|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
30-620 |
6.03e-178 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 538.21 E-value: 6.03e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 30 SIFQLYRYTSTvDRLMLAVGIIVSCATGVGLPLMSIIMGNVsqnfvtLGTIFLDPNSTAsekaaaraefsheVIQNCLKY 109
Cdd:COG1132 8 LLRRLLRYLRP-YRGLLILALLLLLLSALLELLLPLLLGRI------IDALLAGGDLSA-------------LLLLLLLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 110 VYLGCGIFAAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMA 189
Cdd:COG1132 68 LGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 190 QFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYE 269
Cdd:COG1132 148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 270 DALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIGTA 349
Cdd:COG1132 228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 350 LGAAASLYEVIDRIPEIdAYSTEGQTPSKISGRISVNKVEFTYPtrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQ 429
Cdd:COG1132 308 LASAERIFELLDEPPEI-PDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 430 LLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPE 509
Cdd:COG1132 385 LLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 510 GLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKI 589
Cdd:COG1132 465 GYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRI 544
|
570 580 590
....*....|....*....|....*....|.
gi 17558664 590 IVMKAGQVMEVGTHETLIEQKGLYHELVHAQ 620
Cdd:COG1132 545 LVLDDGRIVEQGTHEELLARGGLYARLYRLQ 575
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
689-1273 |
1.34e-166 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 508.55 E-value: 1.34e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 689 KANLFKILRYARPEWIYIFFAIIAALIQGAVMPAFSLFFSQIIN-VFSNPDRDQMKkdghFWALMFLVLAAVQGTSMLFQ 767
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDaLLAGGDLSALL----LLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 768 CSLFGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYY 847
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 848 GWQMAFLVMAIFPFMAVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNIS 927
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 928 KAIIRGLTYGFANSIQFFTYAAAFRFGLFLIFDKNvlMEPENVLRVLFAISFSFGTIGFAASYFPEYIKATFAAGLIFNM 1007
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGS--LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1008 LEEEPRIDGMTSSGTYPQLSGEVKLNKVFFRYPERPavPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEG 1087
Cdd:COG1132 318 LDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDR--PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1088 AVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLQpgEYTHEQIETACSKANIHKFIDELPDGYETRVGEK 1167
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1168 GTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVV 1247
Cdd:COG1132 474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570 580
....*....|....*....|....*.
gi 17558664 1248 EQGTHNELIAKRGAYFALTQKQSSNQ 1273
Cdd:COG1132 554 EQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-1262 |
3.87e-159 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 515.73 E-value: 3.87e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 28 KISIFQLYRYTSTVDRLMLAVGIIVSCATGVGLPLMSIIMGNVSQNfVTLGtifldpnstasekaaaraEFSHEVIqncL 107
Cdd:PTZ00265 44 KIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIMKN-MNLG------------------ENVNDII---F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 108 KYVYLGCGIFAAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQM 187
Cdd:PTZ00265 102 SLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 188 MAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKR 267
Cdd:PTZ00265 182 ASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 268 YEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYS--------GRLESGTVLTVFFSVMMGSMALGQA 339
Cdd:PTZ00265 262 FNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTII 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 340 GQQFATIGTALGAAASLYEVIDRIPEIDAySTEGQTPSKISgRISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGS 419
Cdd:PTZ00265 342 LPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 420 SGCGKSTIIQLLQRFYNPDAGQILIDDI-PIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYG---------------- 482
Cdd:PTZ00265 420 SGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyne 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 483 ------------------------------RSD-----------VSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQ 521
Cdd:PTZ00265 500 dgndsqenknkrnscrakcagdlndmsnttDSNeliemrknyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASK 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 522 MSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAHRLSTVRNADKIIVM------- 592
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLsnrergs 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 593 ---------------------------------------KAGQ-VMEVGTHETLIEQK-GLYHELVHAQVFA-------- 623
Cdd:PTZ00265 660 tvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinNAGSyIIEQGTHDALMKNKnGIYYTMINNQKVSskkssnnd 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 624 ---DVDDKPKK-KEAER-----RMSRQTSQRKGSVNFKTQESQVDEKPGAPPAPEAAEKEIKRLKKELEEEGAVKANLFK 694
Cdd:PTZ00265 740 ndkDSDMKSSAyKDSERgydpdEMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKAPNNLRIVYRE 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 695 ILRYARpEWIYIFFAIIAAliqGAVMPAFSLFFSQIINV---FSNPDRDQMKkdghfWALMFLVLAAVQGTSMLFQCSLF 771
Cdd:PTZ00265 820 IFSYKK-DVTIIALSILVA---GGLYPVFALLYAKYVSTlfdFANLEANSNK-----YSLYILVIAIAMFISETLKNYYN 890
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 772 GVAAERLTMRIRSKVYRNVLRQDATYFDMPKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQM 851
Cdd:PTZ00265 891 NVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIV 970
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 852 A-------FLVMAIFPF---MAVGQALMMKYHGGSAT-----SDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCS 916
Cdd:PTZ00265 971 AavltgtyFIFMRVFAIrarLTANKDVEKKEINQPGTvfaynSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEK 1050
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 917 HLDAPHGGNISKAIIRGLTYGFANSIQFFTYAAAFRFGLFLIfdKNVLMEPENVLRVLFAISFSFGTIGFAASYFPEYIK 996
Cdd:PTZ00265 1051 AIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLI--RRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSEN 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 997 ATFAAGLIFNMLEEEPRIDGMTSSGTYPQ----LSGEVKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKS 1072
Cdd:PTZ00265 1129 AKLSFEKYYPLIIRKSNIDVRDNGGIRIKnkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKS 1208
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1073 TVISLLERLYD------------------------------------------------------PLEGAVTVDNNDLRQ 1098
Cdd:PTZ00265 1209 TVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICD 1288
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1099 MNPKHLRKHIALVSQEPILFDTSIRENIVYGLQpgEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQR 1178
Cdd:PTZ00265 1289 YNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE--DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQR 1366
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1179 IAIARALIRNPKILLLDEATSALDTESEKQVQ-VALDAAAK-DRTCIVVAHRLSTIVNAGCIMVVKN----GQVVE-QGT 1251
Cdd:PTZ00265 1367 IAIARALLREPKILLLDEATSSLDSNSEKLIEkTIVDIKDKaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGT 1446
|
1450
....*....|..
gi 17558664 1252 HNELI-AKRGAY 1262
Cdd:PTZ00265 1447 HEELLsVQDGVY 1458
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
117-621 |
2.44e-143 |
|
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: 451.98 E-value: 2.44e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 117 FAAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNlERVREG-TGDKVGLAFQMMaQFIGGF 195
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDV-ESIREFlTGSLLTALLDLL-FVLIFL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 196 AVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHG 275
Cdd:COG2274 288 IVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKY 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 276 KKTGIKkSFLIGAGLASFFVIIYA-SYCLAFWVGTNFVYSGRLESGTVLTvfFSVMMGSM--ALGQAGQQFATIGTALGA 352
Cdd:COG2274 368 LNARFK-LRRLSNLLSTLSGLLQQlATVALLWLGAYLVIDGQLTLGQLIA--FNILSGRFlaPVAQLIGLLQRFQDAKIA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 353 AASLYEVIDRIPEIDAYSTEGQTPsKISGRISVNKVEFTYPtRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQ 432
Cdd:COG2274 445 LERLDDILDLPPEREEGRSKLSLP-RLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 433 RFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLN 512
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 513 TLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVM 592
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
490 500
....*....|....*....|....*....
gi 17558664 593 KAGQVMEVGTHETLIEQKGLYHELVHAQV 621
Cdd:COG2274 683 DKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1030-1269 |
1.19e-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: 426.96 E-value: 1.19e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDTSIRENIVYGLQPGeyTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNP 1189
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQKQ 1269
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
383-620 |
1.63e-139 |
|
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: 423.87 E-value: 1.63e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 543 LLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQ 620
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
110-620 |
1.17e-131 |
|
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: 416.41 E-value: 1.17e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 110 VYLGCGIFAAGFLqascFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMA 189
Cdd:TIGR02204 69 LVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 190 QFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRY- 268
Cdd:TIGR02204 145 MCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFg 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 269 ---EDALEHGKKTGIKKSFLIgaglASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLT-VFFSVMMGsMALGQAGQQFA 344
Cdd:TIGR02204 225 gavEKAYEAARQRIRTRALLT----AIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQfVFYAVMVA-GSIGTLSEVWG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 345 TIGTALGAAASLYEVIDRIPEIDAYSTEGQTPSKISGRISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGK 424
Cdd:TIGR02204 300 ELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 425 STIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFI 504
Cdd:TIGR02204 380 STLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFI 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 505 KTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVR 584
Cdd:TIGR02204 460 SALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVL 539
|
490 500 510
....*....|....*....|....*....|....*.
