mTIGEIIaeplrTYhpklsrQEVKDRVKAMMLKVGLLpnLINryPHEF-------------------SGGQCQRIGIARA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1150 VLKNPSVLLLDEATSALD-SQSERVVQ--DALERVMvGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSL 1220
Cdd:PRK15079 176 LILEPKLIICDEPVSALDvSIQAQVVNllQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1015-1222 |
1.49e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.29 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVK-------IDGRDIRSYHLRSLRRHIALVSQEPTLFA-GT 1086
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1087 IRENIiyggvSDKIDEAEIIEAAKAANAHDFITS-LTEGYDTYCGDRGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:TIGR03269 382 VLDNL-----TEAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1165 ALDSQSERVVQDAL--ERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:TIGR03269 457 TMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
715-930 |
1.71e-11 |
|
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: 66.65 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 715 YALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRDENSSgaICSRLAKDANVVRSLVGDRMA 794
Cdd:cd18548 41 TGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSS--LITRLTNDVTQVQNFVMMLLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 795 LVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCFYTrrVLLKSM--SKKAIKAQDESSKLAAEAVSNVRTITAFSS 872
Cdd:cd18548 119 MLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFL--IMKKAIplFKKVQKKLDRLNRVVRENLTGIRVIRAFNR 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 873 QERIMKMLEKAQESPRRESIR-QSWFAGFGLAMSQSLTSCTWALdFWYGGRLIQDGYIT 930
Cdd:cd18548 197 EDYEEERFDKANDDLTDTSLKaGRLMALLNPLMMLIMNLAIVAI-LWFGGHLINAGSLQ 254
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
370-555 |
2.47e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 370 SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFY--DPLAGEILIDGVSIDklqvkwlrsqmglvsQEpalf 447
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG---------------RE---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 448 aTTIKENILfgkEDASMDDVVE---AAKASNAHNFISQLPNgyetqvgergvqMSGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:COG2401 100 -ASLIDAIG---RKGDFKDAVEllnAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|...
gi 15229473 525 TSALDSESERVVQEALENAS--IGRTTILIAHR 555
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1008-1215 |
2.51e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKS----TIIGLIERFYDPLKGIVKIDGRDIRSYHLRSlrRHIALVSQEP--- 1080
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRG--RKIATIMQNPrsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 -----TLFAGTIRENIIYGGVSDK------IDEAEIIEAAKAANAHDFitsltegydtycgdrgvQLSGGQKQRIAIARA 1149
Cdd:PRK10418 92 fnplhTMHTHARETCLALGKPADDatltaaLEAVGLENAARVLKLYPF-----------------EMSGGMLQRMMIALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1150 VLKNPSVLLLDEATSALDSQSERVVQDALERVMVGRTS--VVIAHRLSTIQNC-DAIAVLDKGKLVERG 1215
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
81-298 |
2.74e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 65.97 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 81 SVALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPN 160
Cdd:cd18550 42 ALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 161 FLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNE-AGFVAEQ-AISSVRTVYAFSGE 238
Cdd:cd18550 120 VVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAElNSIMQETlSVSGALLVKLFGRE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 239 RKTISKFSTALQGSVKLGIKQGLAkgitigsnGITFAMWGFMS---------WYGSRMVMYHGAQGGTV 298
Cdd:cd18550 200 DDEAARFARRSRELRDLGVRQALA--------GRWFFAALGLFtaigpalvyWVGGLLVIGGGLTIGTL 260
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
994-1167 |
2.75e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.79 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTRPDVIifKNFSIKIEEGKSTAIVGPSGSGKST----IIGLiERFYDplkGIVKIDGRDIRsyHLRSL 1069
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVI--KGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERITS---GEIWIGGRVVN--ELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1070 RRHIALVSQEPTLFAG-TIRENIIYG----GVS-DKIDEAEIIEAAkaanahdfITSLTEGYDTycgdRGVQLSGGQKQR 1143
Cdd:PRK11650 75 DRDIAMVFQNYALYPHmSVRENMAYGlkirGMPkAEIEERVAEAAR--------ILELEPLLDR----KPRELSGGQRQR 142
|
170 180
....*....|....*....|....
gi 15229473 1144 IAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
715-878 |
3.02e-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: 65.89 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 715 YALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMA 794
Cdd:cd18547 47 ILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDT--HSHGDIMSRVTNDVDNISQALSQSLT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 795 LVVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIvcFYTRRVLLKSmSKKAIKAQDESSKLAA---EAVSNVRTITAFS 871
Cdd:cd18547 125 QLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSL--LVTKFIAKRS-QKYFRKQQKALGELNGyieEMISGQKVVKAFN 201
|
....*..
gi 15229473 872 SQERIMK 878
Cdd:cd18547 202 REEEAIE 208
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1012-1209 |
3.78e-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: 63.42 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKST---------IIGLIErfydplkGIVKIDGRDIRSyhlrSLRRHIALVSQEPTL 1082
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTlldvlagrkTAGVIT-------GEILINGRPLDK----NFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1083 FAG-TIRENIIYggvSDKIdeaeiieaakaanahdfitsltegydtycgdRGvqLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:cd03232 91 SPNlTVREALRF---SALL-------------------------------RG--LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1162 ATSALDSQSERVVQDALERV-MVGRTSVVIAHRLS--TIQNCDAIAVLDKG 1209
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
82-245 |
3.81e-11 |
|
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: 65.59 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 82 VALLYVACG--SWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhvTSTSD-VITSVSSDSFVIQDVLSEKL 158
Cdd:cd18546 41 AAAAYLAVVlaGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE---RETSGrIMTRMTSDIDALSELLQTGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 159 PNFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNE--AGFVaeQAISSVRTVYAFS 236
Cdd:cd18546 118 VQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAvnADLQ--ETLAGIRVVQAFR 195
|
....*....
gi 15229473 237 GERKTISKF 245
Cdd:cd18546 196 RERRNAERF 204
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
358-582 |
4.16e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSRletsifdDFC-----LRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKW 432
Cdd:PRK10522 322 TLELRNVTFAYQDN-------GFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 433 LRSqmglvsqepaLFATTIKENILFgkeDASMDDVVEAAKASNAHNFISQLPNGYETQVGE---RGVQMSGGQKQRIAIA 509
Cdd:PRK10522 395 YRK----------LFSAVFTDFHLF---DQLLGPEGKPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 510 RAIIKSPTILLLDEATSALDSESERVVQEALENA--SIGRTTILIAHRLSTIRNADVISVVKNGHIVE-TGSHDEL 582
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
377-573 |
4.42e-11 |
|
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: 63.22 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 377 FDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQV-KWLRSQMGLVSQEP---ALFAT-TI 451
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkreGLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 452 KENILFGkedasmddvveaakasnahnfisqlpngyetqvgergVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSE 531
Cdd:cd03215 96 AENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15229473 532 SERVVQEAL-ENASIGRTTILIahrlST-----IRNADVISVVKNGHI 573
Cdd:cd03215 139 AKAEIYRLIrELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
737-934 |
4.64e-11 |
|
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: 65.05 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 737 FAYMGEYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVV-RSLVGDRMALVVQTVSAV-TIAFTMGLviA 814
Cdd:cd18590 60 FMCTLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMsRSVALNANVLLRSLVKTLgMLGFMLSL--S 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 815 WRLALVMIAVQPVIIVcfyTRRVLLKSMSKKAIKAQD---ESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRES 891
Cdd:cd18590 136 WQLTLLTLIEMPLTAI---AQKVYNTYHQKLSQAVQDsiaKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLK 212
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15229473 892 IRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYITAKAL 934
Cdd:cd18590 213 DRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSL 255
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1010-1212 |
5.38e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1010 VIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRdiRSYHLRSLRRH---IALVSQEPTLFAG- 1085
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqlgIYLVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 TIRENIIYGGVSDKIDEAEIIEAAKAANAH---DFITSLTEGYDtycgdrgvqlsggqKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:PRK15439 102 SVKENILFGLPKRQASMQKMKQLLAALGCQldlDSSAGSLEVAD--------------RQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1163 TSALD-SQSERVVQDALERVMVGRTSVVIAHRLSTI-QNCDAIAVLDKGKLV 1212
Cdd:PRK15439 168 TASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIA 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1012-1213 |
5.60e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFY--DPLKGIVKIDGRDIrsyhlrslrrhialvSQEptlfaGTIRE 1089
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NIiyGGVSDKIDEAEIIEAAKAANAHDFITSLTEgydtycgdrgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQ 1169
Cdd:COG2401 105 AI--GRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15229473 1170 SERVVQDALERVM--VGRTSVVIAHR---LSTIQNcDAIAVLDKGKLVE 1213
Cdd:COG2401 171 TAKRVARNLQKLArrAGITLVVATHHydvIDDLQP-DLLIFVGYGGVPE 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
369-602 |
5.69e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 369 PSRLETsifddFCLRVPSGKTVALVGGSGSGKSTVIS----LLqrfydPLAGEILIDGVSIDKLQVKWLRSQMG-LVSQE 443
Cdd:PRK03695 9 STRLGP-----LSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 444 PALFATTIkenilFGKEDASMDDVVEAAKASNAHNFISQ---LPNGYETQVGergvQMSGGQKQRIAIARAIIK-SPTI- 518
Cdd:PRK03695 79 TPPFAMPV-----FQYLTLHQPDKTRTEAVASALNEVAEalgLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvWPDIn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 519 -----LLLDEATSALDseserVVQEAL------ENASIGRTTILIAHRLS-TIRNADVISVVKNGHIVETGSHDELM--E 584
Cdd:PRK03695 150 pagqlLLLDEPMNSLD-----VAQQAAldrllsELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLtpE 224
|
250
....*....|....*...
gi 15229473 585 NIDGQYSTLVHLQQIEKQ 602
Cdd:PRK03695 225 NLAQVFGVNFRRLDVEGH 242
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
379-577 |
7.05e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 379 DFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGLVSQEPALFATTIKENILFG 458
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 459 K-------EDASMDD--VVEAAKASnahnfISQLPNGYEtQVGErgvqMSGGQKQRIAIARAIIKSPTILLLDEATSALD 529
Cdd:PRK15056 105 RyghmgwlRRAKKRDrqIVTAALAR-----VDMVEFRHR-QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15229473 530 SESE-RVVQEALENASIGRTTILIAHRLSTIRNADVISVVKNGHIVETG 577
Cdd:PRK15056 175 VKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
331-558 |
7.10e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 331 RIMEVINRVpKIDSDNPDGHKLEKIRGEVEfkNVKFVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQ-R 409
Cdd:PLN03211 41 KFMDVCYRV-KFENMKNKGSNIKRILGHKP--KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 410 FY-DPLAGEILIDGVSIDKLQVKwlrsQMGLVSQEPALFA-TTIKENILFGKEDASMDDVVEAAKASNAHNFISQL--PN 485
Cdd:PLN03211 118 IQgNNFTGTILANNRKPTKQILK----RTGFVTQDDILYPhLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELglTK 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 486 GYETQVGE---RGVqmSGGQKQRIAIARAIIKSPTILLLDEATSALDSESE-RVVQEALENASIGRTTILIAHRLST 558
Cdd:PLN03211 194 CENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
376-581 |
7.88e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.56 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 376 IFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGvsidklQVKWLRS-QMGLvsqEPALfatTIKEN 454
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLElGAGF---HPEL---TGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 455 ILFG--------KE-DASMDDVVEAAkasNAHNFISQlPngyetqvgergVQM-SGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:COG1134 109 IYLNgrllglsrKEiDEKFDEIVEFA---ELGDFIDQ-P-----------VKTySSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 525 TSALDSE----SERVVQEALENasiGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDE 581
Cdd:COG1134 174 LAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
82-299 |
9.93e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 64.03 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 82 VALLYVAC--GSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLP 159
Cdd:cd18545 42 IALLFLALnlVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 160 NFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIpglmygrALISISRKIREEYNEA--------GFVAEqAISSVRT 231
Cdd:cd18545 120 NLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL-------VVFLLRRRARKAWQRVrkkisnlnAYLHE-SISGIRV 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 232 VYAFSGERKTISKFSTALQGSVKLGIKQGLAKGI---TIG-SNGITFAmwgFMSWYGSRMVMYHGAQGGTVF 299
Cdd:cd18545 192 IQSFAREDENEEIFDELNRENRKANMRAVRLNALfwpLVElISALGTA---LVYWYGGKLVLGGAITVGVLV 260
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1012-1170 |
1.28e-10 |
|
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: 61.99 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrSYHLRSLRRHIALVSQEPTLFAG-TIREN 1090
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1091 I-----IYGGVSDKIDEAEIIEaakaanahdfitSLTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:TIGR01189 94 LhfwaaIHGGAQRTIEDALAAV------------GLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
....*
gi 15229473 1166 LDSQS 1170
Cdd:TIGR01189 158 LDKAG 162
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
378-571 |
1.33e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKwlRSQ---MGLVSQEPALFAT-TIKE 453
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--SSQeagIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 454 NILFGKEDAS---------MDDvvEAAKASNAHNfisqLPNGYETQVGErgvqMSGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:PRK10762 99 NIFLGREFVNrfgridwkkMYA--EADKLLARLN----LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 525 TSAL-DSESE---RVVQEALENasiGRTTILIAHRLSTIRN-ADVISVVKNG 571
Cdd:PRK10762 169 TDALtDTETEslfRVIRELKSQ---GRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
747-934 |
1.58e-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: 63.64 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 747 RIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQP 826
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 827 VIIVCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQE----RIMKMLEKAQESPRRESIR---QSWFAG 899
Cdd:cd18589 148 LLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEgeaqRYRQRLQKTYRLNKKEAAAyavSMWTSS 227
|
170 180 190
....*....|....*....|....*....|....*.