gi 17558664 585 NADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQ 620
Cdd:TIGR02204 540 KADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
681-1269 |
3.61e-129 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 414.23 E-value: 3.61e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 681 ELEEEGAVKANLFKILRYARPEWIYIFFAIIAALIQGAVMPAFSLFFSQIIN-VFSNPDRDQMkkdghfWALMFLVLAAV 759
Cdd:COG2274 133 EFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDrVLPNQDLSTL------WVLAIGLLLAL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 760 --QGTSMLFQCSLFGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLaTDAPNIKSAIDYRLGSIFNAIASV 837
Cdd:COG2274 207 lfEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 838 GGGLGIAFYYGWQMAFLVMAIFPFMAVGQALMMKYhggSATSDAKEMENAGKTA---MEAIENIRTVQALTLQTKLY--- 911
Cdd:COG2274 284 LIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPR---LRRLSREESEASAKRQsllVETLRGIETIKALGAESRFRrrw 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 912 -NIFCSHLDAphggNISKAIIRGLTYGFANSIQFFTYAAAFRFGLFLIFDknvlmepeNVLRV--LFAISFSFGT----I 984
Cdd:COG2274 361 eNLLAKYLNA----RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVID--------GQLTLgqLIAFNILSGRflapV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 985 GFAASYFPEYIKATFAAGLIFNMLEEEPRIDGMTSSGTYPQLSGEVKLNKVFFRYPERPAvPILQGLNVHVKPGQTLALV 1064
Cdd:COG2274 429 AQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIV 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1065 GPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLQpgEYTHEQIETAC 1144
Cdd:COG2274 508 GRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDP--DATDEEIIEAA 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1145 SKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIV 1224
Cdd:COG2274 586 RLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVII 665
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 17558664 1225 VAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQKQ 1269
Cdd:COG2274 666 IAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
98-617 |
1.90e-128 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 412.58 E-value: 1.90e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 98 FSHEVIQNCLkyvyLGCGIFAAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGT 177
Cdd:TIGR00958 200 LASAIFFMCL----LSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 178 GDKVGLAFQMMAQFIGGFAVAFTYDWLLTLIMMSLSPFMmicgLFLAKLLAT--AATKEAKQYAVA--GGIAEEVLTSIR 253
Cdd:TIGR00958 276 SLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV----FLAEKVFGKryQLLSEELQEAVAkaNQVAEEALSGMR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 254 TVIAFNGQEYECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLtvffSVMMGS 333
Cdd:TIGR00958 352 TVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 334 MALGQAGQQFATIGT----ALGAAASLYEVIDRIPEIDaySTEGQTPSKISGRISVNKVEFTYPTRADVKILKGVSLDAQ 409
Cdd:TIGR00958 428 EQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRKPNIP--LTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLH 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 410 PGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDE 489
Cdd:TIGR00958 506 PGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 490 DIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASr 569
Cdd:TIGR00958 586 EIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRAS- 664
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 17558664 570 gRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELV 617
Cdd:TIGR00958 665 -RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
696-1014 |
4.88e-120 |
|
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: 375.64 E-value: 4.88e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 696 LRYARPEWIYIFFAIIAALIQGAVMPAFSLFFSQIINVFSNPDRDQMKKDGHFWALMFLVLAAVQGTSMLFQCSLFGVAA 775
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 776 ERLTMRIRSKVYRNVLRQDATYFDMPKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLV 855
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 856 MAIFPFMAVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGLT 935
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 936 YGFANSIQFFTYAAAFRFGLFLIFDKNvlMEPENVLRVLFAISFSFGTIGFAASYFPEYIKATFAAGLIFNMLEEEPRI 1014
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGE--YTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
119-624 |
2.34e-118 |
|
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: 380.60 E-value: 2.34e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 119 AGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVA 198
Cdd:TIGR02203 70 CSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 199 FTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYeDALEHgKKT 278
Cdd:TIGR02203 150 LYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRF-DAVSN-RNR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 279 GIKKSFLIGAGLASFFVIIYASYCLAF--WVGTNFVYSGRLESGTvLTVFFSVMMGSMA-LGQAGQQFATIGTALGAAAS 355
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIASLALAVvlFIALFQAQAGSLTAGD-FTAFITAMIALIRpLKSLTNVNAPMQRGLAAAES 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 356 LYEVIDRIPEIDaysTEGQTPSKISGRISVNKVEFTYPTRaDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFY 435
Cdd:TIGR02203 307 LFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 436 NPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGR-SDVSDEDIARALKEANAADFIKTFPEGLNTL 514
Cdd:TIGR02203 383 EPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTP 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 515 VGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKA 594
Cdd:TIGR02203 463 IGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDD 542
|
490 500 510
....*....|....*....|....*....|
gi 17558664 595 GQVMEVGTHETLIEQKGLYHELvHAQVFAD 624
Cdd:TIGR02203 543 GRIVERGTHNELLARNGLYAQL-HNMQFRE 571
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
692-1269 |
1.50e-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: 378.66 E-value: 1.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 692 LFKILRYARPEWIYIFFAIIAALIQGAVMPAFSLFFSQII-NVFSNPDRDQMKKdghfWALMFLVLAAVQGTSMLFQCSL 770
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIdHGFSKDSSGLLNR----YFAFLLVVALVLALGTAARFYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 771 FGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQ 850
Cdd:TIGR02204 82 VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 851 MAFLVMAIFPFMaVGQALMMKYHGGSATSDAKE-MENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKA 929
Cdd:TIGR02204 160 LTSLVLLAVPLV-LLPILLFGRRVRKLSRESQDrIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 930 IIRGLTYGFANSIQFFTYAAAFRFGLFLIFDKNvlMEPENVLRVLFAISFSFGTIGFAASYFPEYIKATFAAGLIFNMLE 1009
Cdd:TIGR02204 239 RTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGK--MSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1010 EEPRIDGMTSSGTYPQ-LSGEVKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGA 1088
Cdd:TIGR02204 317 AEPDIKAPAHPKTLPVpLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1089 VTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGlQPgEYTHEQIETACSKANIHKFIDELPDGYETRVGEKG 1168
Cdd:TIGR02204 397 ILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG-RP-DATDEEVEAAARAAHAHEFISALPEGYDTYLGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1169 TQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVE 1248
Cdd:TIGR02204 475 VTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVA 554
|
570 580
....*....|....*....|.
gi 17558664 1249 QGTHNELIAKRGAYFALTQKQ 1269
Cdd:TIGR02204 555 QGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
46-356 |
2.56e-116 |
|
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: 364.87 E-value: 2.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 46 LAVGIIVSCATGVGLPLMSIIMGNVSQNFVTLGTIFLDPNstasekaaaraEFSHEVIQNCLKYVYLGCGIFAAGFLQAS 125
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPD-----------EFLDDVNKYALYFVYLGIGSFVLSYIQTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 126 CFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLL 205
Cdd:cd18577 70 CWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 206 TLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFL 285
Cdd:cd18577 150 TLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 286 IGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIGTALGAAASL 356
Cdd:cd18577 230 SGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
680-1265 |
4.60e-113 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 370.98 E-value: 4.60e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 680 KELEEEGAVKANL-FKILRYARPEWIY----IFFAIIAALIQGAVmPAFSlffSQIIN-VFSNPDRDQMKKDGHFWALMF 753
Cdd:TIGR00958 136 KEAEQGQSETADLlFRLLGLSGRDWPWlisaFVFLTLSSLGEMFI-PFYT---GRVIDtLGGDKGPPALASAIFFMCLLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 754 L---VLAAVQGTSMLFqcslfgvAAERLTMRIRSKVYRNVLRQDATYFDMpkHSPGRITTRLATDAPNIKSAIDYRLGSI 830
Cdd:TIGR00958 212 IassVSAGLRGGSFNY-------TMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 831 FNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKL 910
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 911 YNIFCSHLDAPHGGNISKAIIRgLTYGFANSI-QFFTYAAAFRFGLFLIFDKNvlMEPENVLRVLFaISFSFGTIGFAAS 989
Cdd:TIGR00958 363 ASRFKEALEETLQLNKRKALAY-AGYLWTTSVlGMLIQVLVLYYGGQLVLTGK--VSSGNLVSFLL-YQEQLGEAVRVLS 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 990 YF-PEYIKATFAAGLIFNMLEEEPRIDgmtSSGTY--PQLSGEVKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGP 1066
Cdd:TIGR00958 439 YVySGMMQAVGASEKVFEYLDRKPNIP---LTGTLapLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1067 SGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLQpgEYTHEQIETACSK 1146
Cdd:TIGR00958 516 SGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLT--DTPDEEIMAAAKA 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1147 ANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQValDAAAKDRTCIVVA 1226
Cdd:TIGR00958 594 ANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIA 671
|
570 580 590
....*....|....*....|....*....|....*....
gi 17558664 1227 HRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFAL 1265
Cdd:TIGR00958 672 HRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
254-620 |
3.26e-111 |
|
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: 362.60 E-value: 3.26e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 254 TVIAFNGQEYECKRYEDALEHGKKTGIK--KS-FLIGAGLAsffVIIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVM 330
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKsqTSlALLNFGQA---LIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 331 MGSMALGQAGQQFATIGTALGAAASLYEVIDRIPEI-DAystEGQTPSKIS-GRISVNKVEFTYptRADVKILKGVSLDA 408
Cdd:COG5265 307 QLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVaDA---PDAPPLVVGgGEVRFENVSFGY--DPERPILKGVSFEV 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 409 QPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSD 488
Cdd:COG5265 382 PAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 489 EDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENAS 568
Cdd:COG5265 462 EEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17558664 569 RGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQ 620
Cdd:COG5265 542 RGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
383-616 |
8.65e-108 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 339.21 E-value: 8.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPtRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 543 LLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHEL 616
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
115-611 |
6.16e-105 |
|
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: 344.05 E-value: 6.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 115 GIFAAGFLQASCFMVICEKLSNRF--------RRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQ 186
Cdd:COG4988 62 GLLLAVLLLRALLAWLRERAAFRAaarvkrrlRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 187 MMAQFIGGFAVAFTYDWLLTLIMMSLSP----FMMICGLFLAKLLAtaatKEAKQYAVAGGIAEEVLTSIRTVIAFNGQE 262
Cdd:COG4988 142 AALVPLLILVAVFPLDWLSGLILLVTAPliplFMILVGKGAAKASR----RQWRALARLSGHFLDRLRGLTTLKLFGRAK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 263 YECKR-YEDALEHGKKT--GIKKSFLIGAGLaSFFViiYASYCL-AFWVGTNFVYsGRLesgTVLTVFFSVMMGS---MA 335
Cdd:COG4988 218 AEAERiAEASEDFRKRTmkVLRVAFLSSAVL-EFFA--SLSIALvAVYIGFRLLG-GSL---TLFAALFVLLLAPeffLP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 336 LGQAGQQFATIGTALGAAASLYEVIDRiPEIDAYSTEGQTPSKISGRISVNKVEFTYPTRADVkiLKGVSLDAQPGQTVA 415
Cdd:COG4988 291 LRDLGSFYHARANGIAAAEKIFALLDA-PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 416 LVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARAL 495
Cdd:COG4988 368 LVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAAL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 496 KEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIV 575
Cdd:COG4988 448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
|
490 500 510
....*....|....*....|....*....|....*.
gi 17558664 576 IAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKG 611
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1030-1265 |
1.79e-104 |
|
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: 330.35 E-value: 1.79e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDTSIRENIVYGlQPGEyTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNP 1189
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFAL 1265
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
120-620 |
2.95e-104 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 342.77 E-value: 2.95e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 120 GFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERV------------REGtgdkvglafqm 187
Cdd:PRK11176 82 SFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVassssgalitvvREG----------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 188 mAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKR 267
Cdd:PRK11176 151 -ASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 268 YEDALEHGKKTGIKksfLIGAGLASFFVI-IYASYCLAF--WVGTNFVYSGRLESGTVlTVFFSVMMGSM----ALGQAG 340
Cdd:PRK11176 230 FDKVSNRMRQQGMK---MVSASSISDPIIqLIASLALAFvlYAASFPSVMDTLTAGTI-TVVFSSMIALMrplkSLTNVN 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 341 QQFATiGTAlgAAASLYEVIDRIPEIDaystEGQ-TPSKISGRISVNKVEFTYPTRaDVKILKGVSLDAQPGQTVALVGS 419
Cdd:PRK11176 306 AQFQR-GMA--ACQTLFAILDLEQEKD----EGKrVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGR 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 420 SGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDV-SDEDIARALKEA 498
Cdd:PRK11176 378 SGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMA 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 499 NAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAH 578
Cdd:PRK11176 458 YAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 17558664 579 RLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQ 620
Cdd:PRK11176 538 RLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
383-620 |
6.53e-104 |
|
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: 328.81 E-value: 6.53e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 543 LLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQ 620
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1005-1277 |
5.74e-103 |
|
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: 339.87 E-value: 5.74e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1005 FNMLEEEPRIDGMTSSGTYPQLSGEVKLNKVFFRY-PERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYD 1083
Cdd:COG5265 333 FDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1084 PLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGlQPGEyTHEQIETACSKANIHKFIDELPDGYETR 1163
Cdd:COG5265 410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG-RPDA-SEEEVEAAARAAQIHDFIESLPDGYDTR 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1164 VGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKN 1243
Cdd:COG5265 488 VGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEA 567
|
250 260 270
....*....|....*....|....*....|....
gi 17558664 1244 GQVVEQGTHNELIAKRGAYFALTQKQSSNQSGGA 1277
Cdd:COG5265 568 GRIVERGTHAELLAQGGLYAQMWARQQEEEEAEE 601
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
693-1265 |
7.01e-102 |
|
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: 335.92 E-value: 7.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 693 FKILRYARPEWIYIFFAIIAALIQGAVMPAFSLFFSQIIN-VFSNPDRdqmkkdGHFWA--LMFLVLAAVQGTSMLFQCS 769
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDdGFGGRDR------SVLWWvpLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 770 LFGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGW 849
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 850 QMAFLVMAIFPFMAVgqalMMKYHGGSATSDAKEMENAGKTAM----EAIENIRTVQALTLQTKLYNIFcshlDAPHGGN 925
Cdd:TIGR02203 155 QLTLIVVVMLPVLSI----LMRRVSKRLRRISKEIQNSMGQVTtvaeETLQGYRVVKLFGGQAYETRRF----DAVSNRN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 926 ISKAIiRGLTYGFANS--IQFFTYAAafrfglflifdknvlmepenVLRVLFAISF----SFGTIGFAASYF------PE 993
Cdd:TIGR02203 227 RRLAM-KMTSAGSISSpiTQLIASLA--------------------LAVVLFIALFqaqaGSLTAGDFTAFItamialIR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 994 YIK------ATFAAGL-----IFNMLEEEPRIDgmTSSGTYPQLSGEVKLNKVFFRYPERpAVPILQGLNVHVKPGQTLA 1062
Cdd:TIGR02203 286 PLKsltnvnAPMQRGLaaaesLFTLLDSPPEKD--TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1063 LVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGlQPGEYTHEQIET 1142
Cdd:TIGR02203 363 LVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYG-RTEQADRAEIER 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1143 ACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTC 1222
Cdd:TIGR02203 442 ALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT 521
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 17558664 1223 IVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFAL 1265
Cdd:TIGR02203 522 LVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1030-1269 |
1.78e-101 |
|
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: 322.26 E-value: 1.78e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPerPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDTSIRENIVYGlQPGEyTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNP 1189
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDA-TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQKQ 1269
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
381-611 |
3.51e-100 |
|
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: 318.40 E-value: 3.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 381 GRISVNKVEFTYptRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL 460
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNP 540
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 541 KILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKG 611
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
192-618 |
1.40e-98 |
|
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: 326.72 E-value: 1.40e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 192 IGGFAVAFT--YDWLLTLIMMslspFMMICGLFLAKLLATAATKEAKQYAVA--GGIAEEVLTSIR---TVIAFNGQEYE 264
Cdd:COG4987 142 VILAAVAFLafFSPALALVLA----LGLLLAGLLLPLLAARLGRRAGRRLAAarAALRARLTDLLQgaaELAAYGALDRA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 265 CKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLeSGTVLTVFFSVMMGS----MALGQAG 340
Cdd:COG4987 218 LARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGAL-SGPLLALLVLAALALfealAPLPAAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 341 QQfatIGTALGAAASLYEVIDRIPEIDAYSTEGQTPSkiSGRISVNKVEFTYPTrADVKILKGVSLDAQPGQTVALVGSS 420
Cdd:COG4987 297 QH---LGRVRAAARRLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 421 GCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANA 500
Cdd:COG4987 371 GSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGL 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 501 ADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRL 580
Cdd:COG4987 451 GDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRL 530
|
410 420 430
....*....|....*....|....*....|....*...
gi 17558664 581 STVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVH 618
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
695-1260 |
6.63e-97 |
|
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: 321.71 E-value: 6.63e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 695 ILRYARPEWIYIFFAIIAALIQGAVMPAFSLFFSQIIN--VFSNPDRDQMKkdghFWALMFLVLAAVQGTSMLFQcSLFG 772
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPLSALL----PLLGLLLAVLLLRALLAWLR-ERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 773 V-AAERLTMRIRSKVYRNVLRQDATYfdMPKHSPGRITTrLATDapNIKSAIDYR---LGSIFNAIASVGGGLGIAFYYG 848
Cdd:COG4988 83 FrAAARVKRRLRRRLLEKLLALGPAW--LRGKSTGELAT-LLTE--GVEALDGYFaryLPQLFLAALVPLLILVAVFPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 849 WQMAFLVMAIFPFMAVGQALMmkyhgGSATSDAKEmenagktameaiENIRTVQALT---------LQT-KLYNifcshL 918
Cdd:COG4988 158 WLSGLILLVTAPLIPLFMILV-----GKGAAKASR------------RQWRALARLSghfldrlrgLTTlKLFG-----R 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 919 DAPHGGNI-------SKAIIRGLTYGFANS--IQFFTYAAAFrfglflifdknvlmepenVLRVLFAISFSFGTIGFAAS 989
Cdd:COG4988 216 AKAEAERIaeasedfRKRTMKVLRVAFLSSavLEFFASLSIA------------------LVAVYIGFRLLGGSLTLFAA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 990 YF-----PEYIK-----ATF---------AAGLIFNMLEEEPRIDGMTSSGTYPQLSGEVKLNKVFFRYPERPavPILQG 1050
Cdd:COG4988 278 LFvlllaPEFFLplrdlGSFyharangiaAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1051 LNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGl 1130
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1131 QPgEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQ 1210
Cdd:COG4988 435 RP-DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEIL 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 17558664 1211 VALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRG 1260
Cdd:COG4988 514 QALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
305-635 |
3.12e-95 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 318.06 E-value: 3.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 305 FWVGTNFVYSGRLESGTVLT-VFFSVMMgsmaLGQAGQQFATIGTALGAAASL---YEVIDRIPEI----DAYStegqtP 376
Cdd:PRK13657 258 LVLGAALVQKGQLRVGEVVAfVGFATLL----IGRLDQVVAFINQVFMAAPKLeefFEVEDAVPDVrdppGAID-----L 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 377 SKISGRISVNKVEFTYPTRAdvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKY 456
Cdd:PRK13657 329 GRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 LRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARAL 536
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 537 VRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHEL 616
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
330
....*....|....*....
gi 17558664 617 VHAQVFADVDDKPKKKEAE 635
Cdd:PRK13657 567 LRAQGMLQEDERRKQPAAE 585
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1028-1260 |
5.75e-92 |
|
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: 295.67 E-value: 5.75e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1028 GEVKLNKVFFRYpeRPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH 1107
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILFDTSIRENIVYGLQpgEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIR 1187
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRP--NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1188 NPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRG 1260
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
734-1269 |
4.72e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 300.78 E-value: 4.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 734 FSNPDRDQMKkdghfW-ALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRL 812
Cdd:PRK11176 56 FGKADRSVLK-----WmPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 813 ATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVGQALM----------MKYHGGSATSDAK 882
Cdd:PRK11176 129 TYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVskrfrnisknMQNTMGQVTTSAE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 883 EMENAGKTAM----EAIENIR--TVQALTLQTKLYNIFCShldaphggNISKAIIRgLTYGFAnsIQFFTYAAAF----- 951
Cdd:PRK11176 209 QMLKGHKEVLifggQEVETKRfdKVSNRMRQQGMKMVSAS--------SISDPIIQ-LIASLA--LAFVLYAASFpsvmd 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 952 --RFGLF-LIFDKNV-LMEPenvLRVLFAISFSFGTiGFAASYfpeyikatfaagLIFNMLEEEPRIDgmtsSGTY--PQ 1025
Cdd:PRK11176 278 tlTAGTItVVFSSMIaLMRP---LKSLTNVNAQFQR-GMAACQ------------TLFAILDLEQEKD----EGKRviER 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1026 LSGEVKLNKVFFRYPERpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLR 1105
Cdd:PRK11176 338 AKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1106 KHIALVSQEPILFDTSIRENIVYGLQpGEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARAL 1185
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIAYART-EQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1186 IRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFAL 1265
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
....