gi 15229473 900 F-GLAMSQSLtsctwaldFWYGGRLIQDGYITAKAL 934
Cdd:cd18589 228 FsGLALKVGI--------LYYGGQLVTAGTVSSGDL 255
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
363-563 |
1.64e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 363 NVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWlRSQMGLVSQ 442
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 443 EPALFAT-TIKENILFGKEDAS----MDDVVEAAKASNAHNFisqlPNGYetqvgergvqMSGGQKQRIAIARAIIKSPT 517
Cdd:PRK13540 82 RSGINPYlTLRENCLYDIHFSPgavgITELCRLFSLEHLIDY----PCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15229473 518 ILLLDEATSALDSES-ERVVQEALENASIGRTTILIAHRLSTIRNAD 563
Cdd:PRK13540 148 LWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
365-532 |
1.76e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 365 KFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGE-ILIDGVSIdklqvkwlrsqmGLVSQE 443
Cdd:PRK11819 14 KVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKV------------GYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 444 PALFAT-TIKENI-------------------LFGKEDASMDDVV-EAAK------ASNAHNFISQL---------PNGy 487
Cdd:PRK11819 79 PQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFDALAaEQGElqeiidAADAWDLDSQLeiamdalrcPPW- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15229473 488 ETQVGergvQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSES 532
Cdd:PRK11819 158 DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1016-1222 |
2.02e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1016 FSIKIEEGKSTAIVGPSGSGKSTII----GLIerfydPLKGIVKIDGRDIRSYHLRSLRRHIA-LVSQEPTLFA------ 1084
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLarmaGLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAmpvfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1085 ---------------GTIRENIIYGGVSDKIDeaeiieaakaanahdfiTSLTegydtycgdrgvQLSGGQKQRIAIARA 1149
Cdd:PRK03695 90 ltlhqpdktrteavaSALNEVAEALGLDDKLG-----------------RSVN------------QLSGGEWQRVRLAAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1150 VLK-----NPS--VLLLDEATSALD-SQservvQDALERVMV-----GRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERG 1215
Cdd:PRK03695 141 VLQvwpdiNPAgqLLLLDEPMNSLDvAQ-----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASG 215
|
....*..
gi 15229473 1216 THSSLLS 1222
Cdd:PRK03695 216 RRDEVLT 222
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1023-1198 |
2.23e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.08 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1023 GKSTAIVGPSGSGKSTIIGLIERFYDPL-KGIVKIDGRDIRSYHLRSLRRHIAlvsqeptlfagtireniiyggvsdkid 1101
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1102 eaeiieaakaanahdfitsltegydtycGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALE-- 1179
Cdd:smart00382 55 ----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....
gi 15229473 1180 -----RVMVGRTSVVIAHRLSTIQ 1198
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLG 130
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1009-1212 |
2.33e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFY--DPLKGIVKIDGRDIRSYHLRSL-RRHIALVSQEPTLFAG 1085
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 -TIRENIIYGGvSDKIDEAEIIEAAKAANAHDFITSLTegYDTYCGDRGV-QLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:TIGR02633 93 lSVAENIFLGN-EITLPGGRMAYNAMYLRAKNLLRELQ--LDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1164 SALDSQSERVVQDALERVMV-GRTSVVIAHRLSTIQN-CDAIAVLDKGKLV 1212
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
338-560 |
2.38e-10 |
|
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: 64.77 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 338 RVPKIDSDNPDGHKLEKI--RGEVE-------FKNVKFVYPSrlETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQ 408
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVpgRGIVEyqdngikFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILG 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 409 RFYdPLAGEILidgvSIDKlqvkwlRSQMGLVSQEPALFATTIKENILF--GKEDASMDDVVEAAKASNAHNFisQLPNG 486
Cdd:TIGR00954 500 ELW-PVYGGRL----TKPA------KGKLFYVPQRPYMTLGTLRDQIIYpdSSEDMKRRGLSDKDLEQILDNV--QLTHI 566
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 487 YETQVGERGVQ-----MSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASIgrTTILIAHRLSTIR 560
Cdd:TIGR00954 567 LEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGI--TLFSVSHRKSLWK 643
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
995-1192 |
2.45e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI----RSyHLRSLR 1070
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRS-RLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1071 RHIALVSQEPTLF---------AGTIREN------IIYGGVSDKIDEAeiieaakaanahdfitsltegydtycGDRGV- 1134
Cdd:PRK11831 84 KRMSMLFQSGALFtdmnvfdnvAYPLREHtqlpapLLHSTVMMKLEAV--------------------------GLRGAa 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1135 -----QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERV--MVGRTSVVIAH 1192
Cdd:PRK11831 138 klmpsELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSH 202
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
82-248 |
2.93e-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: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 82 VALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSeKLPNF 161
Cdd:cd18543 43 LLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLA-FGPFL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 162 LMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKT 241
Cdd:cd18543 120 LGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRE 199
|
....*..
gi 15229473 242 ISKFSTA 248
Cdd:cd18543 200 LDRFEAA 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1014-1215 |
3.18e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRS---YHLRSLRRHIALVSQ------------ 1078
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspGKLQALRRDIQFIFQdpyasldprqtv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 -----EPTLFAGTIRENIIYGGVSDKIDEAEIIEAAKAANAHDFitsltegydtycgdrgvqlSGGQKQRIAIARAVLKN 1153
Cdd:PRK10261 421 gdsimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEF-------------------SGGQRQRICIARALALN 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1154 PSVLLLDEATSALD----SQSERVVQDaLERVMvGRTSVVIAHRLSTIQNCD-AIAVLDKGKLVERG 1215
Cdd:PRK10261 482 PKVIIADEAVSALDvsirGQIINLLLD-LQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
923-1195 |
3.21e-10 |
|
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: 64.38 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 923 LIQDgYITAKALFETfmiLVSTGRVIADAGSMTTDLAKGSDAVGSVFAVLDRYTSIDPEDP----------DGYETERIT 992
Cdd:TIGR00954 365 LMQE-FYNNGRLLLK---AADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPrveeiesgreGGRNSNLVP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 993 GQVEFLDVDfsyptrpDVIIFKN--------------FSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDG 1058
Cdd:TIGR00954 441 GRGIVEYQD-------NGIKFENiplvtpngdvliesLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1059 RDirsyhlrslrrHIALVSQEPTLFAGTIRENIIY---------GGVSDKideaeiIEAAKAANAH-DFITSLTEGYDTY 1128
Cdd:TIGR00954 514 KG-----------KLFYVPQRPYMTLGTLRDQIIYpdssedmkrRGLSDK------DLEQILDNVQlTHILEREGGWSAV 576
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1129 CgDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERvmVGRTSVVIAHRLS 1195
Cdd:TIGR00954 577 Q-DWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
370-583 |
3.57e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 370 SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQ-RFYDPLA-------GEILIDG---VSIDKLQVKWLRSQMG 438
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGeplAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQePAlFATTIKENILFGK--------EDASMD-DVVEAAKASnahnfisqlpNGYETQVGERGVQMSGGQKQRIAIA 509
Cdd:PRK13547 90 QAAQ-PA-FAFSAREIVLLGRypharragALTHRDgEIAWQALAL----------AGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 510 RAI---------IKSPTILLLDEATSALD-SESERV---VQEALENASIGRTTILIAHRLSTiRNADVISVVKNGHIVET 576
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLldtVRRLARDWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAH 236
|
....*..
gi 15229473 577 GSHDELM 583
Cdd:PRK13547 237 GAPADVL 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
366-577 |
3.62e-10 |
|
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: 61.58 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 366 FVYPSRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRsQMGLV--SQE 443
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 444 PALFATTIKENILFGKEdasMDDVVEAAKASNAHNFISQLPNGYETQVGERgvQMSGGQKQRIAIARAIIKSPTILLLDE 523
Cdd:cd03267 105 QLWWDLPVIDSFYLLAA---IYDLPPARFKKRLDELSELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 524 ATSALDSESERVVQEAL--ENASIGRTTILIAHRLSTI-RNADVISVVKNGHIVETG 577
Cdd:cd03267 180 PTIGLDVVAQENIRNFLkeYNRERGTTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1015-1222 |
3.89e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHL-RSLRRHIALVSQEPTLFAG-TIRENII 1092
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSRmTVEENLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1093 YGGV-SDKideaeIIEAAKAANAHDFITSLTEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSE 1171
Cdd:PRK11614 103 MGGFfAER-----DQFQERIKWVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1172 RVVQDALERVMV-GRTSVVIAHRLS-TIQNCDAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK11614 174 QQIFDTIEQLREqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
111-245 |
4.80e-10 |
|
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: 62.08 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 111 ARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFI 190
Cdd:cd18549 75 TDMRRDLFEHLQKLSFSFFDNN--KTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 191 VLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKF 245
Cdd:cd18549 153 PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKF 207
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
33-245 |
4.87e-10 |
|
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: 62.04 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 33 LLMGLGLIGAVGDGFTtPLVL--LITSKLMNNIGGSSFNTDTFMQSISKnsVALLYVAcgSWVVCFLEGYCWTRTGERQT 110
Cdd:cd18547 3 LVIILAIISTLLSVLG-PYLLgkAIDLIIEGLGGGGGVDFSGLLRILLL--LLGLYLL--SALFSYLQNRLMARVSQRTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 111 ARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVglpfi 190
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTH--SHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLI----- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 191 VLLVIPgLMYgraLIS--ISRKIREEYNE--------AGFVaEQAISSVRTVYAFSGERKTISKF 245
Cdd:cd18547 151 VLVTVP-LSL---LVTkfIAKRSQKYFRKqqkalgelNGYI-EEMISGQKVVKAFNREEEAIEEF 210
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1007-1209 |
6.04e-10 |
|
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: 60.20 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1007 RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIrSYHLRSLRRHIALVSQEPTLFAG- 1085
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 TIRENIIYggvsdkideaeiieaAKAANAHDFI-TSLTEGYDTYCGDRGV-QLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:cd03231 89 SVLENLRF---------------WHADHSDEQVeEALARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15229473 1164 SALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNCDAIAVLDKG 1209
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1001-1215 |
8.46e-10 |
|
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: 60.42 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1001 DFSYPTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLierfydpLKGIVKIDGRDIRSYHLRSLRRHIALVSQEP 1080
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKI-------LSGLLQPTSGEVRVAGLVPWKRRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 TLFAGtiRENIIYG-GVSDKIDEAEIIEAAKAANAHDFITSLTEGYDtyCG---DRGV-QLSGGQKQRIAIARAVLKNPS 1155
Cdd:cd03267 98 VVFGQ--KTQLWWDlPVIDSFYLLAAIYDLPPARFKKRLDELSELLD--LEellDTPVrQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1156 VLLLDEATSALDSQSERVVQDALERVMVGRTSVVI--AHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
81-289 |
8.77e-10 |
|
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: 61.31 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 81 SVALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSsDSFVIQDVLSEKLPN 160
Cdd:cd18570 45 SIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETR--KTGEIISRFN-DANKIREAISSTTIS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 161 FLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEY--NEAGFVaeQAISSVRTVYAFSGE 238
Cdd:cd18570 122 LFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNaeLNSYLI--ESLKGIETIKSLNAE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 239 ----RKTISKFSTALQGSVKLG---IKQGLAKGIT--IGSNGITfamwgfmsWYGSRMVM 289
Cdd:cd18570 200 eqflKKIEKKFSKLLKKSFKLGklsNLQSSIKGLIslIGSLLIL--------WIGSYLVI 251
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
359-529 |
9.68e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLEtsIFDDFCLRVPSGKTVALVGGSGSGKSTvislLQRFYDPL----AGEILIDGVSIDKLQVKWLR 434
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAGLeritSGEIWIGGRVVNELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 435 SQMglVSQEPALFA-TTIKENILFGKEDASMDD------VVEAAKASNAHNFISQLPNgyetqvgergvQMSGGQKQRIA 507
Cdd:PRK11650 78 IAM--VFQNYALYPhMSVRENMAYGLKIRGMPKaeieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVA 144
|
170 180
....*....|....*....|..
gi 15229473 508 IARAIIKSPTILLLDEATSALD 529
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLD 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
387-577 |
1.22e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 387 GKTVALVGGSGSGKSTVISLLQRFYDPLAGEILI---DGVSIDKL-----QVKWL-RSQMGLVSQEPA------------ 445
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYalseaERRRLlRTEWGFVHQHPRdglrmqvsaggn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 446 ----LFATTIKE--NIlfgKEDAS--MDDV-VEAAKasnahnfISQLPNGYetqvgergvqmSGGQKQRIAIARAIIKSP 516
Cdd:PRK11701 112 igerLMAVGARHygDI---RATAGdwLERVeIDAAR-------IDDLPTTF-----------SGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 517 TILLLDEATSALDSEservVQEALEN------ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETG 577
Cdd:PRK11701 171 RLVFMDEPTGGLDVS----VQARLLDllrglvRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
373-578 |
1.30e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLL--QRFYDPLAGEILIDGVSIDKLQVKwLRSQMGL----------- 439
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 -VSQE--------------------PALFATTIKENIlfgkEDASMDDVveaakasnahnFISQLPN-GYetqvgergvq 497
Cdd:CHL00131 98 gVSNAdflrlaynskrkfqglpeldPLEFLEIINEKL----KLVGMDPS-----------FLSRNVNeGF---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 498 mSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAH--RLSTIRNADVISVVKNGHIV 574
Cdd:CHL00131 153 -SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKII 231
|
....