gi 17558664 1266 TQKQ 1269
Cdd:PRK11176 576 HKMQ 579
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
690-1267 |
8.27e-87 |
|
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: 293.98 E-value: 8.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 690 ANLFKILRYARPEWIYIFFAIIAALIqgAVMPAFSLFFSqiinvfSnpdrdqmkkdGhfWalmFLVLAAVQGTSMLFQCS 769
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLL--TLLAGIGLLAL------S----------G--W---LIAAAALAPPILNLFVP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 770 -----LFGVA------AERLT---------MRIRSKVYRNVLRQDATYFdmPKHSPGRITTRLATDapnIKSAIDYRLGS 829
Cdd:COG4987 58 ivgvrAFAIGrtvfryLERLVshdatlrllADLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVAD---VDALDNLYLRV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 830 IFNAIASVGGGLGIAF---YYGWQMAfLVMAIFPFMAVGQALMMKYHGGSATSdAKEMENAGKTAMEAIENIRTVQALTL 906
Cdd:COG4987 133 LLPLLVALLVILAAVAflaFFSPALA-LVLALGLLLAGLLLPLLAARLGRRAG-RRLAAARAALRARLTDLLQGAAELAA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 907 ------QTKLYNIFCSHLDAPHGGNiskAIIRGLTYGFANSIQFFTYAAAFRFGLFLIFDkNVLMEPENVLRVLFAI-SF 979
Cdd:COG4987 211 ygaldrALARLDAAEARLAAAQRRL---ARLSALAQALLQLAAGLAVVAVLWLAAPLVAA-GALSGPLLALLVLAALaLF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 980 -SFGTIGFAASYFPEYIKAtfaAGLIFNMLEEEPRIdGMTSSGTYPQLSGEVKLNKVFFRYPERPAvPILQGLNVHVKPG 1058
Cdd:COG4987 287 eALAPLPAAAQHLGRVRAA---ARRLNELLDAPPAV-TEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1059 QTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLqpGEYTHE 1138
Cdd:COG4987 362 ERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLAR--PDATDE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1139 QIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAK 1218
Cdd:COG4987 440 ELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 17558664 1219 DRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQ 1267
Cdd:COG4987 520 GRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
375-597 |
5.56e-84 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 273.58 E-value: 5.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 375 TPSKISGRISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNI 454
Cdd:cd03248 4 APDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 KYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIAR 534
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 535 ALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQV 597
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
831-1269 |
4.36e-83 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 284.16 E-value: 4.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 831 FNAIASVGGGLGIAFYYGWQMAFL--VMAIFpFMAVGQALMMKYHGGSATSDAKEmENAGKTAMEAIENIRTVQAltlqt 908
Cdd:PRK13657 138 LATLVALVVLLPLALFMNWRLSLVlvVLGIV-YTLITTLVMRKTKDGQAAVEEHY-HDLFAHVSDAIGNVSVVQS----- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 909 klYNIFCSHLDAPHG--GNISKAIIRGLTY-GFANSIQ----FFTYAAAFRFGLFLIFDknvlmepeNVLRVLFAISF-S 980
Cdd:PRK13657 211 --YNRIEAETQALRDiaDNLLAAQMPVLSWwALASVLNraasTITMLAILVLGAALVQK--------GQLRVGEVVAFvG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 981 FGT---------IGFAASYFPEyikatfAAGL--IFNMLEEEPRIDGMTSSGTYPQLSGEVKLNKVFFRYP-ERPAVpil 1048
Cdd:PRK13657 281 FATlligrldqvVAFINQVFMA------APKLeeFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDnSRQGV--- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1049 QGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVY 1128
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRV 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1129 GlQPGEyTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQ 1208
Cdd:PRK13657 432 G-RPDA-TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1209 VQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQKQ 1269
Cdd:PRK13657 510 VKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1026-1246 |
1.56e-82 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 269.34 E-value: 1.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1026 LSGEVKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLR 1105
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1106 KHIALVSQEPILFDTSIRENIVYGLQPGEYthEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARAL 1185
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSF--ECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1186 IRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQV 1246
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
141-621 |
2.50e-82 |
|
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: 285.10 E-value: 2.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 141 QFFHSVMRQEIAWYDKNTSGtlsnklfDNLERVREG-------TGDKVGLAFQMMAQFIGgFAVAFTYDWLLTLIMMSLS 213
Cdd:TIGR01846 217 RLYRHLLGLPLGYFESRRVG-------DTVARVRELeqirnflTGSALTVVLDLLFVVVF-LAVMFFYSPTLTGVVIGSL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 214 PFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFLIGAGLASF 293
Cdd:TIGR01846 289 VCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAI 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 294 FVIIYASYCLAFWVGTNFVYSGRLESGTVltVFFSVMMGSMA-----LGQAGQQFATIGTALgaaASLYEVIDRIPEidA 368
Cdd:TIGR01846 369 ELIQKLTFAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpvlrLAQLWQDFQQTGIAL---ERLGDILNSPTE--P 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 369 YSTEGQTPSKISGRISVNKVEFTYPTRADVkILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID--D 446
Cdd:TIGR01846 442 RSAGLAALPELRGAITFENIRFRYAPDSPE-VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDgvD 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 447 IPIEDFNikYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQ 526
Cdd:TIGR01846 521 LAIADPA--WLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQ 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 527 KQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETL 606
Cdd:TIGR01846 599 RQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
490
....*....|....*
gi 17558664 607 IEQKGLYHELVHAQV 621
Cdd:TIGR01846 679 LALQGLYARLWQQQS 693
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
383-620 |
5.76e-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: 268.20 E-value: 5.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptRADVK-ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID--DIPIEDFNikYLRQ 459
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghDLALADPA--WLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRN 539
Cdd:cd03252 77 QVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 540 PKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHA 619
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 17558664 620 Q 620
Cdd:cd03252 237 Q 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
383-596 |
1.35e-80 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 261.55 E-value: 1.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRaDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIrygrsdvsdediaralkeanaadfiktfpeglntlvgdrgvqMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 543 LLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQ 596
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
133-618 |
6.88e-79 |
|
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: 275.67 E-value: 6.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 133 KLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNK--LFDNLERVREGTGDKVGLAFQMMAQFiggFAVAFTYDWLLTLIMM 210
Cdd:TIGR03796 224 KLAVGMSARFLWHILRLPVRFFAQRHAGDIASRvqLNDQVAEFLSGQLATTALDAVMLVFY---ALLMLLYDPVLTLIGI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 211 SLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAfNGQEYECKR-----YEDALEHGKKTGIKKSFL 285
Cdd:TIGR03796 301 AFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKA-SGLESDFFSrwagyQAKLLNAQQELGVLTQIL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 286 igAGLASFFVIIyaSYCLAFWVGTNFVYSGRLESGTvLTVFFSVMMGSMA-------LGQAGQQFAtigtalGAAASLYE 358
Cdd:TIGR03796 380 --GVLPTLLTSL--NSALILVVGGLRVMEGQLTIGM-LVAFQSLMSSFLEpvnnlvgFGGTLQELE------GDLNRLDD 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 359 VIDRIPEIDAYSTEGQT-----PSKISGRISVNKVEFTYpTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQR 433
Cdd:TIGR03796 449 VLRNPVDPLLEEPEGSAatsepPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAG 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 434 FYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNT 513
Cdd:TIGR03796 528 LYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDA 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 514 LVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALenASRGRTTIVIAHRLSTVRNADKIIVMK 593
Cdd:TIGR03796 608 ELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLE 685
|
490 500
....*....|....*....|....*
gi 17558664 594 AGQVMEVGTHETLIEQKGLYHELVH 618
Cdd:TIGR03796 686 RGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1030-1245 |
7.43e-79 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 256.93 E-value: 7.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAvPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDTSIRENIvyglqpgeytheqietacskanihkfidelpdgyetrvgekgtqLSGGQKQRIAIARALIRNP 1189
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQ 1245
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1030-1269 |
3.54e-78 |
|
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: 257.80 E-value: 3.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYpeRPAVP-ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHI 1108
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1109 ALVSQEPILFDTSIRENIVYGlQPGEYTHEQIETAcSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRN 1188
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAA-KLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1189 PKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQK 1268
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 17558664 1269 Q 1269
Cdd:cd03252 237 Q 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
196-592 |
5.05e-77 |
|
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: 264.92 E-value: 5.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 196 AVAFTYDWLLTLIMMSLSP----FMMICGLFlakllatAATKEAKQYAVAGGIAEEVLTSIR---TVIAFNGQEYECKR- 267
Cdd:TIGR02857 137 AAVFPQDWISGLILLLTAPlipiFMILIGWA-------AQAAARKQWAALSRLSGHFLDRLRglpTLKLFGRAKAQAAAi 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 268 YEDALEHGKKT--GIKKSFLIGAGL---ASFFVIIYASYclafwVGTNFVYsGRLESGTVLTV------FFsvmmgsMAL 336
Cdd:TIGR02857 210 RRSSEEYRERTmrVLRIAFLSSAVLelfATLSVALVAVY-----IGFRLLA-GDLDLATGLFVlllapeFY------LPL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 337 GQAGQQFATIGTALGAAASLYEVIDRIPEIDAYSTEgqTPSKISGRISVNKVEFTYPTRADVkiLKGVSLDAQPGQTVAL 416
Cdd:TIGR02857 278 RQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVAL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 417 VGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALK 496
Cdd:TIGR02857 354 VGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 497 EANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVI 576
Cdd:TIGR02857 434 RAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLV 513
|
410
....*....|....*.
gi 17558664 577 AHRLSTVRNADKIIVM 592
Cdd:TIGR02857 514 THRLALAALADRIVVL 529
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
695-1270 |
7.33e-77 |
|
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: 269.30 E-value: 7.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 695 ILRYaRPEWIYIFFAIIAALIQGAVMPafsLFFSQIIN-VFSNPDRDQMkkdgHFWALMFLVLAAVQGTSMLFQCSLFGV 773
Cdd:TIGR01846 134 IIRY-RKQFREVLLISLALQLFALVTP---LLFQVVIDkVLVHRGLSTL----SVLALAMLAVAIFEPALGGLRTYLFAH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 774 AAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLaTDAPNIK-----SAIDYRLGSIFNAIAsvgggLGIAFYYG 848
Cdd:TIGR01846 206 LTSRIDVELGARLYRHLLGLPLGYFE--SRRVGDTVARV-RELEQIRnfltgSALTVVLDLLFVVVF-----LAVMFFYS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 849 WQMAFLVMAIFPF-----MAVGQALMMKYhggsatsDAKEMENAGKTAM--EAIENIRTVQALTLQTKLYNIFCSHL--- 918
Cdd:TIGR01846 278 PTLTGVVIGSLVCyallsVFVGPILRKRV-------EDKFERSAAATSFlvESVTGIETIKATATEPQFQNRWDRQLaay 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 919 -----DAPHGGNISKAIIrGLtygfansIQFFTYAAAFRFGLFLIFDKNvLMEPENVLRVLFAISFSfGTIGFAASYFPE 993
Cdd:TIGR01846 351 vaasfRVTNLGNIAGQAI-EL-------IQKLTFAILLWFGAHLVIGGA-LSPGQLVAFNMLAGRVT-QPVLRLAQLWQD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 994 YIKATFAAGLIFNMLEEePRIDGMTSSGTYPQLSGEVKLNKVFFRY-PERPavPILQGLNVHVKPGQTLALVGPSGCGKS 1072
Cdd:TIGR01846 421 FQQTGIALERLGDILNS-PTEPRSAGLAALPELRGAITFENIRFRYaPDSP--EVLSNLNLDIKPGEFIGIVGPSGSGKS 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1073 TVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGlQPGeYTHEQIETACSKANIHKF 1152
Cdd:TIGR01846 498 TLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC-NPG-APFEHVIHAAKLAGAHDF 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1153 IDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTI 1232
Cdd:TIGR01846 576 ISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTV 655
|
570 580 590
....*....|....*....|....*....|....*...
gi 17558664 1233 VNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQKQS 1270
Cdd:TIGR01846 656 RACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
42-366 |
1.28e-76 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 256.22 E-value: 1.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 42 DRLMLAVGIIVSCATGVGLPLMSIIMGNVSQNFVTLGTifldpnstasekaaarAEFSHEVIQNCLKYVYLGCGIFAAGF 121
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDD----------------DELRSEANFWALMFLVLAIVAGIAYF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 122 LQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYD--KNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAF 199
Cdd:cd18578 71 LQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 200 TYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTG 279
Cdd:cd18578 151 VYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 280 IKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIGTALGAAASLYEV 359
Cdd:cd18578 231 LRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRL 310
|
....*..
gi 17558664 360 IDRIPEI 366
Cdd:cd18578 311 LDRKPEI 317
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
706-1265 |
2.74e-75 |
|
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: 265.27 E-value: 2.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAAL---IQGAVMPAFSLFFSQIINVFSNPDrdqmkkdghfW-----ALMFLVlAAVQGTSMLFQCSLFGVAAER 777
Cdd:TIGR03796 156 LLYLLLAGLllvLPGLVIPAFSQIFVDEILVQGRQD----------WlrpllLGMGLT-ALLQGVLTWLQLYYLRRLEIK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 778 LTMRIRSKVYRNVLRQDATYFDMpkHSPGRITTRLATDApNIKSAIDYRLgsifnaIASVGGGLGIAFY------YGWQM 851
Cdd:TIGR03796 225 LAVGMSARFLWHILRLPVRFFAQ--RHAGDIASRVQLND-QVAEFLSGQL------ATTALDAVMLVFYallmllYDPVL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 852 AFLVMAifpfMAVGQALMMKYHGGS-ATSDAKEMENAGK---TAMEAIENIRTVQALTLQ----TKLYNIFCSHLDAPHG 923
Cdd:TIGR03796 296 TLIGIA----FAAINVLALQLVSRRrVDANRRLQQDAGKltgVAISGLQSIETLKASGLEsdffSRWAGYQAKLLNAQQE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 924 GNISKAIIRGLtygfANSIQFFTYAAAFRFGLFLIFDKNVLMepeNVLRVLFAISFSF-----GTIGFAASyFPEyikat 998
Cdd:TIGR03796 372 LGVLTQILGVL----PTLLTSLNSALILVVGGLRVMEGQLTI---GMLVAFQSLMSSFlepvnNLVGFGGT-LQE----- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 999 FAAGLI---------FNMLEEEPRIDGMTSsGTYPQLSGEVKLNKVFFRYpERPAVPILQGLNVHVKPGQTLALVGPSGC 1069
Cdd:TIGR03796 439 LEGDLNrlddvlrnpVDPLLEEPEGSAATS-EPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGS 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1070 GKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVygLQPGEYTHEQIETACSKANI 1149
Cdd:TIGR03796 517 GKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLT--LWDPTIPDADLVRACKDAAI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1150 HKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVqvalDAAAKDR--TCIVVAH 1227
Cdd:TIGR03796 595 HDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII----DDNLRRRgcTCIIVAH 670
|
570 580 590
....*....|....*....|....*....|....*...