gi 15229473 575 ETGS 578
Cdd:CHL00131 232 KTGD 235
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1009-1216 |
1.62e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1009 DVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERF--YDPLKGIVKIDGRDIRSY--HLRSlRRHIALVSQEPTLFA 1084
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLepEERA-HLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1085 GTIRENIIYGGVSDKideaEIIEAAKAANAHDFITSLTE-----GYDTYCGDRGVQ--LSGGQKQRIAIARAVLKNPSVL 1157
Cdd:CHL00131 98 GVSNADFLRLAYNSK----RKFQGLPELDPLEFLEIINEklklvGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1158 LLDEATSALDSQSERVVQDALERVMVGRTSVV-IAH--RLSTIQNCDAIAVLDKGKLVERGT 1216
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
386-566 |
2.06e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 386 SGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRSQMGlvsqepalfattikenilfgkedasmd 465
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 466 dvveaakasnahnfisqlpngyetqVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALENASI 545
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180
....*....|....*....|....*...
gi 15229473 546 -------GRTTILIAHRLSTIRNADVIS 566
Cdd:smart00382 109 lllksekNLTVILTTNDEKDLGPALLRR 136
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
369-532 |
2.26e-09 |
|
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: 58.43 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 369 PSRLETSIFDDFCLRVPSGKTVALVGGSGSGKST---VISLLQRFYDPLAGEILIDGVSIDKLQVKWlRSQMGLVSQEPA 445
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 446 LFAT-TIKENILFgkedasmddvveAAKAsNAHNFIsqlpngyetqvgeRGVqmSGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:cd03233 94 HFPTlTVRETLDF------------ALRC-KGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNS 145
|
....*...
gi 15229473 525 TSALDSES 532
Cdd:cd03233 146 TRGLDSST 153
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1015-1222 |
2.36e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKS----TIIGLIerfydPLKGIVKIDGrDIRsYH-----------LRSLR-RHIALVSQ 1078
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSPPVVYPSG-DIR-FHgesllhaseqtLRGVRgNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1079 EP------------------TLFAGTIRENiiyggvsdkideaeiieaakaanAHDFITSltegydtyCGDR-GV----- 1134
Cdd:PRK15134 100 EPmvslnplhtlekqlyevlSLHRGMRREA-----------------------ARGEILN--------CLDRvGIrqaak 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1135 -------QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALE--RVMVGRTSVVIAHRLSTI-QNCDAIA 1204
Cdd:PRK15134 149 rltdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVrKLADRVA 228
|
250
....*....|....*...
gi 15229473 1205 VLDKGKLVERGTHSSLLS 1222
Cdd:PRK15134 229 VMQNGRCVEQNRAATLFS 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
359-542 |
3.11e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILI-DGVsidklqvkwlrsQM 437
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQE-PALFAT-TIKENILFGKEDASMDDVVEAAKA-SNAHNFisqlpNGYETQ--VGergvQMSGGQKQRIAIARAI 512
Cdd:TIGR03719 388 AYVDQSrDALDPNkTVWEEISGGLDIIKLGKREIPSRAyVGRFNF-----KGSDQQkkVG----QLSGGERNRVHLAKTL 458
|
170 180 190
....*....|....*....|....*....|
gi 15229473 513 IKSPTILLLDEATSALDSESERVVQEALEN 542
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLN 488
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
361-558 |
3.21e-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: 58.02 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 361 FKNVKFVYPSRLET-SIFDDFCLRVPSGKTVALVGGSGSGKSTVISLL-QRFYDPL-AGEILIDGVSIDKLqvkwLRSQM 437
Cdd:cd03232 6 WKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLDKN----FQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQEPALFAT-TIKENILFgkedasmddvveAAKAsnahnfisqlpngyetqvgeRGvqMSGGQKQRIAIARAIIKSP 516
Cdd:cd03232 82 GYVEQQDVHSPNlTVREALRF------------SALL--------------------RG--LSVEQRKRLTIGVELAAKP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15229473 517 TILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLST 558
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSA 170
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
370-554 |
3.26e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 370 SRLETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKL------QVKWLRSQMGLvsqE 443
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 444 PALFATtikENILFGKEDASM--DDVVEAAKAsnahnfisqlpngyetQVGERGV------QMSGGQKQRIAIARAIIKS 515
Cdd:PRK13538 87 TELTAL---ENLRFYQRLHGPgdDEALWEALA----------------QVGLAGFedvpvrQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15229473 516 PTILLLDEATSALDSESERVVQEALE-NASIGRTTILIAH 554
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAqHAEQGGMVILTTH 187
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
368-554 |
1.11e-08 |
|
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: 57.42 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 368 YPSRLETsiFDDFCLRVPSG-----KTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSidklqvkwlrsqmglVSQ 442
Cdd:cd03237 3 YPTMKKT--LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 443 EP----ALFATTIKEnILFGKEDASMDDV---VEAAKASnahnfisQLPNGYETQVGErgvqMSGGQKQRIAIARAIIKS 515
Cdd:cd03237 66 KPqyikADYEGTVRD-LLSSITKDFYTHPyfkTEIAKPL-------QIEQILDREVPE----LSGGELQRVAIAACLSKD 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15229473 516 PTILLLDEATSALDSESE----RVVQEALENASigRTTILIAH 554
Cdd:cd03237 134 ADIYLLDEPSAYLDVEQRlmasKVIRRFAENNE--KTAFVVEH 174
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
32-289 |
1.27e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 57.93 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 32 WLLMGLGLIGAVGDGFTTPLVlliTSKLMNNIGGSSfntdTFMQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQTA 111
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWL---IRELVDLVTIGS----KSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIV 191
Cdd:cd18778 74 DLRSDLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 192 LLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKqgLAKGITIGSNG 271
Cdd:cd18778 152 FLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLR--AMKLWAIFHPL 229
|
250 260
....*....|....*....|.
gi 15229473 272 ITFA-MWG--FMSWYGSRMVM 289
Cdd:cd18778 230 MEFLtSLGtvLVLGFGGRLVL 250
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
378-582 |
1.52e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKS----TVISLLQRFYDPLAGEILIDGVSIDKLQVKWLR----SQMGLVSQEPAlfaT 449
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPM---T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEdasmddVVEAAKASNAHNFISQLPNGYE--TQVG------ERGV---QMSGGQKQRIAIARAIIKSPTI 518
Cdd:PRK11022 101 SLNPCYTVGFQ------IMEAIKVHQGGNKKTRRQRAIDllNQVGipdpasRLDVyphQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 519 LLLDEATSALDSESERVVQEAL------ENASIgrttILIAHRLSTI-RNADVISVVKNGHIVETGSHDEL 582
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLlelqqkENMAL----VLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
96-239 |
1.97e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 57.58 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 96 FLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVG 175
Cdd:cd18565 72 YLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAIL 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 176 FILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREeynEAGFVA---EQAISSVRTVYAFSGER 239
Cdd:cd18565 150 FYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVRE---AVGDLNarlENNLSGIAVIKAFTAED 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1008-1215 |
2.27e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI-RSYHLRSLRRHIALVSQEPTLFAG- 1085
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnKLDHKLAAQLGIGIIYQELSVIDEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 TIRENIIYGGVSDK----IDEAEIIEAAKAANAHDFITSLTEGYDTYCGDrgvqLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:PRK09700 96 TVLENLYIGRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1162 ATSALdSQSErvvQDALERVM-----VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:PRK09700 172 PTSSL-TNKE---VDYLFLIMnqlrkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1006-1213 |
3.17e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1006 TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYdP---LKGIVKIDG-----RDIRSyhlrSLRRHIALVS 1077
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGevcrfKDIRD----SEALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1078 QE----PTLfagTIRENIIYG------GVsdkIDEAEIIEAAKAANAHdfiTSLTEGYDTYCGDRGVqlsgGQKQRIAIA 1147
Cdd:NF040905 85 QElaliPYL---SIAENIFLGnerakrGV---IDWNETNRRARELLAK---VGLDESPDTLVTDIGV----GKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1148 RAVLKNPSVLLLDEATSAL-DSQSERVVQDALERVMVGRTSVVIAHRLSTI-QNCDAIAVLDKGKLVE 1213
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
374-600 |
3.45e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 374 TSIFDDFCLRvpSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEIL-----IDGVSIDKLQ----VKWLRSQMGLVSQEP 444
Cdd:PRK10938 18 TLQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQsqfshITRLSFEQLQklvsDEWQRNNTDMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 445 ALFATTIKENILFGKEDasmddvvEAAKASNAHNF-ISQLpngyetqVGERGVQMSGGQKQRIAIARAIIKSPTILLLDE 523
Cdd:PRK10938 96 DDTGRTTAEIIQDEVKD-------PARCEQLAQQFgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 524 ATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMEniDGQYSTLVHLQQIE 600
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ--QALVAQLAHSEQLE 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1003-1176 |
3.65e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.64 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1003 SYPtrPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIiglierfydpLKGIVKIDgRDIRSYHLRSLRRHIALVSQEPTL 1082
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTL----------LRIMAGVD-KDFNGEARPQPGIKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1083 FAG-TIRENI----------------IY-----------------GGVSDKIDEAeiieaakaaNAHDFITSLTEGYDTY 1128
Cdd:TIGR03719 80 DPTkTVRENVeegvaeikdaldrfneISakyaepdadfdklaaeqAELQEIIDAA---------DAWDLDSQLEIAMDAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1129 -C--GDRGVQ-LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQS----ERVVQD 1176
Cdd:TIGR03719 151 rCppWDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1012-1215 |
3.73e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKST----IIGLIERFYDPLKGIVKIDG---RDIRSyHLRSLRRHIA--------LV 1076
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGitpEEIKK-HYRGDVVYNAetdvhfphLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1077 SQEPTLFAGTIRE-NIIYGGVSDKIDEAEIIEAAKAanahdfITSLTEGYDTYCGD---RGVqlSGGQKQRIAIARAVLK 1152
Cdd:TIGR00956 155 VGETLDFAARCKTpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1153 NPSVLLLDEATSALDSQServvqdALERVMVGRTSVVIAHR--LSTIQNC--------DAIAVLDKGKLVERG 1215
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTtpLVAIYQCsqdayelfDKVIVLYEGYQIYFG 293
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
995-1179 |
4.21e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSyHLRSLRRHIA 1074
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 LVSQE----PTLfagTIRENIIY----GGVSDKIDEAEIieaakaanahdfITSLTEGYDTYCGdrgvQLSGGQKQRIAI 1146
Cdd:PRK13540 78 FVGHRsginPYL---TLRENCLYdihfSPGAVGITELCR------------LFSLEHLIDYPCG----LLSSGQKRQVAL 138
|
170 180 190
....*....|....*....|....*....|...
gi 15229473 1147 ARAVLKNPSVLLLDEATSALDSQSERVVQDALE 1179
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
994-1213 |
4.24e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTRpdviifkNFSIK-----IEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRS 1068
Cdd:PRK10522 322 TLELRNVTFAYQDN-------GFSVGpinltIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1069 LRRHIALVSQEPTLF------AGTIRENIIYG------GVSDKIDEaeiieaakaanAHDFITSLtegydtycgdrgvQL 1136
Cdd:PRK10522 395 YRKLFSAVFTDFHLFdqllgpEGKPANPALVEkwlerlKMAHKLEL-----------EDGRISNL-------------KL 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVV-QDALERVM-VGRTSVVIAHRLSTIQNCDAIAVLDKGKLVE 1213
Cdd:PRK10522 451 SKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1014-1223 |
4.56e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.25 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTII----GLIErfydPLKGIVKIDGRDIrsYHLRS-LRRHIALV----SQ----EP 1080
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIkmltGILV----PTSGEVRVLGYVP--FKRRKeFARRIGVVfgqrSQlwwdLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 TL--FAgTIREniIYGgVSDKIDEAEIIEAAKAANAHDFItsltegydtycgDRGV-QLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:COG4586 113 AIdsFR-LLKA--IYR-IPDAEYKKRLDELVELLDLGELL------------DTPVrQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1158 LLDEATSALDSQSERVVQDAL-----ERvmvGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLkeynrER---GTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1011-1222 |
4.90e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1011 IIFKNFSIKIEEGKSTAIVGPSGSGKSTIIG-LIERFYDP-------LKGIVKIDGRDIRSYHLRSLRRHIALVSQ--EP 1080
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 TlFAGTIRENIIYG--------GVSDKIDEAEIIEAAKAANAhdfitsltegyDTYCGDRGVQLSGGQKQRIAIARAVLK 1152
Cdd:PRK13547 95 A-FAFSAREIVLLGrypharraGALTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1153 ---------NPSVLLLDEATSALDSQSERVVQDALERVM----VGRTSVVIAHRLSTiQNCDAIAVLDKGKLVERGTHSS 1219
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPAD 241
|
...
gi 15229473 1220 LLS 1222
Cdd:PRK13547 242 VLT 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
968-1212 |
5.22e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 968 VFAVLDRYT------SIDPEDPDGYETERI----TGQveflDVDFSYPTRPDVI--------------IFKNFSIKIEEG 1023
Cdd:COG1129 203 VFEIADRVTvlrdgrLVGTGPVAELTEDELvrlmVGR----ELEDLFPKRAAAPgevvleveglsvggVVRDVSFSVRAG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1024 KSTAIVGPSGSGKS----TIIGLierfYDPLKGIVKIDGR--DIRSYHlRSLRRHIALVS---QEPTLFAG-TIRENII- 1092
Cdd:COG1129 279 EILGIAGLVGAGRTelarALFGA----DPADSGEIRLDGKpvRIRSPR-DAIRAGIAYVPedrKGEGLVLDlSIRENITl 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1093 --------YGGVSDKideaeiieaAKAANAHDFITSL---TEGYDTYCGdrgvQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:COG1129 354 asldrlsrGGLLDRR---------RERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDE 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1162 ATSALD--SQSE--RVVQDALERvmvGRTSVVIahrlST-----IQNCDAIAVLDKGKLV 1212
Cdd:COG1129 421 PTRGIDvgAKAEiyRLIRELAAE---GKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1013-1236 |
6.03e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.66 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRsyhlRSLRRH-IALV--SQEPTLFAGTIRE 1089
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVpqSEEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NIIYGGVSDKIDEAEIIeaakaaNAHD--FITSLTEGYDT--YCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PRK15056 99 DVVMMGRYGHMGWLRRA------KKRDrqIVTAALARVDMveFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 1166 LDSQSE-RVVQDALERVMVGRTSVVIAHRLSTIQN-CDaIAVLDKGklvergthsSLLSKGPTGIYFSLVSLQ 1236
Cdd:PRK15056 173 VDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEfCD-YTVMVKG---------TVLASGPTETTFTAENLE 235
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
719-883 |
7.18e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 55.56 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 719 FVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMALVVQ 798
Cdd:cd18606 41 YAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDT--TPLGRILNRFSKDTDVLDNELPDSLRMFLY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 799 TVSavTIAFTMGLVIAWrLALVMIAVqPVIIVCFY--------TRRVL--LKSMSKkaikaqdesSKLAA---EAVSNVR 865
Cdd:cd18606 119 TLS--SIIGTFILIIIY-LPWFAIAL-PPLLVLYYfianyyraSSRELkrLESILR---------SFVYAnfsESLSGLS 185
|
170
....*....|....*...
gi 15229473 866 TITAFSSQERIMKMLEKA 883
Cdd:cd18606 186 TIRAYGAQDRFIKKNEKL 203
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
714-930 |
7.71e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. 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). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 55.59 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 714 IYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRlAKDANVVRSLVGDRM 793
Cdd:cd18555 43 VLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFEN--RSSGDLLFR-ANSNVYIRQILSNQV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 794 -ALVVQTVSAVTIAFTMgLVIAWRLALVMIAVQPVIIV-CFYTRRVlLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFS 871
Cdd:cd18555 120 iSLIIDLLLLVIYLIYM-LYYSPLLTLIVLLLGLLIVLlLLLTRKK-IKKLNQEEIVAQTKVQSYLTETLYGIETIKSLG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 872 SQERI----MKMLEKAQESPRRESIRQSWFAGFglamSQSLTSCTWALDFWYGGRLIQDGYIT 930
Cdd:cd18555 198 SEKNIykkwENLFKKQLKAFKKKERLSNILNSI----SSSIQFIAPLLILWIGAYLVINGELT 256
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1014-1203 |
9.93e-08 |
|
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: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTII------GLIERF---------YDPLKGIVKID----------GRDIRS----Y 1064
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLhlkkeqpgnHDRIEGLEHIDkvividqspiGRTPRSnpatY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1065 -----HLRSL-------RRHialvsQEPTLfagtireNIIYGG--VSDKIDEAEIieaakaaNAHDF---ITSLTEGYDT 1127
Cdd:cd03271 92 tgvfdEIRELfcevckgKRY-----NRETL-------EVRYKGksIADVLDMTVE-------EALEFfenIPKIARKLQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1128 YC---------GDRGVQLSGGQKQRIAIARAVLK---NPSVLLLDEATSALDSQSERVVQDALER-VMVGRTSVVIAHRL 1194
Cdd:cd03271 153 LCdvglgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNL 232
|
....*....
gi 15229473 1195 STIQNCDAI 1203
Cdd:cd03271 233 DVIKCADWI 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1012-1167 |
1.05e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKidgrdiRSYHLRslrrhIALVSQ----EPTLFAGTI 1087
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR-----IGYVPQklylDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 RENIIYGGVSDKideaeiieaakaanahDFITSLTEGYDTYCGDRGVQ-LSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:PRK09544 88 RFLRLRPGTKKE----------------DILPALKRVQAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
.
gi 15229473 1167 D 1167
Cdd:PRK09544 152 D 152
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
714-885 |
1.14e-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: 54.82 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 714 IYALSFVGLAVLSFLINISqhynFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRM 793
Cdd:cd18580 44 YAALLVLASVLLVLLRWLL----FVLAGLRASRRLHDKLLRSVLRAPMSFFDT--TPSGRILNRFSKDIGLIDEELPLAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 794 ALVVQTVSAVTIAFTMGLVIAWRLALVMIavqPVIIVCFYTRRVLLKSMskKAIKAQDESSK-----LAAEAVSNVRTIT 868
Cdd:cd18580 118 LDFLQSLFSVLGSLIVIAIVSPYFLIVLP---PLLVVYYLLQRYYLRTS--RQLRRLESESRsplysHFSETLSGLSTIR 192
|
170
....*....|....*..
gi 15229473 869 AFSSQERIMKMLEKAQE 885
Cdd:cd18580 193 AFGWQERFIEENLRLLD 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1016-1192 |
1.15e-07 |
|
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: 54.34 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1016 FSIKIEEGKST-----AIVGPSGSGKSTIIGLierfydpLKGIVKIDGRDIRSyhlrsLRRHIALVSQEPTL-FAGTIRE 1089
Cdd:cd03237 13 FTLEVEGGSISeseviGILGPNGIGKTTFIKM-------LAGVLKPDEGDIEI-----ELDTVSYKPQYIKAdYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1090 NIiyggvSDKIDEAEIIEAAKAANAHDF-ITSLTegydtycgDRGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:cd03237 81 LL-----SSITKDFYTHPYFKTEIAKPLqIEQIL--------DREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180
....*....|....*....|....*..
gi 15229473 1168 SQSERVVQDALERVMVG--RTSVVIAH 1192
Cdd:cd03237 148 VEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1013-1207 |
1.20e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKI-EEGKSTAIVGPSGSGKSTII---------------------GLIERF-----YDPLKGIVKidgRDIRSYH 1065
Cdd:PRK13409 88 FKLYGLPIpKEGKVTGILGPNGIGKTTAVkilsgelipnlgdyeeepswdEVLKRFrgtelQNYFKKLYN---GEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1066 lrslrrHIALVSQEPTLFAGTIRE---NIIYGGVSDKIDEAEIieaakaanahdfITSLTegydtycgDRGV-QLSGGQK 1141
Cdd:PRK13409 165 ------KPQYVDLIPKVFKGKVREllkKVDERGKLDEVVERLG------------LENIL--------DRDIsELSGGEL 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 1142 QRIAIARAVLKNPSVLLLDEATSALDSqSERV-VQDALERVMVGRTSVVIAHRLstiqncdaiAVLD 1207
Cdd:PRK13409 219 QRVAIAAALLRDADFYFFDEPTSYLDI-RQRLnVARLIRELAEGKYVLVVEHDL---------AVLD 275
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
995-1197 |
1.25e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERfyDPLKGI---VKIDGR---------DIR 1062
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGYsndLTLFGRrrgsgetiwDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1063 syhlrslrRHIALVSQEPTL---FAGTIReNIIYGGVSDKIDEAEIIEAAKAANAHDFITSLteGYDTYCGDRGVQ-LSG 1138
Cdd:PRK10938 336 --------KHIGYVSSSLHLdyrVSTSVR-NVILSGFFDSIGIYQAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSW 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1139 GQkQRIA-IARAVLKNPSVLLLDEATSALDSQSERVVQDALErVMV--GRTSVV------------IAHRLSTI 1197
Cdd:PRK10938 405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD-VLIseGETQLLfvshhaedapacITHRLEFV 476
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
378-594 |
1.45e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVKWLRsQMGLV----SQ----------- 442
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlwwdlpaidsf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 443 ---------EPALFATTIKEnilfgkedasMDDVVEaakasnahnfISQLpngYETQVgeRgvQMSGGQKQRIAIARAII 513
Cdd:COG4586 118 rllkaiyriPDAEYKKRLDE----------LVELLD----------LGEL---LDTPV--R--QLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 514 KSPTILLLDEATSALDSESERVVQEAL--ENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELMENIdGQY 590
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLkeYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERF-GPY 249
|
....
gi 15229473 591 STLV 594
Cdd:COG4586 250 KTIV 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
995-1216 |
1.49e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYpTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVK-------------IDGRDI 1061
Cdd:PRK10261 15 VENLNIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1062 RSYHLRSLR-RHIALVSQEPTL-----------FAGTIRENIIYGGVSDKIDEAEIIEAAKAANAHDFITSLTEgydtyc 1129
Cdd:PRK10261 94 SAAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPH------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1130 gdrgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDS-------QSERVVQDALERVMvgrtsVVIAHRLSTIQN-CD 1201
Cdd:PRK10261 168 -----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaqilQLIKVLQKEMSMGV-----IFITHDMGVVAEiAD 237
|
250
....*....|....*
gi 15229473 1202 AIAVLDKGKLVERGT 1216
Cdd:PRK10261 238 RVLVMYQGEAVETGS 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
989-1196 |
1.73e-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: 55.33 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 989 ERITGQV-EFLDVDFSYPTRpdvIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIdGRDIrsyhlr 1067
Cdd:TIGR03719 316 PRLGDKViEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1068 slrrHIALVSQEptlfagtiRENI-----IYGGVSDKIDEAEIIEAAKAANAhdfitsltegydtYCGD---RGV----- 1134
Cdd:TIGR03719 386 ----KLAYVDQS--------RDALdpnktVWEEISGGLDIIKLGKREIPSRA-------------YVGRfnfKGSdqqkk 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1135 --QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERvmVGRTSVVIAH------RLST 1196
Cdd:TIGR03719 441 vgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLN--FAGCAVVISHdrwfldRIAT 508
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
715-1161 |
2.30e-07 |
|
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: 55.19 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 715 YALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVL-----TFE-VGwfdrdensSGAICSRLAKD-ANVVRS 787
Cdd:COG4615 50 LLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILaapleRLErIG--------AARLLAALTEDvRTISQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 788 LVgdRMALVVQtvSAVTIAFTMG--LVIAWRLALVMIAVQPVIIVCFYTRRVLLKSMSKKAIKAQDEsskLaaeavsnvr 865
Cdd:COG4615 122 FV--RLPELLQ--SVALVLGCLAylAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDR---L--------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 866 titafssQERIMKMLEKAQE----SPRRESIRQSWFAG--------FGLAMSQSLTSCTWALDFWYGgrLI--------Q 925
Cdd:COG4615 186 -------FKHFRALLEGFKElklnRRRRRAFFDEDLQPtaeryrdlRIRADTIFALANNWGNLLFFA--LIglilfllpA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 926 DGYITAKALFE-TFMILVSTGRVIADAGSMTTdLAKGSDA---VGSVFAVLDRYTSIDPEDPDGyETERITGQVEFLDVD 1001
Cdd:COG4615 257 LGWADPAVLSGfVLVLLFLRGPLSQLVGALPT-LSRANVAlrkIEELELALAAAEPAAADAAAP-PAPADFQTLELRGVT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1002 FSYPTRPDVIIFK--NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQE 1079
Cdd:COG4615 335 YRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1080 PTLFAGtireniIYGGVSDKIDEAeiieaakaanAHDFI--------TSLTEG-YDTycgdrgVQLSGGQKQRIAIARAV 1150
Cdd:COG4615 415 FHLFDR------LLGLDGEADPAR----------ARELLerleldhkVSVEDGrFST------TDLSQGQRKRLALLVAL 472
|
490
....*....|.
gi 15229473 1151 LKNPSVLLLDE 1161
Cdd:COG4615 473 LEDRPILVFDE 483
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
387-557 |
2.33e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 387 GKTVALVGGSGSGKSTVISLL--QRFYDPLAGEILIDGVSidKLQVKWLR-----SQMGLVSQEpalfaTTIKENILF-- 457
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFP--KKQETFARisgycEQNDIHSPQ-----VTVRESLIYsa 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 458 --------GKEDASM--DDVVEAAKASNAHNFISQLPngyetqvGERGvqMSGGQKQRIAIARAIIKSPTILLLDEATSA 527
Cdd:PLN03140 979 flrlpkevSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190
....*....|....*....|....*....|.
gi 15229473 528 LDSESERVVQEALENA-SIGRTTILIAHRLS 557
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTvDTGRTVVCTIHQPS 1080
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1015-1216 |
2.60e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDI--------------RSY-HLRSLRRHIA----L 1075
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVienlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1076 VSQ----EPTLFAGTIRENIIYGGVSDKIDEAeiieaakaanAH--DFItSLTEGYDTYCGDrgvqLSGGQKQRIAIARA 1149
Cdd:PRK11300 103 VAQhqqlKTGLFSGLLKTPAFRRAESEALDRA----------ATwlERV-GLLEHANRQAGN----LAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1150 VLKNPSVLLLDEATSALDSQSERVVQDALE--RVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERGT 1216
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
387-554 |
2.65e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 387 GKTVALVGGSGSGKSTVISLLQrfydplaGEILIDGVSIdKLQVKWlrsQMGLVSQE-PALFATTIKENILFGKEDASMD 465
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLK-------NEISADGGSY-TFPGNW---QLAWVNQEtPALPQPALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 466 DVVEAAKASNAHNFISQLPN---------------------GYETQVGERGVQ-MSGGQKQRIAIARAIIKSPTILLLDE 523
Cdd:PRK10636 96 AQLHDANERNDGHAIATIHGkldaidawtirsraasllhglGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190
....*....|....*....|....*....|.