gi 17558664 1228 RLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFAL 1265
Cdd:TIGR03796 671 RLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
195-620 |
1.70e-74 |
|
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: 262.20 E-value: 1.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 195 FAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATaatKEAKQYAVAGGIAEEVL------TSIRTVIAFNGQEYE-CKR 267
Cdd:TIGR03797 267 LGLMFYYSWKLALVAVALALVAIAVTLVLGLLQVR---KERRLLELSGKISGLTVqlingiSKLRVAGAENRAFARwAKL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 268 YEDALEHGKKTGIKKSFL--IGAGLASFFVIIyasyclAFWVGTNFVYSGRLESGTVLTVF--FSVMMGSMAlgqagqQF 343
Cdd:TIGR03797 344 FSRQRKLELSAQRIENLLtvFNAVLPVLTSAA------LFAAAISLLGGAGLSLGSFLAFNtaFGSFSGAVT------QL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 344 ATIGTALGAAASLYE----VIDRIPEIDAYSTEgqtPSKISGRISVNKVEFTYptRAD-VKILKGVSLDAQPGQTVALVG 418
Cdd:TIGR03797 412 SNTLISILAVIPLWErakpILEALPEVDEAKTD---PGKLSGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 419 SSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIrYGRSDVSDEDIARALKEA 498
Cdd:TIGR03797 487 PSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 499 NAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALE--NASRgrttIVI 576
Cdd:TIGR03797 566 GLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLErlKVTR----IVI 641
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 17558664 577 AHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQ 620
Cdd:TIGR03797 642 AHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
365-1267 |
1.16e-73 |
|
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: 270.28 E-value: 1.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 365 EIDAYSTEGQTPSKISGR-ISVNKVEFTYpTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQIl 443
Cdd:TIGR00957 618 ELEPDSIERRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 444 iddipiedfnikYLRQLVGVVSQEPNLFNTSIEQNIRYGRSdvSDEDIARALKEANA--ADfIKTFPEGLNTLVGDRGVQ 521
Cdd:TIGR00957 696 ------------HMKGSVAYVPQQAWIQNDSLRENILFGKA--LNEKYYQQVLEACAllPD-LEILPSGDRTEIGEKGVN 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 522 MSGGQKQRIAIARALVRNPKILLLDEATSALDAE-SESIVQSAL--ENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVM 598
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 599 EVGTHETLIEQKGLYHELVHAQVFADVD--------------DKPKK-------------KEAERRMSRQTSQRKGSVNF 651
Cdd:TIGR00957 841 EMGSYQELLQRDGAFAEFLRTYAPDEQQghledswtalvsgeGKEAKliengmlvtdvvgKQLQRQLSASSSDSGDQSRH 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 652 --KTQESQVDEKPGAPPapeaaekeiKRLKKELEEEGAVKANLFkiLRYARPEWIYIFFAIIAALI-QGAVMPAFSLFFS 728
Cdd:TIGR00957 921 hgSSAELQKAEAKEETW---------KLMEADKAQTGQVELSVY--WDYMKAIGLFITFLSIFLFVcNHVSALASNYWLS 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 729 QIIN--VFSNPDRDQMKKDGHFWALMFLVLAAVQGTSMlfQCSLFGVAAERltmRIRSKVYRNVLRQDATYFDmpKHSPG 806
Cdd:TIGR00957 990 LWTDdpMVNGTQNNTSLRLSVYGALGILQGFAVFGYSM--AVSIGGIQASR---VLHQDLLHNKLRSPMSFFE--RTPSG 1062
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 807 RITTRLATDAPNIKS----AIDYRLGSIFNAIASVggglgIAFYYGWQMAFLVMaifPFMAVGQALMMKYHGGSaTSDAK 882
Cdd:TIGR00957 1063 NLVNRFSKELDTVDSmippVIKMFMGSLFNVIGAL-----IVILLATPIAAVII---PPLGLLYFFVQRFYVAS-SRQLK 1133
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 883 EMENAGKTAM-----EAIENIRTVQALTLQTKLYNIFCSHLDAphggniskaiirgltygfaNSIQFFTYAAAFRF-GLF 956
Cdd:TIGR00957 1134 RLESVSRSPVyshfnETLLGVSVIRAFEEQERFIHQSDLKVDE-------------------NQKAYYPSIVANRWlAVR 1194
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 957 LIFDKNVLMepenVLRVLFAI----SFSFGTIGFAASYfpeYIKATFAAGLIFNML--------------------EEEP 1012
Cdd:TIGR00957 1195 LECVGNCIV----LFAALFAVisrhSLSAGLVGLSVSY---SLQVTFYLNWLVRMSsemetnivaverlkeyseteKEAP 1267
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1013 -RIDGMTSSGTYPQlSGEVKLNKVFFRYpeRPAVP-ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVT 1090
Cdd:TIGR00957 1268 wQIQETAPPSGWPP-RGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII 1344
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1091 VDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENivygLQP-GEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGT 1169
Cdd:TIGR00957 1345 IDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN----LDPfSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE 1420
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1170 QLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQ 1249
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
970
....*....|....*...
gi 17558664 1250 GTHNELIAKRGAYFALTQ 1267
Cdd:TIGR00957 1501 GAPSNLLQQRGIFYSMAK 1518
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-353 |
4.23e-73 |
|
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: 246.42 E-value: 4.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 48 VGIIVSCATGVGLPLMSIIMGNVSQNFVTLGTIFLDPNSTA-SEKAAARAEFSHEVIQNCLKYVYLGCGIFAAGFLQASC 126
Cdd:cd18558 3 VGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGlNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 127 FMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLLT 206
Cdd:cd18558 83 WGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 207 LIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFLI 286
Cdd:cd18558 163 LVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 287 GAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIGTALGAA 353
Cdd:cd18558 243 NISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAA 309
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
129-617 |
4.30e-69 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 255.72 E-value: 4.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 129 VICEKLSNRFRRQFFHSVMRQEIAWYD--KNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLLT 206
Cdd:PTZ00265 892 VIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVA 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 207 LIMMSLSPFMMICGLFLAKLLATAATkEAKQYAVAGGI----------------AEEVLTSIRTVIAFNGQEYECKRYED 270
Cdd:PTZ00265 972 AVLTGTYFIFMRVFAIRARLTANKDV-EKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 271 ALEHGKKtGIKKSFLIGAGL------ASFFViiyasYCLAFWVGTNFVYSGRLESGTVLTVFFS-VMMGSMAlgqaGQQF 343
Cdd:PTZ00265 1051 AIDYSNK-GQKRKTLVNSMLwgfsqsAQLFI-----NSFAYWFGSFLIRRGTILVDDFMKSLFTfLFTGSYA----GKLM 1120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 344 ATIGTALGAAASL---YEVIDRIPEIDAYSTEG---QTPSKISGRISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALV 417
Cdd:PTZ00265 1121 SLKGDSENAKLSFekyYPLIIRKSNIDVRDNGGiriKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 418 GSSGCGKSTIIQLLQRFYN------------------------------------------------------PDAGQIL 443
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKIL 1280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 444 IDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMS 523
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLS 1360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 524 GGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENA--SRGRTTIVIAHRLSTVRNADKIIVM----KAGQV 597
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSF 1440
|
570 580
....*....|....*....|..