gi 15229473 524 ATSALDSESERVVQEALENASigRTTILIAH 554
Cdd:PRK10636 176 PTNHLDLDAVIWLEKWLKSYQ--GTLILISH 204
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
720-949 |
2.96e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 53.74 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 720 VGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLaKDANVVRSLVGDRMALVVQT 799
Cdd:cd18566 49 VIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFER--EPSGAHLERL-NSLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 800 VSAVTIAFTMGLVIAWRLALVMIAVQPVIIVCFYTRRVLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSS----QER 875
Cdd:cd18566 126 LPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMepqmLRR 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 876 IMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTwaldFWYGGRLIQDGYITAKALFeTFMILVstGRVIA 949
Cdd:cd18566 206 YERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAV----VAFGALLVINGDLTVGALI-ACTMLS--GRVLQ 272
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
363-582 |
3.17e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.96 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 363 NVKFVYPSRLETSIFD-DFCLRvpSGKTVALVGGSGSGKS-TVISLLQRFYDP--LAGEILIDGVSIDKL---QVKWLRS 435
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDlNFSLR--AGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLpekELNKLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 436 -QMGLVSQEPAlfaTT------IKENIL--------FGKEDASMDDV--VEAAKASNAHNFISQLPNgyetqvgergvQM 498
Cdd:PRK09473 97 eQISMIFQDPM---TSlnpymrVGEQLMevlmlhkgMSKAEAFEESVrmLDAVKMPEARKRMKMYPH-----------EF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 499 SGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE------NASIgrttILIAHRLSTIRN-ADVISVVKNG 571
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelkrefNTAI----IMITHDLGVVAGiCDKVLVMYAG 238
|
250
....*....|.
gi 15229473 572 HIVETGSHDEL 582
Cdd:PRK09473 239 RTMEYGNARDV 249
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
359-529 |
3.49e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.81 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDgvsiDKLQVkwlrsqmG 438
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRI-------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 439 LVSQEPALFAT---TIKENILFgKEDASMDDVVEAAKASNAHNFISQlpngyETQvgergvQMSGGQKQRIAIARAIIKS 515
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDA-----PMQ------KLSGGETQRVLLARALLNR 138
|
170
....*....|....
gi 15229473 516 PTILLLDEATSALD 529
Cdd:PRK09544 139 PQLLVLDEPTQGVD 152
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
994-1216 |
3.89e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.59 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTRPdviiFK---NFSIKIEEGKSTAIVGPSGSGKS----TIIGLIERFYDPLKGIVKIDGRDIRSYHL 1066
Cdd:PRK11022 5 NVDKLSVHFGDESAP----FRavdRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1067 RSLRR----HIALVSQEPTL-------FAGTIRENI-IYGGVSDKIDEAEIIEAAKAANAHDFITSLtegyDTYCGdrgv 1134
Cdd:PRK11022 81 KERRNlvgaEVAMIFQDPMTslnpcytVGFQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIPDPASRL----DVYPH---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1135 QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDAL------ERVMVgrtsVVIAHRLSTI-QNCDAIAVLD 1207
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLlelqqkENMAL----VLITHDLALVaEAAHKIIVMY 228
|
....*....
gi 15229473 1208 KGKLVERGT 1216
Cdd:PRK11022 229 AGQVVETGK 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1007-1180 |
3.95e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.11 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1007 RPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIR----SYHlRSLrrhialvsqeptL 1082
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYH-QDL------------L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1083 FAG---------TIRENI-IYGGVSDKIDEAEIIEAAKAANAHDFitsltEgyDTYCGdrgvQLSGGQKQRIAIARAVLK 1152
Cdd:PRK13538 78 YLGhqpgiktelTALENLrFYQRLHGPGDDEALWEALAQVGLAGF-----E--DVPVR----QLSAGQQRRVALARLWLT 146
|
170 180
....*....|....*....|....*...
gi 15229473 1153 NPSVLLLDEATSALDSQSERVVQDALER 1180
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
382-578 |
4.20e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 52.62 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 382 LRVPSGKTVALVGGSGSGKSTVI------SLLQRFY----DPLAGEILIDGVSIDKLQVkwlrsqmglVSQEP------- 444
Cdd:cd03271 16 VDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHlkkeQPGNHDRIEGLEHIDKVIV---------IDQSPigrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 445 ------ALFaTTIKEniLF-----GK-----------EDASMDDVVEAAkASNAHNFISQLPN-------------GYeT 489
Cdd:cd03271 87 npatytGVF-DEIRE--LFcevckGKrynretlevryKGKSIADVLDMT-VEEALEFFENIPKiarklqtlcdvglGY-I 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 490 QVGERGVQMSGGQKQRIAIARAIIK---SPTILLLDEATSALDSESER----VVQEALENasiGRTTILIAHRLSTIRNA 562
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKklleVLQRLVDK---GNTVVVIEHNLDVIKCA 238
|
250 260
....*....|....*....|..
gi 15229473 563 D-VISV-----VKNGHIVETGS 578
Cdd:cd03271 239 DwIIDLgpeggDGGGQVVASGT 260
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
377-582 |
4.82e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.87 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 377 FDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQVK-WLRSQMGLVS---QEPALFAT-TI 451
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrKGEGLVLDlSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 452 KENILFgkedASMDDVV------EAAKASNAHNFISQL---PNGYETQVGergvQMSGGQKQRIAIARAIIKSPTILLLD 522
Cdd:COG1129 348 RENITL----ASLDRLSrgglldRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 523 EATSALD----SESERVVQEALENasiGRTTILIahrlST-----IRNADVISVVKNGHIVETGSHDEL 582
Cdd:COG1129 420 EPTRGIDvgakAEIYRLIRELAAE---GKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1013-1207 |
6.15e-07 |
|
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: 53.63 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKI-EEGKSTAIVGPSGSGKSTIIGL---------------------IERF-----YDPLKGIVKidgRDIRSYH 1065
Cdd:COG1245 88 FRLYGLPVpKKGKVTGILGPNGIGKSTALKIlsgelkpnlgdydeepswdevLKRFrgtelQDYFKKLAN---GEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1066 lrslrrHIALVSQEPTLFAGTIREniiyggVSDKIDEAEiieaakaaNAHDFIT--SLTEGYDtycgdRGV-QLSGGQKQ 1142
Cdd:COG1245 165 ------KPQYVDLIPKVFKGTVRE------LLEKVDERG--------KLDELAEklGLENILD-----RDIsELSGGELQ 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1143 RIAIARAVLKNPSVLLLDEATSALD-SQ---SERVVQDALERvmvGRTSVVIAHRLstiqncdaiAVLD 1207
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLDiYQrlnVARLIRELAEE---GKYVLVVEHDL---------AILD 276
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1008-1212 |
7.03e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLR-SLRRHIALVSQEPTLFAG- 1085
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKsSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 TIRENIIYG----GVSDKIDEAEIIEAAKAANAHdfiTSLTEGYDTYCGDrgvqLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:PRK10762 95 TIAENIFLGrefvNRFGRIDWKKMYAEADKLLAR---LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1162 ATSAL-DSQSE---RVVQDALERvmvGRTSVVIAHRLSTI-QNCDAIAVLDKGKLV 1212
Cdd:PRK10762 168 PTDALtDTETEslfRVIRELKSQ---GRGIVYISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
74-298 |
7.24e-07 |
|
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: 52.40 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 74 MQSISKNSVALLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlHVtSTSDVITSVSSDSFVIQDV 153
Cdd:cd18548 35 LSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID-KF-GTSSLITRLTNDVTQVQNF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 154 LSEKLPNFLMSASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRALISISRKIREEYNEAGFVAEQAISSVRTVY 233
Cdd:cd18548 113 VMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIR 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 234 AFSGERKTISKFSTALQGSVKLGIKqgLAKGITIGSNGITFAMWGFM---SWYGSRMVMYHGAQGGTV 298
Cdd:cd18548 193 AFNREDYEEERFDKANDDLTDTSLK--AGRLMALLNPLMMLIMNLAIvaiLWFGGHLINAGSLQVGDL 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
378-586 |
9.13e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSID-KLQVKWLRSQMGLVSQEPALF-ATTIKENI 455
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 456 LFGKEDASMDDVVEAAKASNAHNFISQLpnGYETQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALdseSERV 535
Cdd:PRK10982 95 WLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 536 VQ------EALENASIGrtTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL-MENI 586
Cdd:PRK10982 170 VNhlftiiRKLKERGCG--IVYISHKMEEIFQlCDEITILRDGQWIATQPLAGLtMDKI 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
367-556 |
9.42e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.48 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 367 VYPSRLETSIfDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIdKLQVKWLRSQMGLVSQEPAL 446
Cdd:TIGR01257 1946 VYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 447 fattikENILFGKEDASMDDVVEAAKASNahnfISQLPN------GYETQVGERGVQMSGGQKQRIAIARAIIKSPTILL 520
Cdd:TIGR01257 2024 ------DDLLTGREHLYLYARLRGVPAEE----IEKVANwsiqslGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190
....*....|....*....|....*....|....*....
gi 15229473 521 LDEATSALDSESERVVQEALenASI---GRTTILIAHRL 556
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTI--VSIireGRAVVLTSHSM 2130
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
716-927 |
1.01e-06 |
|
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: 52.18 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 716 ALSFVGLAVLSFLINISQHyNFAYmgeYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVVRSLVGDRMAL 795
Cdd:cd18565 61 VAAFLLESLFQYLSGVLWR-RFAQ---RVQHDLRTDTYDHVQRLDMAFFE--DRQTGDLMSVLNNDVNQLERFLDDGANS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 796 VVQTVSAVTIAFTMGLVIAWRLALVMIAVQPVIIVC--FYTRRVllksmSKKAIKAQDESSKLAA---EAVSNVRTITAF 870
Cdd:cd18565 135 IIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGtyWFQRRI-----EPRYRAVREAVGDLNArleNNLSGIAVIKAF 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 871 SSQERIMKMLEKAQESPR---RESIRQSwfAGFGLAMsQSLTSCTWALDFWYGGRLIQDG 927
Cdd:cd18565 210 TAEDFERERVADASEEYRdanWRAIRLR--AAFFPVI-RLVAGAGFVATFVVGGYWVLDG 266
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1014-1212 |
2.32e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKS----TIIGLIErfydPLKGIVKIDGRDIRSYHLRSLRRH-IALVSQEPT---LFAG 1085
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSelaeALAGLRP----PASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLgrgLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 -TIRENIIYGGVSDK-------IDEAEiieaakaanAHDFITSLTEGYDTYCGDRGV---QLSGGQKQRIAIARAVLKNP 1154
Cdd:COG3845 351 mSVAENLILGRYRRPpfsrggfLDRKA---------IRAFAEELIEEFDVRTPGPDTparSLSGGNQQKVILARELSRDP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1155 SVLLLDEATSALDSQSERVVQDAL-ERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLV 1212
Cdd:COG3845 422 KLLIAAQPTRGLDVGAIEFIHQRLlELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1017-1222 |
2.63e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1017 SIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSL---------RRHIALVSQEPTLFAGTI 1087
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLqklvsdewqRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1088 REnIIYGGVSDkideaeiiEAAKAANAHDF-ITSLTEgydtycgDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:PRK10938 103 AE-IIQDEVKD--------PARCEQLAQQFgITALLD-------RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 1167 DSQSERVVQDALERVMV-GRTSVVIAHRLSTIQNC-DAIAVLDKGKLVERGTHSSLLS 1222
Cdd:PRK10938 167 DVASRQQLAELLASLHQsGITLVLVLNRFDEIPDFvQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
373-567 |
2.66e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVaLVGGSGSGKSTVISLLQRFYDPLAGEILIDGVSIDKLQ---VKWLRSQMGLVSQepalfaT 449
Cdd:PRK13541 13 QKNLFDLSITFLPSAITY-IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLE------M 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDASMDDVVEAAkasnAHNFISQlpngyeTQVGERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALD 529
Cdd:PRK13541 86 TVFENLKFWSEIYNSAETLYAA----IHYFKLH------DLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 15229473 530 SESERVVQEALE-NASIGRTTILIAHRLSTIRNADVISV 567
Cdd:PRK13541 156 KENRDLLNNLIVmKANSGGIVLLSSHLESSIKSAQILQL 194
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1013-1215 |
2.83e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.31 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYHLRSL----RRHIA-----LVSQEP--- 1080
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLLrtewgFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1081 ---TLFAG-TIRENII------YGGV--------------SDKIDeaeiieaakaanahdfitsltegydtycgDRGVQL 1136
Cdd:PRK11701 102 lrmQVSAGgNIGERLMavgarhYGDIratagdwlerveidAARID-----------------------------DLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALD-SQSERVVQdaLERVMVGRT--SVVI-----------AHRLstiqncda 1202
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvSVQARLLD--LLRGLVRELglAVVIvthdlavarllAHRL-------- 222
|
250
....*....|...
gi 15229473 1203 iAVLDKGKLVERG 1215
Cdd:PRK11701 223 -LVMKQGRVVESG 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
377-568 |
4.03e-06 |
|
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: 49.67 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 377 FDDFCLRVP-SGKTVALVGGSGSGKSTVISLLQ--------RFYDPLAGEILIDGVSIDKLQ---VKWLRSQMGL----- 439
Cdd:cd03236 15 FKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDEFRGSELQnyfTKLLEGDVKVivkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 440 -VSQEPALFATTIKENILFGKEDASMDDVVEAAKAsnahnfisqlpngyeTQVGERGV-QMSGGQKQRIAIARAIIKSPT 517
Cdd:cd03236 95 yVDLIPKAVKGKVGELLKKKDERGKLDELVDQLEL---------------RHVLDRNIdQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 518 ILLLDEATSALDSESE----RVVQEALENasiGRTTILIAHRLSTIRN-ADVISVV 568
Cdd:cd03236 160 FYFFDEPSSYLDIKQRlnaaRLIRELAED---DNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1008-1170 |
4.44e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIiglierfydpLK---GIVK-IDGRDIRSYHLRslrrhIALVSQEPTLF 1083
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTL----------LRimaGVDKeFEGEARPAPGIK-----VGYLPQEPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AG-TIRENI----------------IY-----------------GGVSDKIDEAeiieaakaaNAHDFITSLTEGYDTY- 1128
Cdd:PRK11819 83 PEkTVRENVeegvaevkaaldrfneIYaayaepdadfdalaaeqGELQEIIDAA---------DAWDLDSQLEIAMDALr 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15229473 1129 C--GDRGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQS 1170
Cdd:PRK11819 154 CppWDAKVtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
994-1216 |
4.74e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 994 QVEFLDVDFSYPTrPDVIIFKNFSIKIEEGKSTAIVGPSGSGKS----TIIGLIERfYDPLKGIVKIDGRDI---RSYHL 1066
Cdd:PRK09473 14 DVKDLRVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREIlnlPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1067 RSLR-RHIALVSQEP-TLFAGTIREN-------IIYGGVSDK---------IDEAEIIEAAKAAN--AHDFitsltegyd 1126
Cdd:PRK09473 92 NKLRaEQISMIFQDPmTSLNPYMRVGeqlmevlMLHKGMSKAeafeesvrmLDAVKMPEARKRMKmyPHEF--------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1127 tycgdrgvqlSGGQKQRIAIARAVLKNPSVLLLDEATSALDSqserVVQ-------DALERVMvgRTSVV-IAHRLSTIQ 1198
Cdd:PRK09473 163 ----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDV----TVQaqimtllNELKREF--NTAIImITHDLGVVA 226
|
250
....*....|....*....
gi 15229473 1199 N-CDAIAVLDKGKLVERGT 1216
Cdd:PRK09473 227 GiCDKVLVMYAGRTMEYGN 245
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1136-1212 |
5.29e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1136 LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQServvQDALERVMVG-RTSVV-IAHRLSTIQN-CDAIAVLDKGKLV 1212
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTfQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-566 |
5.31e-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: 50.55 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 358 EVEFKNVKFVYPSrLETSiFDDFCLRVPSGK-----TVALVGGSGSGKSTVISLLqrfydplAGEILIDGVSIDKlQVKw 432
Cdd:COG1245 334 REKEEETLVEYPD-LTKS-YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDE-DLK- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 433 lrsqmglVSQEPAlfattikenilFGKEDASMDdVVEAAKASNAHNFIS-----------QLPNGYETQVGErgvqMSGG 501
Cdd:COG1245 403 -------ISYKPQ-----------YISPDYDGT-VEEFLRSANTDDFGSsyykteiikplGLEKLLDKNVKD----LSGG 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 502 QKQRIAIARAIIKSPTILLLDEATSALDSESE----RVVQEALENAsiGRTTILIAHRLSTIrnaDVIS 566
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRRFAENR--GKTAMVVDHDIYLI---DYIS 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
373-540 |
5.64e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEI-LIDGVSIDKL---QVKWLRSQMGLVsQEPALFA 448
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFaqhQLEFLRADESPL-QHLARLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 449 TTIKENIL------FG-KEDasmddvveaakasnahnfisqlpngyetQVGERGVQMSGGQKQRIAIARAIIKSPTILLL 521
Cdd:PRK10636 403 PQELEQKLrdylggFGfQGD----------------------------KVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170
....*....|....*....
gi 15229473 522 DEATSALDSESERVVQEAL 540
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEAL 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
359-542 |
5.84e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRLetsIFDDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILI-DGVsidklqvkwlrsQM 437
Cdd:PRK11819 325 IEAENLSKSFGDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETV------------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 438 GLVSQ-----EPAlfaTTIKENILFGkedasmDDVVEAAK---ASNAH----NFisqlpNGYETQ--VGergvQMSGGQK 503
Cdd:PRK11819 390 AYVDQsrdalDPN---KTVWEEISGG------LDIIKVGNreiPSRAYvgrfNF-----KGGDQQkkVG----VLSGGER 451
|
170 180 190
....*....|....*....|....*....|....*....
gi 15229473 504 QRIAIARAIIKSPTILLLDEATSALDSESERVVQEALEN 542
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1013-1195 |
9.55e-06 |
|
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: 48.52 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKI-EEGKSTAIVGPSGSGKSTIIGLIE--------RFYDP--LKGIVK-IDGRDIRSYHLRSLRRHIAL----- 1075
Cdd:cd03236 15 FKLHRLPVpREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPpdWDEILDeFRGSELQNYFTKLLEGDVKVivkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1076 -VSQEPTLFAGTIRENIiyggvsDKIDEaeiieaakaanahdfitslTEGYDTYCG--------DRGV-QLSGGQKQRIA 1145
Cdd:cd03236 95 yVDLIPKAVKGKVGELL------KKKDE-------------------RGKLDELVDqlelrhvlDRNIdQLSGGELQRVA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1146 IARAVLKNPSVLLLDEATSALD-SQSERVVQDALERVMVGRTSVVIAHRLS 1195
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDiKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
377-536 |
1.12e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 377 FDDFCLRVPSGK-----TVALVGGSGSGKSTVISLLqrfydplAGEILIDGVSIDKlQVKwlrsqmglVSQEPalfatti 451
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLL-------AGVLKPDEGEVDP-ELK--------ISYKP------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 452 keNILFGKEDASMDDVVEAAKASNAHNFIS-------QLPNGYETQVGErgvqMSGGQKQRIAIARAIIKSPTILLLDEA 524
Cdd:PRK13409 407 --QYIKPDYDGTVEDLLRSITDDLGSSYYKseiikplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170
....*....|..
gi 15229473 525 TSALDSEsERVV 536
Cdd:PRK13409 481 SAHLDVE-QRLA 491
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
966-1170 |
1.18e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 966 GSVFAVLDrYTSIDPEDPDGYETERITGQVEFL--DVDFSYPTRPDV-IIFKNFSIKIEEGKSTAIVGPSGSGKSTII-- 1040
Cdd:TIGR00956 730 GEVLGSTD-LTDESDDVNDEKDMEKESGEDIFHwrNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTTLLnv 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1041 -------GLIErfydplKGIVKIDGRDIRSyhlrSLRRHIALVSQE----PTLfagTIRENIIYGG-------VSDKide 1102
Cdd:TIGR00956 809 laervttGVIT------GGDRLVNGRPLDS----SFQRSIGYVQQQdlhlPTS---TVRESLRFSAylrqpksVSKS--- 872
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1103 aeiieaakaaNAHDFITS------LTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLL-LDEATSALDSQS 1170
Cdd:TIGR00956 873 ----------EKMEYVEEviklleMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1137-1223 |
1.41e-05 |
|
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: 49.63 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVM-VGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVER 1214
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCL 2151
|
....*....
gi 15229473 1215 GTHSSLLSK 1223
Cdd:TIGR01257 2152 GTIQHLKSK 2160
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1134-1197 |
1.49e-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: 1.49e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1134 VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRLSTI 1197
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVL 135
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
113-289 |
1.55e-05 |
|
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: 48.18 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 113 MREKYLRAVLRQDVGYFDLHvtSTSDVITSVSSDSFVIQDVLSeklPNFLMSA-STFVGSYIVGFILL--WRLAIVGL-- 187
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKN--RTGDLMARATNDLNAVRMALG---PGILYLVdALFLGVLVLVMMFTisPKLTLIALlp 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 188 -PFIVLLVIpglMYGRALISISRKIREEYNE-AGFVAEqAISSVRTVYAFSGERKTISKFSTALQGSVKLGIKqgLAKgi 265
Cdd:cd18541 150 lPLLALLVY---RLGKKIHKRFRKVQEAFSDlSDRVQE-SFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR--LAR-- 221
|
170 180 190
....*....|....*....|....*....|..
gi 15229473 266 tigSNGITFAMWGFMS--------WYGSRMVM 289
Cdd:cd18541 222 ---VDALFFPLIGLLIglsflivlWYGGRLVI 250
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1023-1227 |
1.78e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1023 GKSTAIVGPSGSGKSTIIglierfyDPLKGIVK---IDGrDIRSYHLRSLRRHIALVS--------QEPTLfagTIRENI 1091
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLM-------DVLAGRKTggyIEG-DIRISGFPKKQETFARISgyceqndiHSPQV---TVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1092 IYggvSDKIDEAEIIEAAKAANAHDFITSLTEG---YDTYCGDRGVQ-LSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PLN03140 975 IY---SAFLRLPKEVSKEEKMMFVDEVMELVELdnlKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 1168 SQSERVVQDALER-VMVGRTSVVIAHRLSTiqncDAIAVLDKGKLVERGTHssLLSKGPTG 1227
Cdd:PLN03140 1052 ARAAAIVMRTVRNtVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ--VIYSGPLG 1106
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
497-583 |
1.79e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 497 QMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALE--NASIGRTTILIAHRLSTIRN-ADVISVVKNGHI 573
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 15229473 574 VETGSHDELM 583
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
384-565 |
1.88e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 384 VPSGKTVALVGGSGSGKST-------------VISLLQRFYDPLAgeilidgVSIDKLQvkwLRSQMGLvsqepalfatt 450
Cdd:cd03238 18 IPLNVLVVVTGVSGSGKSTlvneglyasgkarLISFLPKFSRNKL-------IFIDQLQ---FLIDVGL----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 451 ikenilfgkedasmddvveaakasnahnfisqlpnGYETqVGERGVQMSGGQKQRIAIARAIIKSP--TILLLDEATSAL 528
Cdd:cd03238 77 -----------------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGL 120
|
170 180 190
....*....|....*....|....*....|....*...
gi 15229473 529 DSESERVVQEALEN-ASIGRTTILIAHRLSTIRNADVI 565
Cdd:cd03238 121 HQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWI 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1013-1197 |
1.94e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKIEEGKS-----TAIVGPSGSGKSTIIGLierfydpLKGIVKIDGRDIrsyhLRSLRrhialVSQEP----TLF 1083
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKL-------LAGVLKPDEGEV----DPELK-----ISYKPqyikPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AGTIRENIiyGGVSDKIDEAEIIeaakaanaHDFIT--SLTEGYDTYCGDrgvqLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:PRK13409 414 DGTVEDLL--RSITDDLGSSYYK--------SEIIKplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190
....*....|....*....|....*....|....*....
gi 15229473 1162 ATSALDSqSERV-VQDALERVMVGR--TSVVIAHRLSTI 1197
Cdd:PRK13409 480 PSAHLDV-EQRLaVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
487-553 |
2.02e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 2.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 487 YETQVGE---RGVqmSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEAL-ENASIGRTTILIA 553
Cdd:TIGR00956 198 RNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALkTSANILDTTPLVA 266
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1013-1197 |
2.08e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.63 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1013 FKNFSIKIEEGK-----STAIVGPSGSGKSTIIGLierfydpLKGIVKIDGRDIRSyhlrSLRrhialVSQEP----TLF 1083
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKI-------LAGVLKPDEGEVDE----DLK-----ISYKPqyisPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1084 AGTIREnIIYGGVSDKIDEAEIIeaakaanaHDFIT--SLTEGYDTYCGDrgvqLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:COG1245 415 DGTVEE-FLRSANTDDFGSSYYK--------TEIIKplGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|....*....