gi 17558664 598 MEV-GTHETLIE-QKGLYHELV 617
Cdd:PTZ00265 1441 VQAhGTHEELLSvQDGVYKKYV 1462
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
133-633 |
4.76e-69 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 243.47 E-value: 4.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 133 KLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVglaFQMMAQFIGGFAVAFTY----DWLLTLI 208
Cdd:PRK10789 66 QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGV---LTLVDSLVMGCAVLIVMstqiSWQLTLL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 209 MMSLSPFMMIC------GLFLAKLLATAAtkeakqYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYE-DALEHGKKtgik 281
Cdd:PRK10789 143 ALLPMPVMAIMikrygdQLHERFKLAQAA------FSSLNDRTQESLTSIRMIKAFGLEDRQSALFAaDAEDTGKK---- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 282 kSFLIGAGLASF----FVIIYASYCLAFWVGTNFVYSGRLESGTvLTVFfsVM-MGSM-----ALGQagqQFATIGTALG 351
Cdd:PRK10789 213 -NMRVARIDARFdptiYIAIGMANLLAIGGGSWMVVNGSLTLGQ-LTSF--VMyLGLMiwpmlALAW---MFNIVERGSA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 352 AAASLYEVIDRIPEIDaystEGQTP-SKISGRISVNKVEFTYPTrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQL 430
Cdd:PRK10789 286 AYSRIRAMLAEAPVVK----DGSEPvPEGRGELDVNIRQFTYPQ-TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 431 LQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEG 510
Cdd:PRK10789 361 IQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 511 LNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKII 590
Cdd:PRK10789 441 YDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEIL 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 17558664 591 VMKAGQVMEVGTHETLIEQKGLYHELVH-AQVFADVDDKPKKKE 633
Cdd:PRK10789 521 VMQHGHIAQRGNHDQLAQQSGWYRDMYRyQQLEAALDDAPEIRE 564
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
325-618 |
1.61e-68 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 242.04 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 325 VFFSVMMGSMALGQAGQQFATIGTALGAAASLYEVIDRIPEIDaYSTEGQTPSKiSGRISVNKVEFTYPTRADvKILKGV 404
Cdd:PRK11160 283 FVFAALAAFEALMPVAGAFQHLGQVIASARRINEITEQKPEVT-FPTTSTAAAD-QVSLTLNNVSFTYPDQPQ-PVLKGL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 405 SLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRS 484
Cdd:PRK11160 360 SLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 485 DVSDEDIARALKEANAADFIKTfPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSAL 564
Cdd:PRK11160 440 NASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL 518
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 565 ENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVH 618
Cdd:PRK11160 519 AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
383-1263 |
4.62e-68 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 252.59 E-value: 4.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLqrfynpdagqiLIDDIPIEDFNIKyLRQLVG 462
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-----------LGELSHAETSSVV-IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIRYGrSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKI 542
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 543 LLLDEATSALDAE-SESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQv 621
Cdd:PLN03232 762 YIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENA- 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 622 fADVDDKPKKKEAERRMSRQTSqrkgsvnfkTQESQVDEKPGAPPAPEAAEKEIkRLKKELEEEGAVKANLfkILRYARP 701
Cdd:PLN03232 841 -GKMDATQEVNTNDENILKLGP---------TVTIDVSERNLGSTKQGKRGRSV-LVKQEERETGIISWNV--LMRYNKA 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 702 -EWIYIFFAIIAALIQGAVMPAFSlffSQIINVFSNPDRDQMKKDGHF---WALMFLVLAAVQGTSMLFQCSLFGVAAER 777
Cdd:PLN03232 908 vGGLWVVMILLVCYLTTEVLRVSS---STWLSIWTDQSTPKSYSPGFYivvYALLGFGQVAVTFTNSFWLISSSLHAAKR 984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 778 LtmriRSKVYRNVLRQDATYFDMpkHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVgggLGIAFYYGWQMAFLVMA 857
Cdd:PLN03232 985 L----HDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQL---LSTFALIGTVSTISLWA 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 858 IFPFMAVGQALMMKYHggSATSDAKEMENAGKTAM-----EAIENIRTVQALTLQTKLYNIFCSHLDaphgGNISKAI-- 930
Cdd:PLN03232 1056 IMPLLILFYAAYLYYQ--STSREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKINGKSMD----NNIRFTLan 1129
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 931 --------IRGLTYGFANSIQFFTYAA------------AFRFGLFLIFDKNVLMEPENVLRVLFAISFSFGTIGFAASY 990
Cdd:PLN03232 1130 tssnrwltIRLETLGGVMIWLTATFAVlrngnaenqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNY 1209
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 991 FpeyikatfaaglifNMLEEEPRIDGMTSSGTYPQLSGEVKLNKVFFRY-PERPavPILQGLNVHVKPGQTLALVGPSGC 1069
Cdd:PLN03232 1210 I--------------DLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYrPGLP--PVLHGLSFFVSPSEKVGVVGRTGA 1273
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1070 GKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIvyglQP-GEYTHEQIETACSKAN 1148
Cdd:PLN03232 1274 GKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI----DPfSEHNDADLWEALERAH 1349
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1149 IHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHR 1228
Cdd:PLN03232 1350 IKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHR 1429
|
890 900 910
....*....|....*....|....*....|....*
gi 17558664 1229 LSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYF 1263
Cdd:PLN03232 1430 LNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
381-602 |
2.56e-67 |
|
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: 226.22 E-value: 2.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 381 GRISVNKVEFTYPTRADVkILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL 460
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLFNTSIEQNIR-YGRSdvSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRN 539
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDpFGEY--SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 540 PKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGT 602
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1028-1250 |
5.50e-67 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 225.16 E-value: 5.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1028 GEVKLNKVFFRYPERPaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH 1107
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILFDTSIRENIVYGLQPGeyTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIR 1187
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1188 NPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQG 1250
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
381-597 |
5.54e-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: 222.46 E-value: 5.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 381 GRISVNKVEFTYPTrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL 460
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNP 540
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 541 KILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQV 597
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
740-1269 |
1.04e-65 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 234.23 E-value: 1.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 740 DQMKKDGHF-------WALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRL 812
Cdd:PRK10790 51 DNMVAKGNLplglvagLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD--TQPVGQLISRV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 813 ATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVgqaLMMKYHGGSaTSDAKEME------N 886
Cdd:PRK10790 129 TNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLV---VMVIYQRYS-TPIVRRVRayladiN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 887 AGKTamEAIENIRTVQALTLQTKLynifcshldaphggniskaiirGLTYGFANSIQFFTYAAAFRFGLFLI------FD 960
Cdd:PRK10790 205 DGFN--EVINGMSVIQQFRQQARF----------------------GERMGEASRSHYMARMQTLRLDGFLLrpllslFS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 961 KNVLMEpenvLRVLFAISfSFGTIGFAASY-FPEYI------------------KATFAAGLIFNMLEEEPRIDGmtsSG 1021
Cdd:PRK10790 261 ALILCG----LLMLFGFS-ASGTIEVGVLYaFISYLgrlneplielttqqsmlqQAVVAGERVFELMDGPRQQYG---ND 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1022 TYPQLSGEVKLNKVFFRYpeRPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNP 1101
Cdd:PRK10790 333 DRPLQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1102 KHLRKHIALVSQEPILFDTSIRENIVYGLqpgEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAI 1181
Cdd:PRK10790 411 SVLRQGVAMVQQDPVVLADTFLANVTLGR---DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1182 ARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGA 1261
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGR 567
|
....*...
gi 17558664 1262 YFALTQKQ 1269
Cdd:PRK10790 568 YWQMYQLQ 575
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
196-580 |
6.48e-65 |
|
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: 230.33 E-value: 6.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 196 AVAFTYDWLLTLIMMSlspfMMICGLFLAKLLATAATKEAKQYAVA--GGIAEEVLTSIR---TVIAFNGQEYECKRYED 270
Cdd:TIGR02868 146 AAIAVLSVPAALILAA----GLLLAGFVAPLVSLRAARAAEQALARlrGELAAQLTDALDgaaELVASGALPAALAQVEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 271 ALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLeSGTVLTVF----FSVMMGSMALGQAGQQfatI 346
Cdd:TIGR02868 222 ADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRL-APVTLAVLvllpLAAFEAFAALPAAAQQ---L 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 347 GTALGAAASLYEVIDRIPEIDAYSTEGQTPSKISG-RISVNKVEFTYPTRADVkiLKGVSLDAQPGQTVALVGSSGCGKS 425
Cdd:TIGR02868 298 TRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 426 TIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIK 505
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLR 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 506 TFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRL 580
Cdd:TIGR02868 456 ALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1028-1251 |
8.81e-65 |
|
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: 218.90 E-value: 8.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1028 GEVKLNKVFFRYPErPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH 1107
Cdd:cd03244 1 GDIEFKNVSLRYRP-NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILFDTSIRENivygLQP-GEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALI 1186
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSN----LDPfGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1187 RNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGT 1251
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
706-1004 |
9.47e-65 |
|
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: 221.96 E-value: 9.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIINVFSN-----PDRDQMKKDGHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTM 780
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDfgsgeSSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 781 RIRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFP 860
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 861 FMAVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGLTYGFAN 940
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 941 SIQFFTYAAAFRFGLFLIFDKNvlMEPENVLRVLFAISFSFGTIGFAASYFPEYIKATFAAGLI 1004
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGE--ISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
111-620 |
5.97e-64 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 229.22 E-value: 5.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 111 YLGCGIFAAG--FLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMM 188
Cdd:PRK10790 71 YVGLQLLAAGlhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 189 AqFIGGFAVA-FTYDWLLTLIMMSLSPFMMICgLFLAKLLATAATKEAKQYavaggIAE------EVLTSIRTVIAFNGQ 261
Cdd:PRK10790 151 A-LIGAMLVAmFSLDWRMALVAIMIFPAVLVV-MVIYQRYSTPIVRRVRAY-----LADindgfnEVINGMSVIQQFRQQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 262 EYECKRYEDA-LEHGK---KTGIKKSFLIGAGLASFFVIIYASYCLAFwvgtNFVYSGRLESGtVLTVFFSvMMGSM--A 335
Cdd:PRK10790 224 ARFGERMGEAsRSHYMarmQTLRLDGFLLRPLLSLFSALILCGLLMLF----GFSASGTIEVG-VLYAFIS-YLGRLneP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 336 LGQAGQQFATIGTALGAAASLYEVIDRIPEidAYSTEGQTPSkiSGRISVNKVEFTYptRADVKILKGVSLDAQPGQTVA 415
Cdd:PRK10790 298 LIELTTQQSMLQQAVVAGERVFELMDGPRQ--QYGNDDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 416 LVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRsDVSDEDIARAL 495
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQAL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 496 KEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALEnASRGRTT-I 574
Cdd:PRK10790 451 ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA-AVREHTTlV 529
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 17558664 575 VIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQ 620
Cdd:PRK10790 530 VIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
383-1264 |
8.59e-64 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 239.25 E-value: 8.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQllqrfynpdagQILIDDIPIEDFNIkYLRQLVG 462
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS-----------AMLGELPPRSDASV-VIRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIRYGrSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKI 542
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 543 LLLDEATSALDAE-SESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELV-HAQ 620
Cdd:PLN03130 762 YIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMeNAG 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 621 VFADVDDKPKKKEAERRMSRQTSQRKGSvNFKTQESQVDEKPGAPPAPeaaekeikrLKKELEEEGAVKANLFKilRYAR 700
Cdd:PLN03130 842 KMEEYVEENGEEEDDQTSSKPVANGNAN-NLKKDSSSKKKSKEGKSVL---------IKQEERETGVVSWKVLE--RYKN 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 701 P---EWI--YIFFAIIAAliqgavmPAFSLFFSQIINVFSNPDRDQMKKDGHF---WALMFL--VLAAVQGTSMLFQCSL 770
Cdd:PLN03130 910 AlggAWVvmILFLCYVLT-------EVFRVSSSTWLSEWTDQGTPKTHGPLFYnliYALLSFgqVLVTLLNSYWLIMSSL 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 771 FgvAAERLtmriRSKVYRNVLRQDATYFdmpkHS-P-GRITTRLATDAPNIKSAI----DYRLGSIFNAIASVggglgia 844
Cdd:PLN03130 983 Y--AAKRL----HDAMLGSILRAPMSFF----HTnPlGRIINRFAKDLGDIDRNVavfvNMFLGQIFQLLSTF------- 1045
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 845 FYYGWQMAFLVMAIFPFMAVGQALMMKYHggSATSDAKEMENAGKTAM-----EAIENIRTVQALTLQTKLYNIFCSHLD 919
Cdd:PLN03130 1046 VLIGIVSTISLWAIMPLLVLFYGAYLYYQ--STAREVKRLDSITRSPVyaqfgEALNGLSTIRAYKAYDRMAEINGRSMD 1123
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 920 -------APHGGNISKAI----IRGLTYGFANSIQFFTYA-----AAF--RFGLFLIFDKNVLMEPENVLRVLFAISFSF 981
Cdd:PLN03130 1124 nnirftlVNMSSNRWLAIrletLGGLMIWLTASFAVMQNGraenqAAFasTMGLLLSYALNITSLLTAVLRLASLAENSL 1203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 982 GTIGFAASY--FPEyikatfaaglifnmlEEEPRIDGMTSSGTYPqLSGEVKLNKVFFRY-PERPavPILQGLNVHVKPG 1058
Cdd:PLN03130 1204 NAVERVGTYidLPS---------------EAPLVIENNRPPPGWP-SSGSIKFEDVVLRYrPELP--PVLHGLSFEISPS 1265
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1059 QTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENivygLQP-GEYTH 1137
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN----LDPfNEHND 1341
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1138 EQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAA 1217
Cdd:PLN03130 1342 ADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEF 1421
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 17558664 1218 KDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFA 1264
Cdd:PLN03130 1422 KSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1000-1262 |
1.62e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 224.21 E-value: 1.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1000 AAGLIFNMLEEEPRI-DGmtsSGTYPQLSGEVKLNKVFFRYPERpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLL 1078
Cdd:PRK10789 286 AYSRIRAMLAEAPVVkDG---SEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1079 ERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGlQPGEyTHEQIETACSKANIHKFIDELPD 1158
Cdd:PRK10789 362 QRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG-RPDA-TQQEIEHVARLASVHDDILRLPQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1159 GYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCI 1238
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEI 519
|
250 260
....*....|....*....|....
gi 17558664 1239 MVVKNGQVVEQGTHNELIAKRGAY 1262
Cdd:PRK10789 520 LVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
706-1274 |
1.11e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 232.23 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQII-NVFSNPDRDQMkkdghfwaLMFLVLAAVQGTSMLFQCSL-FGVAAERLTMRIR 783
Cdd:PTZ00265 62 LGVSFVCATISGGTLPFFVSVFGVIMkNMNLGENVNDI--------IFSLVLIGIFQFILSFISSFcMDVVTTKILKTLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 784 SKVYRNVLRQDATYFDmpkHSPG-RITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFM 862
Cdd:PTZ00265 134 LEFLKSVFYQDGQFHD---NNPGsKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 863 AVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFcSHLDAPHGGNISKA-IIRGLTYGFANS 941
Cdd:PTZ00265 211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKF-NLSEKLYSKYILKAnFMESLHIGMING 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 942 IQFFTYAAAFRFGLFLIFDKNVLMEPEN------VLRVLFAISFSFGTIGFAASYFPEYIKATFAAGLIFNMLEEEPRID 1015
Cdd:PTZ00265 290 FILASYAFGFWYGTRIIISDLSNQQPNNdfhggsVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1016 GMTSSGTYPQLSgEVKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTV-DNN 1094
Cdd:PTZ00265 370 NNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSH 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1095 DLRQMNPKHLRKHIALVSQEPILFDTSIRENI---VYGLQPGEYTHEQIE------------------------------ 1141
Cdd:PTZ00265 449 NLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkysLYSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndmsnt 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1142 ----------------------TACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATS 1199
Cdd:PTZ00265 529 tdsneliemrknyqtikdsevvDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1200 ALDTESEKQVQVALD--AAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQ-------------------------------- 1245
Cdd:PTZ00265 609 SLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnn 688
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 17558664 1246 ---------------VVEQGTHNELIA-KRGAYFAL--TQKQSSNQS 1274
Cdd:PTZ00265 689 nnnnnnnkinnagsyIIEQGTHDALMKnKNGIYYTMinNQKVSSKKS 735
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1010-1265 |
2.54e-61 |
|
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: 221.30 E-value: 2.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1010 EEPridgmTSSGTYPQLSGEVKLNKVFFRYPERPavpilQG---LNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLE 1086
Cdd:TIGR01192 320 EEP-----ADAPELPNVKGAVEFRHITFEFANSS-----QGvfdVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTV 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1087 GAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLQPGeyTHEQIETACSKANIHKFIDELPDGYETRVGE 1166
Cdd:TIGR01192 390 GQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGA--TDEEVYEAAKAAAAHDFILKRSNGYDTLVGE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1167 KGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQV 1246
Cdd:TIGR01192 468 RGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRL 547
|
250
....*....|....*....
gi 17558664 1247 VEQGTHNELIAKRGAYFAL 1265
Cdd:TIGR01192 548 IEKGSFQELIQKDGRFYKL 566
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
695-1269 |
1.11e-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: 221.75 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 695 ILRYARPEWIYIFFAIIAALIQGAVMP-AFSLFFSQIInvfsnPDRDQmkkdGHFWAlMFLVLAAVQGTSMLFQCSLfGV 773
Cdd:TIGR03797 130 ALRGARRDLLAILAMGLLGTLLGMLVPiATGILIGTAI-----PDADR----SLLVQ-IALALLAAAVGAAAFQLAQ-SL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 774 AAERL----TMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRlatdAPNIkSAIDYRLGS--IFNAIASVGG--GLGIAF 845
Cdd:TIGR03797 199 AVLRLetrmDASLQAAVWDRLLRLPVSFFR--QYSTGDLASR----AMGI-SQIRRILSGstLTTLLSGIFAllNLGLMF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 846 YYGWQMAFLVMAIFPF----MAVGQALMMKYHGgsatsdaKEMENAGKTAMEAIENIR----------TVQALTLQTKLY 911
Cdd:TIGR03797 272 YYSWKLALVAVALALVaiavTLVLGLLQVRKER-------RLLELSGKISGLTVQLINgisklrvagaENRAFARWAKLF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 912 NifcshldAPHGGNISKAIIRGLTYGFANSIQFFTYAAAFRFGLFLifdknvlmepenvlrvLFAISFSFGT-IGFAASy 990
Cdd:TIGR03797 345 S-------RQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAISL----------------LGGAGLSLGSfLAFNTA- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 991 FPEYIKAT--FAAGLIFNM------------LEEEPRIDGmtsSGTYP-QLSGEVKLNKVFFRY-PERPavPILQGLNVH 1054
Cdd:TIGR03797 401 FGSFSGAVtqLSNTLISILaviplwerakpiLEALPEVDE---AKTDPgKLSGAIEVDRVTFRYrPDGP--LILDDVSLQ 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1055 VKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLQpge 1134
Cdd:TIGR03797 476 IEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAP--- 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1135 YTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALD 1214
Cdd:TIGR03797 553 LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLE 632
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1215 AAAKDRtcIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQKQ 1269
Cdd:TIGR03797 633 RLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
349-621 |
3.33e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 217.79 E-value: 3.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 349 ALGAAASLYEVIDrIPEIDAYSTEGQTPSKISGRISVNKVEFTYPtraDVKILKG-VSLDAQPGQTVALVGSSGCGKSTI 427
Cdd:PRK11174 317 AVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIEAEDLEILSP---DGKTLAGpLNFTLPAGQRIALVGPSGAGKTSL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 428 IQLLQRFYnPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTF 507
Cdd:PRK11174 393 LNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 508 PEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNAD 587
Cdd:PRK11174 472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWD 551
|
250 260 270
....*....|....*....|....*....|....
gi 17558664 588 KIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQV 621
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1024-1258 |
4.15e-60 |
|
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: 216.92 E-value: 4.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1024 PQLSGEVKLNKVFFRYPERpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH 1103
Cdd:COG4618 325 PRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 LRKHIALVSQEPILFDTSIRENIVyglQPGEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIAR 1183
Cdd:COG4618 404 LGRHIGYLPQDVELFDGTIAENIA---RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALdAAAKDR--TCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1000-1269 |
1.29e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 212.76 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1000 AAGLIFNMLEEEPRIDGMTSSGTYPQlSGEVKLNKVFFRYPERPAvPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLE 1079
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD-QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1080 RLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVygLQPGEYTHEQIETACSKANIHKFIDElPDG 1159
Cdd:PRK11160 388 RAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLL--LAAPNASDEALIEVLQQVGLEKLLED-DKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1160 YETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIM 1239
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
250 260 270
....*....|....*....|....*....|
gi 17558664 1240 VVKNGQVVEQGTHNELIAKRGAYFALTQKQ 1269
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1046-1271 |
1.43e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 213.17 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLerL-YDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRE 1124
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL--LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGlQPgEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTE 1204
Cdd:PRK11174 442 NVLLG-NP-DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1205 SEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGaYFA--LTQKQSS 1271
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG-LFAtlLAHRQEE 587
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
380-604 |
3.75e-58 |
|
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: 211.15 E-value: 3.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 380 SGRISVNKVEFTYPtRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQ 459
Cdd:COG4618 328 KGRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEPNLFNTSIEQNI-RYGrsDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVR 538
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 539 NPKILLLDEATSALDAESESIVQSALENA-SRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHE 604
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1000-1241 |
3.93e-58 |
|
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: 210.22 E-value: 3.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1000 AAGLIFNMLEEEPRID-GMTSSGTYPqlSGEVKLNKVFFRYPERPavPILQGLNVHVKPGQTLALVGPSGCGKSTVISLL 1078
Cdd:TIGR02857 293 AAEALFAVLDAAPRPLaGKAPVTAAP--ASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1079 ERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIvyGLQPGEYTHEQIETACSKANIHKFIDELPD 1158
Cdd:TIGR02857 369 LGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENI--RLARPDASDAEIREALERAGLDEFVAALPQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1159 GYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCI 1238
Cdd:TIGR02857 447 GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
...
gi 17558664 1239 MVV 1241
Cdd:TIGR02857 527 VVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
46-334 |
4.17e-56 |
|
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: 195.94 E-value: 4.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 46 LAVGIIVSCATGVGLPLMSIIMGNVSQNFVTLGtiflDPNStasekaaaraefsHEVIQNCLKYVYLGCGIFAAGFLQAS 125
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDG----DPET-------------QALNVYSLALLLLGLAQFILSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 126 CFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLL 205
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 206 TLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFL 285
Cdd:pfam00664 144 TLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 286 IGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGT--VLTVFFSVMMGSM 334
Cdd:pfam00664 224 NGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
706-977 |
6.02e-56 |
|
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: 195.55 E-value: 6.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIINVFsNPDRDQMKKDGHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSK 785
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-LPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 786 VYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVG 865
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 866 QALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGLTYGFANSIQFF 945
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|..
gi 17558664 946 TYAAAFRFGLFLIFDKNVLMEPENVLRVLFAI 977
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVAFLSLFAQ 269
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
708-1001 |
7.68e-55 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 194.03 E-value: 7.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 708 FAIIAALIQGAVMPAFSLFFSQIINVFSNPDR-----------------DQMKKDGHFWALMFLVLAAVQGTSMLFQCSL 770
Cdd:cd18558 3 VGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMtnitgnssglnssagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQGSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 771 FGVAAERLTMRIRSKVYRNVLRQDATYFdmPKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQ 850
Cdd:cd18558 83 WGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 851 MAFLVMAIFPFMAVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAI 930
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 931 IRGLTYGFANSIQFFTYAAAFRFGLFLIFDKnvLMEPENVLRVLFAISFSFGTIGFAASYFPEYIKATFAA 1001
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQ--EYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAA 309
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
247-619 |
3.41e-53 |
|
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: 199.58 E-value: 3.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 247 EVLTSIRTVIAFNGQEYECKRYEDALEhgkkTGIKKSF----------LIGAGLA-SFFVIIyasyclaFWVGTNFVYSG 315
Cdd:TIGR01193 339 EDLNGIETIKSLTSEAERYSKIDSEFG----DYLNKSFkyqkadqgqqAIKAVTKlILNVVI-------LWTGAYLVMRG 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 316 RLESGTVLTvfFSVMMGSMAlgQAGQQFATIGTALGAAASLYEVIDRIPEIDAYSTEGQTPSKIS---GRISVNKVEFTY 392
Cdd:TIGR01193 408 KLTLGQLIT--FNALLSYFL--TPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNnlnGDIVINDVSYSY 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 393 PTRAdvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFN 472
Cdd:TIGR01193 484 GYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFS 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 473 TSIEQNIRYG-RSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:TIGR01193 562 GSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSN 641
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 552 LDAESESIVQSALENASRgRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHA 619
Cdd:TIGR01193 642 LDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
706-1265 |
1.00e-51 |
|
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: 195.34 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIINVFSnPDRdqMKKDGHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSK 785
Cdd:TIGR01193 158 IVNIVIAAIIVTLISIAGSYYLQKIIDTYI-PHK--MMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 786 VYRNVLRQDATYFDMPKhsPGRITTRLaTDAPNIKSAIDYRLGSIF---NAIASVGGGLGiafYYGWQMAFLVMAIFPFM 862
Cdd:TIGR01193 235 YIKHLFELPMSFFSTRR--TGEIVSRF-TDASSIIDALASTILSLFldmWILVIVGLFLV---RQNMLLFLLSLLSIPVY 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 863 AVGQALMMKYHGGSATsdaKEMENAGKTAMEAIEN---IRTVQALTLQTKLYNifcsHLDAPHGGNISKAiirgLTYGFA 939
Cdd:TIGR01193 309 AVIIILFKRTFNKLNH---DAMQANAVLNSSIIEDlngIETIKSLTSEAERYS----KIDSEFGDYLNKS----FKYQKA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 940 NSIQfftyaAAFRFGLFLIFDKNVLMepenvLRVLFAIS--FSFGT-IGFAA--SYFPEYIKATF-------AAGLIFNM 1007
Cdd:TIGR01193 378 DQGQ-----QAIKAVTKLILNVVILW-----TGAYLVMRgkLTLGQlITFNAllSYFLTPLENIInlqpklqAARVANNR 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1008 LEEEPRIDGMTSSGTYP----QLSGEVKLNKVFFRYPErpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYD 1083
Cdd:TIGR01193 448 LNEVYLVDSEFINKKKRtelnNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1084 PLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLQPGeYTHEQIETACSKANIHKFIDELPDGYETR 1163
Cdd:TIGR01193 526 ARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKEN-VSQDEIWAACEIAEIKDDIENMPLGYQTE 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1164 VGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALdAAAKDRTCIVVAHRLSTIVNAGCIMVVKN 1243
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDH 683
|
570 580
....*....|....*....|..