gi 15229473 1162 ATSALDSqSERV-VQDALERVMVGR--TSVVIAHRLSTI 1197
Cdd:COG1245 482 PSAHLDV-EQRLaVAKAIRRFAENRgkTAMVVDHDIYLI 519
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
476-582 |
2.56e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 476 AHNFISQLPN-------------GYeTQVGERGVQMSGGQKQRIAIARAIIK---SPTILLLDEATSALDSESER----V 535
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKklleV 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15229473 536 VQEALENasiGRTTILIAHRLSTIRNAD-VISV-----VKNGHIVETGSHDEL 582
Cdd:TIGR00630 875 LQRLVDK---GNTVVVIEHNLDVIKTADyIIDLgpeggDGGGTVVASGTPEEV 924
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
387-561 |
2.70e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 387 GKTVALVGGSGSGKSTVISLLqrfydplAGEILID--------GVSIDKLQVKWLRSQMGLVS-------QEPA------ 445
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKIL-------NGEVLLDdgriiyeqDLIVARLQQDPPRNVEGTVYdfvaegiEEQAeylkry 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 446 -----LFATTIKENILfgKEDASMDDVVEAAKA----SNAHNFISQLPNGYETQVGErgvqMSGGQKQRIAIARAIIKSP 516
Cdd:PRK11147 102 hdishLVETDPSEKNL--NELAKLQEQLDHHNLwqleNRINEVLAQLGLDPDAALSS----LSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15229473 517 TILLLDEATSALDSEServvQEALEN------ASIgrttILIAHRLSTIRN 561
Cdd:PRK11147 176 DVLLLDEPTNHLDIET----IEWLEGflktfqGSI----IFISHDRSFIRN 218
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1003-1204 |
3.00e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.81 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1003 SYPTRPDVIIFknfsikieEGKSTAIVGPSGSGKSTIIglierfyDPLKGIVKIDGRDIRSYHLRSLRRHIALVSQEptl 1082
Cdd:cd03227 9 SYFVPNDVTFG--------EGSLTIITGPNGSGKSTIL-------DAIGLALGGAQSATRRRSGVKAGCIVAAVSAE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1083 fagtireniiyggvsdkideaeiieaakaanahdFITSLtegydtycgdrgVQLSGGQKQRIAIARAV----LKNPSVLL 1158
Cdd:cd03227 71 ----------------------------------LIFTR------------LQLSGGEKELSALALILalasLKPRPLYI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15229473 1159 LDEATSALDSQSERVVQDALERVMV-GRTSVVIAHRLSTIQNCDAIA 1204
Cdd:cd03227 105 LDEIDRGLDPRDGQALAEAILEHLVkGAQVIVITHLPELAELADKLI 151
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1012-1218 |
3.07e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1012 IFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLI--ERFYDPLKGIVKIDGRDIRSyhLRSLRRH---IALVSQEPTLFAGT 1086
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLE--LSPEDRAgegIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1087 IRENIIYGGVsDKIDEAEIIEAAKAANAHDFITS----LTEGYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:PRK09580 94 SNQFFLQTAL-NAVRSYRGQEPLDRFDFQDLMEEkialLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229473 1163 TSALDSQSERVVQDALERVMVGRTSVVIAHRLSTIQNC---DAIAVLDKGKLVERGTHS 1218
Cdd:PRK09580 173 DSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYikpDYVHVLYQGRIVKSGDFT 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
492-589 |
3.21e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 492 GERGVQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTILIAHRLSTIRN-ADVISVVK 569
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSmVRDGATVLLTTQYMEEAEQlAHELTVID 218
|
90 100
....*....|....*....|
gi 15229473 570 NGHIVETGSHDELMENIDGQ 589
Cdd:NF000106 219 RGRVIADGKVDELKTKVGGR 238
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
676-898 |
4.52e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs 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: 350049 [Multi-domain] Cd Length: 300 Bit Score: 46.75 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 676 CISATLFGAIQPAYAYSLGSMVSVYFLTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSK 755
Cdd:cd18605 5 LLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 756 VLTFEVGWFDRdeNSSGAICSRLAKDANVVrslvgDR---------MALVVQTVSAVtiaftmgLVIAWRLALVMIAVQP 826
Cdd:cd18605 85 ILFAKMSFFDK--TPVGRILNRFSSDVYTI-----DDslpfilnilLAQLFGLLGYL-------VVICYQLPWLLLLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 827 VIIVCFY-------TRRVL--LKSMSkkaikaqdeSSKLAA---EAVSNVRTITAFSSQERIMK----MLEKAQESPRRE 890
Cdd:cd18605 151 LAFIYYRiqryyraTSRELkrLNSVN---------LSPLYThfsETLKGLVTIRAFRKQERFLKeyleKLENNQRAQLAS 221
|
....*...
gi 15229473 891 SIRQSWFA 898
Cdd:cd18605 222 QAASQWLS 229
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1120-1223 |
4.88e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1120 SLTEGydtyCGDRGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALeRVMV--GRTSVVIAHRLSTI 1197
Cdd:NF000106 133 SLTEA----AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVrdGATVLLTTQYMEEA 207
|
90 100
....*....|....*....|....*..
gi 15229473 1198 -QNCDAIAVLDKGKLVERGTHSSLLSK 1223
Cdd:NF000106 208 eQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
378-582 |
4.97e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLL--QRfyDPLAGEILIDGVSIDKLQVKWLRsQMGL--VSQEP---ALFAT- 449
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERR-RLGVayIPEDRlgrGLVPDm 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDAS-------MDdvvEAAKASNAHNFISQL---PNGYETQVGergvQMSGGQKQRIAIARAIIKSPTIL 519
Cdd:COG3845 352 SVAENLILGRYRRPpfsrggfLD---RKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 520 LLDEATSALDSES-ERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDEL 582
Cdd:COG3845 425 IAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
714-952 |
6.40e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs 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: 350045 [Multi-domain] Cd Length: 314 Bit Score: 46.55 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 714 IYAlsfvGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVG--- 790
Cdd:cd18601 64 IYA----GLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDT--NPIGRILNRFSKDIGHLDDLLPltf 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 791 -DRMALVVQTVSAVTIAftmGLVIAWrlalVMIAVQPVIIVCFYTRRVLLK-SMSKKAIKAQDES---SKLAAeAVSNVR 865
Cdd:cd18601 138 lDFLQLLLQVVGVVLLA---VVVNPW----VLIPVIPLVILFLFLRRYYLKtSREVKRIEGTTRSpvfSHLSS-TLQGLW 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 866 TITAFSSQERIMKMLEKAQESPRResirqSWFAgFgLAMSQsltsctwaldfWYGGRLiqdgyitaKALFETFMILVSTG 945
Cdd:cd18601 210 TIRAYSAQERFQEEFDAHQDLHSE-----AWFL-F-LATSR-----------WLAVRL--------DALCALFVTVVAFG 263
|
250
....*....|.
gi 15229473 946 RVIA----DAG 952
Cdd:cd18601 264 SLFLaeslDAG 274
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
384-587 |
7.51e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 384 VPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGVS---------------IDKLQVKWLrsQMGLVSQEpalfa 448
Cdd:PRK13545 47 VPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAaliaissglngqltgIENIELKGL--MMGLTKEK----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 449 ttIKENIlfgkedasmDDVVEAAKASnahNFISQLPNGYetqvgergvqmSGGQKQRIAIARAIIKSPTILLLDEATSAL 528
Cdd:PRK13545 120 --IKEII---------PEIIEFADIG---KFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229473 529 DSE-SERVVQEALENASIGRTTILIAHRLSTIRNADVISV-VKNGHIVETGSHDELMENID 587
Cdd:PRK13545 175 DQTfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDHYD 235
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
496-565 |
8.28e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.27 E-value: 8.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 496 VQMSGGQKQRIAIARAI----IKSPTILLLDEATSALDSESERVVQEAL-ENASIGRTTILIAHRLSTIRNADVI 565
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKL 150
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
714-944 |
9.99e-05 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 45.90 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 714 IYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDrdENSSGAICSRLAKDANVVRSLV--GD 791
Cdd:cd18549 43 IIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAhhGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 792 RMALVvqtvSAVTI--AFTMGLVIAWRLALVMIAVQPVIIVCFYTRRVLLKSMSKKA------IKAQDESSklaaeaVSN 863
Cdd:cd18549 121 EDLFI----SIITIigSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVrekigeINAQLEDS------LSG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 864 VRTITAFSSQERIMKMLEKA----QESpRRESIRQ-SWFAGFGLAMSQSLTSCTWAldfwYGGRLIQDGYITAKALFeTF 938
Cdd:cd18549 191 IRVVKAFANEEYEIEKFDEGndrfLES-KKKAYKAmAYFFSGMNFFTNLLNLVVLV----AGGYFIIKGEITLGDLV-AF 264
|
....*.
gi 15229473 939 MILVST 944
Cdd:cd18549 265 LLYVNV 270
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
715-880 |
1.25e-04 |
|
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: 45.54 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 715 YALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICSRLAKDANVVRSLVGDRMA 794
Cdd:cd18604 45 YLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDT--TPVGRILNRFSKDIETIDSELADSLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 795 LVVQTVSAVTIAFTMGLVIAWRLALVMIAVqpVIIVCFYTRRVLLKSMSKKAIkaqdESSKLA------AEAVSNVRTIT 868
Cdd:cd18604 123 SLLESTLSLLVILIAIVVVSPAFLLPAVVL--AALYVYIGRLYLRASRELKRL----ESVARSpilshfGETLAGLVTIR 196
|
170
....*....|..
gi 15229473 869 AFSSQERIMKML 880
Cdd:cd18604 197 AFGAEERFIEEM 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1014-1215 |
1.32e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1014 KNFSIKIEEGKSTAIVGPSGSGKSTIigLIERFYDPLKgivkidgrdirsyhlRSLRRHIALVSQEPTLFAGTIReniiy 1093
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGK---------------ARLISFLPKFSRNKLIFIDQLQ----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1094 ggvsdkideaeiieaakaanahdFITSLTEGYDTYcgDRGVQ-LSGGQKQRIAIARAVLKNP--SVLLLDEATSALDSQS 1170
Cdd:cd03238 70 -----------------------FLIDVGLGYLTL--GQKLStLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1171 ERVVQDALER-VMVGRTSVVIAHRLSTIQNCDAI------AVLDKGKLVERG 1215
Cdd:cd03238 125 INQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1005-1167 |
1.38e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.97 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1005 PTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYD-PLKGIVKIDGR--DIRSyHLRSLRRHIALVSQEPT 1081
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRN-PAQAIRAGIAMVPEDRK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1082 lfagtiRENII-YGGVSDKIdeaeiieAAKAANAHDFITSLTEGYDTYCGDRGVQ---------------LSGGQKQRIA 1145
Cdd:TIGR02633 347 ------RHGIVpILGVGKNI-------TLSVLKSFCFKMRIDAAAELQIIGSAIQrlkvktaspflpigrLSGGNQQKAV 413
|
170 180
....*....|....*....|..
gi 15229473 1146 IARAVLKNPSVLLLDEATSALD 1167
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVD 435
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
496-568 |
1.43e-04 |
|
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: 44.10 E-value: 1.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 496 VQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSE----SERVVQEALENASigRTTILIAHRLSTIRN-ADVISVV 568
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGK--KTALVVEHDLAVLDYlSDRIHVF 145
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
380-568 |
2.32e-04 |
|
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: 45.55 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 380 FCLRVP-SGKTVALVGGSGSGKSTVISLLqrfydplAGEIlidgvsidklqvkwlrsqmglvsqepalfattiKENilFG 458
Cdd:COG1245 91 YGLPVPkKGKVTGILGPNGIGKSTALKIL-------SGEL---------------------------------KPN--LG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 459 K--EDASMDDVVEAAKASNAHNFISQLPNG-----YETQ-------------------VGERGV---------------- 496
Cdd:COG1245 129 DydEEPSWDEVLKRFRGTELQDYFKKLANGeikvaHKPQyvdlipkvfkgtvrellekVDERGKldelaeklglenildr 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 497 ---QMSGGQKQRIAIARAIIKSPTILLLDEATSALD----SESERVVQEALENasiGRTTILIAHRLSTIRN-ADVISVV 568
Cdd:COG1245 209 disELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
32-297 |
2.42e-04 |
|
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: 44.39 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 32 WLLMGLGLIGAVGDGFTTplvlLITSKLMNN-IGGSsfNTDTFMQSISKNSVALLYVACGSWVVCFLEGYCwtrtgerqt 110
Cdd:cd18540 5 ILLIILMLLVALLDAVFP----LLTKYAIDHfITPG--TLDGLTGFILLYLGLILIQALSVFLFIRLAGKI--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 111 armrEKYLRAVLRQDV---------GYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNFLMSASTFVGSYIVGFILLWR 181
Cdd:cd18540 70 ----EMGVSYDLRKKAfehlqtlsfSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 182 LAIvglpfIVLLVIPGLmygrALISI---------SRKIREE-------YNEagfvaeqAISSVRTVYAFSGERKTISKF 245
Cdd:cd18540 144 LAL-----IVLAVVPVL----AVVSIyfqkkilkaYRKVRKInsritgaFNE-------GITGAKTTKTLVREEKNLREF 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15229473 246 ----STALQGSVKLGIKQGLAKGI--TIGSNGITFAMwgfmsWYGSRMVMYHGAQGGT 297
Cdd:cd18540 208 keltEEMRRASVRAARLSALFLPIvlFLGSIATALVL-----WYGGILVLAGAITIGT 260
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
688-882 |
3.15e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 44.13 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 688 AYAYSLGSMVSVYFLTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYnfayMGEYLTKRIRERMLSKVLTFEVGWFDRd 767
Cdd:cd18602 29 NHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGEL----AGLRAARRLHDRMLRNIVRAPMRFFDT- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 768 eNSSGAICSRLAKDANVVRSLVGDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIavqPVIIVCFYTRRVLLKSmsKKAI 847
Cdd:cd18602 104 -TPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALI---PIIIVYYFLQKFYRAS--SREL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15229473 848 KAQDESSKL-----AAEAVSNVRTITAFSSQERIM-KMLEK 882
Cdd:cd18602 178 QRLDNITKSpvfshFSETLGGLTTIRAFRQQARFTqQMLEL 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
995-1179 |
3.48e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 995 VEFLDVDFSYPTRPdviIFKNFSIKIEEGKSTAIVGPSGSGKSTIiglierfydplkgivkidgrdirsyhLRSLRRHIa 1074
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTL--------------------------LRTLVGEL- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1075 lvsqEPTlfAGTIR--ENIIYGGVSDKideaeiieaakaaNAHDFITSLT-----EGYDTYCGD----RGV--------- 1134
Cdd:PRK15064 370 ----EPD--SGTVKwsENANIGYYAQD-------------HAYDFENDLTlfdwmSQWRQEGDDeqavRGTlgrllfsqd 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1135 -------QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALE 1179
Cdd:PRK15064 431 dikksvkVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE 482
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
718-949 |
3.61e-04 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, 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 PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 44.13 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 718 SFVGLAVLSFLINI---------SQHYN-------------------FAYMGEYLTKRIRERMLSKV---LTFEVG--WF 764
Cdd:cd18586 3 VFVEVGLFSFFINLlalappifmLQVYDrvlpsgslstllgltlgmvVLLAFDGLLRQVRSRILQRVglrLDVELGrrVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 765 DR------DENSSGAICSRLaKDANVVRSLVGDRMALVVqtVSAVTIAFTMGL--VIAWRLALVMIAVQPVIIVCFYTRR 836
Cdd:cd18586 83 RAvlelplESRPSGYWQQLL-RDLDTLRNFLTGPSLFAF--FDLPWAPLFLAVifLIHPPLGWVALVGAPVLVGLAWLNH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 837 VLLKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSSQERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALD 916
Cdd:cd18586 160 RATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLI 239
|
250 260 270
....*....|....*....|....*....|...
gi 15229473 917 FWYGGRLIQDGYITAKALFETFMILvstGRVIA 949
Cdd:cd18586 240 LGVGAYLVIDGELTIGALIAASILS---GRALA 269
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1136-1167 |
3.78e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 3.78e-04
10 20 30
....*....|....*....|....*....|..
gi 15229473 1136 LSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
373-579 |
4.78e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 373 ETSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLL--QRFYDPLAGEILIDGVSIDKLQVKwLRSQMG--LVSQEPA--- 445
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGifMAFQYPVeip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 446 -----LFATTIKENILFGKEDASMD-----DVVEAAKAsnahnfISQLPNGYETQvgERGVQMSGGQKQRIAIARAIIKS 515
Cdd:PRK09580 92 gvsnqFFLQTALNAVRSYRGQEPLDrfdfqDLMEEKIA------LLKMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 516 PTILLLDEATSALDSESERVVQEALENASIG-RTTILIAH--RLSTIRNADVISVVKNGHIVETGSH 579
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
486-584 |
5.36e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 486 GYETQVGergvQMSGGQKQRIAIARAIIKSPTILLLDEATSALDSESE-RVVQEALENASIGRTTILIAHRLSTIRN-AD 563
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTD 459
|
90 100
....*....|....*....|....*.
gi 15229473 564 VISVVKNGH---IVETG--SHDELME 584
Cdd:PRK10982 460 RILVMSNGLvagIVDTKttTQNEILR 485
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
380-568 |
5.63e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 380 FCLRVPS-GKTVALVGGSGSGKSTVISLLqrfydplAGEIlidgvsidklqvkwlrsqmglvsqepalfattiKENilFG 458
Cdd:PRK13409 91 YGLPIPKeGKVTGILGPNGIGKTTAVKIL-------SGEL---------------------------------IPN--LG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 459 K--EDASMDDVVEAAKASNAHNFISQLPNG-----YETQ-------------------VGERGV---------------- 496
Cdd:PRK13409 129 DyeEEPSWDEVLKRFRGTELQNYFKKLYNGeikvvHKPQyvdlipkvfkgkvrellkkVDERGKldevverlglenildr 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 497 ---QMSGGQKQRIAIARAIIKSPTILLLDEATSALD----SESERVVQEALENasigRTTILIAHRLSTIRN-ADVISVV 568
Cdd:PRK13409 209 disELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIRELAEG----KYVLVVEHDLAVLDYlADNVHIA 284
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1136-1216 |
5.89e-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: 44.23 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1136 LSGGQKQRIAIARAVLK---NPSVLLLDEATSALDSQSERVVQDALER-VMVGRTSVVIAHRLSTIQNCDAIAVL----- 1206
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|.
gi 15229473 1207 DK-GKLVERGT 1216
Cdd:TIGR00630 910 DGgGTVVASGT 920
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
697-881 |
7.37e-04 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 42.97 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 697 VSVYFLTSHDEIKEKTRIYALSFVGLAVLSFLINISQHYNFAYMGEYLTKRIRERMLSKVLTFEVGWFDRdeNSSGAICS 776
Cdd:cd18559 22 LLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFER--TPSGELVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 777 RLAKDANVVrslvgDRMALVVQTVSAVTIAFTMGLVIAWRLALVMIAVQ-PVIIVCFYTRRVL---LKSMSKKAIKAQDE 852
Cdd:cd18559 100 LFSKDLDRV-----DSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGiPLGLLYVPVNRVYaasSRQLKRLESVSKDP 174
|
170 180
....*....|....*....|....*....
gi 15229473 853 SSKLAAEAVSNVRTITAFSSQERIMKMLE 881
Cdd:cd18559 175 RYKLFNETLLGISVIKAFEWEEAFIRQVD 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
359-563 |
8.02e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 359 VEFKNVKFVYPSRletSIFDDFCLRVPSGKTVALVGGSGSGKSTVISLL-----QRFYDPL--------AGEILIDgvsi 425
Cdd:PRK10938 261 IVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGYSNDLtlfgrrrgSGETIWD---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 426 dklqvkwLRSQMGLVSQEPAL---FATTIKENILFGKEDA-SMDDVVEAAKASNAHNFISQLpnGYETQVGERGVQ-MSG 500
Cdd:PRK10938 334 -------IKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSiGIYQAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSW 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 501 GQkQRIA-IARAIIKSPTILLLDEATSALDSESERVVQEALEN-ASIGRTTIL------------IAHRLSTIRNAD 563
Cdd:PRK10938 405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFVPDGD 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1008-1212 |
8.16e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1008 PDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIR-SYHLRSLRRHIALVSQEPTLFAG- 1085
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1086 TIRENIIYGGVSDK---IDeaeiieaakaanaHDFITSLTE------GYDTYCGDRGVQLSGGQKQRIAIARAVLKNPSV 1156
Cdd:PRK10982 89 SVMDNMWLGRYPTKgmfVD-------------QDKMYRDTKaifdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1157 LLLDEATSALdSQSE-----RVVQDALERvmvGRTSVVIAHRLSTI-QNCDAIAVLDKGKLV 1212
Cdd:PRK10982 156 VIMDEPTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
1013-1040 |
8.19e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.74 E-value: 8.19e-04
10 20
....*....|....*....|....*...
gi 15229473 1013 FKNFSIKIEEGKSTAIVGPSGSGKSTII 1040
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
378-583 |
1.03e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 378 DDFCLRVPSGKTVALVGGSGSGKSTVISLLQRFYDPLAGEILIDGvsidklQVKWLRSQMGLVSQEPALfattikENILF 457
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQLTGI------ENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 458 G--------KE-DASMDDVVEaakASNAHNFISQLPNGYetqvgergvqmSGGQKQRIAIARAIIKSPTILLLDEATSAL 528
Cdd:PRK13546 109 KmlcmgfkrKEiKAMTPKIIE---FSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15229473 529 DSE-SERVVQEALENASIGRTTILIAHRLSTIRN-ADVISVVKNGHIVETGSHDELM 583
Cdd:PRK13546 175 DQTfAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
84-212 |
1.11e-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: 42.49 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 84 LLYVACGSWVVCFLEGYCWTRTGERQTARMREKYLRAVLRQDVGYFDlhVTSTSDVITSVSSDSFVIQDVLSEKLPNFLM 163
Cdd:cd18580 45 AALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD--TTPSGRILNRFSKDIGLIDEELPLALLDFLQ 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15229473 164 SASTFVGSYIVGFILLWRLAIVGLPFIVLLVIPGLMYGRAlisiSRKIR 212
Cdd:cd18580 123 SLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRT----SRQLR 167
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1135-1167 |
1.15e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|...
gi 15229473 1135 QLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1015-1215 |
1.34e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1015 NFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIDGrdirSYHLrslrrhIALVSQEPTLFAGTirENI--- 1091
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----SAAL------IAISSGLNGQLTGI--ENIelk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1092 -IYGGVSDKIDEAEIIEAAKAANAHDFITSLTEGYdtycgdrgvqlSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQ- 1169
Cdd:PRK13545 110 gLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTf 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15229473 1170 SERVVQDALERVMVGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVERG 1215
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYG 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
387-529 |
1.36e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 387 GKTVALVGGSGSGKSTV--------ISLLQRFYDPLAGEILIDGVSIDKLQ---------VKWLRSQMGLVSQEPALFAT 449
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFlrymamhaIDGIPKNCQILHVEQEVVGDDTTALQcvlntdierTQLLEEEAQLVAQQRELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 450 TIKENILFGKEDASMDDVVEA---------------AKASNAHNFISQLPNGYETQVgERGVQMSGGQKQRIAIARAIIK 514
Cdd:PLN03073 283 TETGKGKGANKDGVDKDAVSQrleeiykrlelidayTAEARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARALFI 361
|
170
....*....|....*
gi 15229473 515 SPTILLLDEATSALD 529
Cdd:PLN03073 362 EPDLLLLDEPTNHLD 376
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1013-1076 |
1.38e-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: 42.30 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1013 FKNFSIKIEEGKsTAIVGPSGSGKSTIIGLIERFYDPLKGIvKIDGRDirsYHLRSLRRHIALV 1076
Cdd:COG3593 14 IKDLSIELSDDL-TVLVGENNSGKSSILEALRLLLGPSSSR-KFDEED---FYLGDDPDLPEIE 72
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
498-590 |
1.83e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 498 MSGGQKQRIAIARAIIKSPT--ILLLDEATSAL-DSESERVVQEALENASIGRTTILIAHRLSTIRNAD-VISV-----V 568
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADyVIDIgpgagE 568
|
90 100
....*....|....*....|....*
gi 15229473 569 KNGHIVETGSHDELMEN---IDGQY 590
Cdd:TIGR00630 569 HGGEVVASGTPEEILANpdsLTGQY 593
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
498-537 |
2.01e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15229473 498 MSGGQKQRIAIARAIIKSPTILLLDEATSALDSES-ERVVQ 537
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1139-1211 |
2.90e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSQSERvvqdALERVMVGRTS--VVIAH-RLSTIQNCDAIAVLDKGKL 1211
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIR----WLEDVLNERNStmIIISHdRHFLNSVCTHMADLDYGEL 230
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1007-1183 |
3.09e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1007 RPDVIIFKNF-------SIKIEEGkSTAIVGPSGSGKSTIIGLIER-FYDPLKGIVKIDGRDIRS--------------- 1063
Cdd:COG0419 1 KLLRLRLENFrsyrdteTIDFDDG-LNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVgseeasvelefehgg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1064 YHLRSLRRH---IALVSQEPTLFAGTIRE--NI-IYGGVSDKIDEAEIIEAAKAANAHDFIT------SLTEGYDTYCgd 1131
Cdd:COG0419 80 KRYRIERRQgefAEFLEAKPSERKEALKRllGLeIYEELKERLKELEEALESALEELAELQKlkqeilAQLSGLDPIE-- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15229473 1132 rgvQLSGGQKQRIAIARAVlknpsVLLLDeaTSALDSQSERVVQDALERVMV 1183
Cdd:COG0419 158 ---TLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELAI 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
989-1192 |
3.14e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 989 ERITGQV-EFLDVDFSYPTRpdvIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIERFYDPLKGIVKIdGRDIrsyhlr 1067
Cdd:PRK11819 318 PRLGDKViEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1068 slrrHIALVSQEptlfagtiRENI-----IYGGVSDkideaeiieaakaanAHDFITslTEGYDT----YCGD---RGV- 1134
Cdd:PRK11819 388 ----KLAYVDQS--------RDALdpnktVWEEISG---------------GLDIIK--VGNREIpsraYVGRfnfKGGd 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229473 1135 ------QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERvmVGRTSVVIAH 1192
Cdd:PRK11819 439 qqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE--FPGCAVVISH 500
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1135-1222 |
3.27e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1135 QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSQSERVVQDALERVMV--GRTSVVIAHRLSTI-QNCDAIAVLDKGKL 1211
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 15229473 1212 VERGTHSSLLS 1222
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1135-1167 |
4.29e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 4.29e-03
10 20 30
....*....|....*....|....*....|...
gi 15229473 1135 QLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
800-943 |
5.84e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD 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. 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: 350029 [Multi-domain] Cd Length: 290 Bit Score: 40.16 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 800 VSAVTIAFTMGLVIAW---RLALVMIAVQPVIIVC----FYTRRvllKSMSKKAIKAQDESSKLAAEAVSNVRTITAFSS 872
Cdd:cd18585 117 VVALLVILATILFLAFfspALALILLAGLLLAGVVipllFYRLG---KKIGQQLVQLRAELRTELVDGLQGMAELLIFGA 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229473 873 QERIMKMLEKAQESPRRESIRQSWFAGFGLAMSQSLTSCTWALDFWYGGRLIQDGYITAK--ALFeTFMILVS 943
Cdd:cd18585 194 LERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALDGAllAML-VFAVLAS 265
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1135-1203 |
7.02e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 7.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1135 QLSGGQKQRIAIAR--AVLK-NPSVL-LLDEATSALD-SQSERVVQdaLERVMVGRTS-VVIAHRLSTIQNCDAI 1203
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKvKPAPFcILDEVDAPLDdANVERFAN--LLKEFSKNTQfIVITHNKGTMEVADQL 1161
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
1018-1065 |
7.89e-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: 38.88 E-value: 7.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15229473 1018 IKIEEGKSTAIV--GPSGSGKSTIIGLIERFYDPLKGIVKIDGRDIRSYH 1065
Cdd:pfam06414 4 KTTSQERPKAILlgGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELH 53
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1006-1213 |
9.59e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1006 TRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGLIerF-YDPLK-GIVKIDGRDIR-SYHLRSLRRHIALVSQ---E 1079
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL--FgVDKRAgGEIRLNGKDISpRSPLDAVKKGMAYITEsrrD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229473 1080 PTLFAG-TIRENII---------YGGV------SDKIDEAEIIEAAKAANAHDFITSLTEgydtycgdrgvqLSGGQKQR 1143
Cdd:PRK09700 350 NGFFPNfSIAQNMAisrslkdggYKGAmglfheVDEQRTAENQRELLALKCHSVNQNITE------------LSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229473 1144 IAIARAVLKNPSVLLLDEATSALD--SQSE--RVVQDALERvmvGRTSVVIAHRLSTIQN-CDAIAVLDKGKLVE 1213
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDvgAKAEiyKVMRQLADD---GKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
987-1042 |
9.84e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 9.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229473 987 ETERiTGQVEFLDVDFSYpTRPDVIIFKNFSIKIEEGKSTAIVGPSGSGKSTIIGL 1042
Cdd:PRK11147 311 EASR-SGKIVFEMENVNY-QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL 364
|
|
| |