gi 17558664 1244 GQVVEQGTHNELIAKRGAYFAL 1265
Cdd:TIGR01193 684 GKIIEQGSHDELLDRNGFYASL 705
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
383-615 |
6.81e-51 |
|
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: 179.45 E-value: 6.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPN--LFNTSIEQNIRYG--RSDVSDEDIAR----ALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIAR 534
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRErveeALELVGLEHLADRPPHEL-----------SGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 535 ALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIA-HRLSTV-RNADKIIVMKAGQVMEVGTHETLIEQKGL 612
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
...
gi 17558664 613 YHE 615
Cdd:COG1122 228 LEE 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
344-609 |
1.35e-50 |
|
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: 187.80 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 344 ATIGTALGAAASLYEVIDRIPEIDAYSTEGQTPSKIsgrISVNKVEFTYPTRA--DVKILKGVSLDAQPGQTVALVGSSG 421
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPL---LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESG 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 422 CGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN---IKYLRQLVGVVSQEPNL-FNT--SIEQNIRYG---RSDVSDEDIA 492
Cdd:COG1123 302 SGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYSsLNPrmTVGDIIAEPlrlHGLLSRAERR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 493 RALKEAnaadfIKTFpeGLNTLVGDR-GVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAesesIVQSALEN----- 566
Cdd:COG1123 382 ERVAEL-----LERV--GLPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNllrdl 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17558664 567 -ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:COG1123 451 qRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
382-629 |
6.81e-50 |
|
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: 177.54 E-value: 6.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 382 RISVNKVEFTYPTRAdvkILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLV 461
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEPNL-FNTSIEQNIRYGR-------SDVSDED---IARALKEANAADFIktfpeglntlvgDRGV-QMSGGQKQR 529
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRyphlglfGRPSAEDreaVEEALERTGLEHLA------------DRPVdELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 530 IAIARALVRNPKILLLDEATSALDaesesiVQSALE--------NASRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEV 600
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLD------LAHQLEvlellrrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQ 219
|
250 260 270
....*....|....*....|....*....|....*
gi 17558664 601 GT-----HETLIEQkgLYHelVHAQVFAD-VDDKP 629
Cdd:COG1120 220 GPpeevlTPELLEE--VYG--VEARVIEDpVTGRP 250
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
981-1229 |
1.64e-49 |
|
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: 184.87 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 981 FGTIGFAASYFPEYIKAtfaAGLIFNMLEEEPRIDGMTSSGTYPQLSGEV--KLNKVFFRYPERPAVpiLQGLNVHVKPG 1058
Cdd:TIGR02868 287 FAALPAAAQQLTRVRAA---AERIVEVLDAAGPVAEGSAPAAGAVGLGKPtlELRDLSAGYPGAPPV--LDGVSLDLPPG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1059 QTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGlqPGEYTHE 1138
Cdd:TIGR02868 362 ERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA--RPDATDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1139 QIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAK 1218
Cdd:TIGR02868 440 ELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS 519
|
250
....*....|.
gi 17558664 1219 DRTCIVVAHRL 1229
Cdd:TIGR02868 520 GRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
383-601 |
1.92e-49 |
|
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: 173.27 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRaDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNiKYLRQLVG 462
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIrygrsdvsdediaralkeanaadfiktfpeglntlvgdrGVQMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 543 LLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVG 601
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
994-1258 |
2.52e-49 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 184.86 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 994 YIKATFAAGLIFNMLEEEP-RIDGMTssgtYPQLSGEVKLNKVFFRYPErPAVPILQGLNVHVKPGQTLALVGPSGCGKS 1072
Cdd:TIGR01842 284 FSGARQAYKRLNELLANYPsRDPAMP----LPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1073 TVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVyglQPGEY-THEQIETACSKANIHK 1151
Cdd:TIGR01842 359 TLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIA---RFGENaDPEKIIEAAKLAGVHE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1152 FIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVAL-DAAAKDRTCIVVAHRLS 1230
Cdd:TIGR01842 436 LILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPS 515
|
250 260
....*....|....*....|....*...
gi 17558664 1231 TIVNAGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:TIGR01842 516 LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1035-1246 |
4.26e-49 |
|
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: 172.02 E-value: 4.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1035 VFFRYPERPAvPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQE 1114
Cdd:cd03246 6 VSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1115 PILFDTSIRENIvyglqpgeytheqietacskanihkfidelpdgyetrvgekgtqLSGGQKQRIAIARALIRNPKILLL 1194
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1195 DEATSALDTESEKQVQVALDAA-AKDRTCIVVAHRLSTIVNAGCIMVVKNGQV 1246
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
397-606 |
4.79e-49 |
|
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: 173.91 E-value: 4.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYN-----PDAGQILID--DIPIEDFNIKYLRQLVGVVSQEPN 469
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDgkDIYDLDVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 470 LFNTSIEQNIRYG-------RSDVSDEDIARALKEAnaadfiktfpeGLNTLVGDR--GVQMSGGQKQRIAIARALVRNP 540
Cdd:cd03260 92 PFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKA-----------ALWDEVKDRlhALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 541 KILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETL 606
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
383-597 |
7.62e-49 |
|
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: 171.25 E-value: 7.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADVkILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIrygrsdvsdediaralkeanaadfiktfpeglntlvgdrgvqMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 543 LLLDEATSALDAESESIVQSALENAS-RGRTTIVIAHRLSTVRNADKIIVMKAGQV 597
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
384-596 |
2.70e-48 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 171.11 E-value: 2.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPTRAdVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGV 463
Cdd:cd03225 1 ELKNLSFSYPDGA-RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQEPN--LFNTSIEQNIRYG-------RSDVsDEDIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIAR 534
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGlenlglpEEEI-EERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 535 ALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQ 596
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
383-599 |
6.32e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 170.61 E-value: 6.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPT-RADVKILKGVSLDAQPGQTVALVGSSGCGKST---IIQLLQRfynPDAGQILIDDIPIEDFNIKYLR 458
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 459 QL----VGVVSQEPNLFNT-SIEQNI----RYGRSDVSD--EDIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQK 527
Cdd:COG1136 82 RLrrrhIGFVFQFFNLLPElTALENValplLLAGVSRKErrERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 528 QRIAIARALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTVRNADKIIVMKAGQVME 599
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1031-1227 |
1.12e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.23 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIAL 1110
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQEPILFDTSIRENI--VYGLQPGEYTHEQIETACSKANihkfideLPDGY-ETRVGEkgtqLSGGQKQRIAIARALIR 1187
Cdd:COG4619 79 VPQEPALWGGTVRDNLpfPFQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17558664 1188 NPKILLLDEATSALDTESEKQVQVALD--AAAKDRTCIVVAH 1227
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLReyLAEEGRAVLWVSH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
401-550 |
1.56e-47 |
|
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: 166.67 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFN-TSIEQNI 479
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 480 RYGR------SDVSDEDIARALKEANAADFiktfpegLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATS 550
Cdd:pfam00005 81 RLGLllkglsKREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
289-609 |
1.57e-47 |
|
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: 179.47 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 289 GLASFFVIIYASYCLAfwVGTNFVYSGRLESGTVLTVffSVMMGSmALG---QAGQQFATIGTALGAAASLYEVIDRIPE 365
Cdd:TIGR01842 229 NLSKYFRIVLQSLVLG--LGAYLAIDGEITPGMMIAG--SILVGR-ALApidGAIGGWKQFSGARQAYKRLNELLANYPS 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 366 IDAYStegQTPsKISGRISVNKVEFTYPTRADVkILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID 445
Cdd:TIGR01842 304 RDPAM---PLP-EPEGHLSVENVTIVPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 446 DIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNI-RYGRsDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSG 524
Cdd:TIGR01842 379 GADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSG 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 525 GQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENA-SRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTH 603
Cdd:TIGR01842 458 GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGER 537
|
....*.
gi 17558664 604 ETLIEQ 609
Cdd:TIGR01842 538 DEVLAK 543
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
383-601 |
2.51e-47 |
|
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: 169.22 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRAD-VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN---IKYLR 458
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 459 QLVGVVSQEPNL-FN------TSIEQNIRYGRSDVSDEDIARALKEA-----NAADFIKTFPEglntlvgdrgvQMSGGQ 526
Cdd:cd03257 82 KEIQMVFQDPMSsLNprmtigEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 527 KQRIAIARALVRNPKILLLDEATSALDAesesIVQSALEN------ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVME 599
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDV----SVQAQILDllkklqEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
..
gi 17558664 600 VG 601
Cdd:cd03257 227 EG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1048-1199 |
6.47e-47 |
|
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: 164.74 E-value: 6.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILF-DTSIRENI 1126
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1127 VYGLQPGEYTHEQietacSKANIHKFIDEL--PDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATS 1199
Cdd:pfam00005 81 RLGLLLKGLSKRE-----KDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1030-1245 |
8.96e-47 |
|
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: 166.49 E-value: 8.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERP--AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLL--ErlYDPLEGAVTVdnndlrqmnpkhlR 1105
Cdd:cd03250 1 ISVEDASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSV-------------P 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1106 KHIALVSQEPILFDTSIRENIVYGLQPGEYTHEQIETACSkanIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARAL 1185
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1186 IRNPKILLLDEATSALDTESEKQV--QVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQ 1245
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
397-609 |
1.52e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 167.09 E-value: 1.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIED--FNIKYLRQLVGVVSQEPNLF-NT 473
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRKVGMVFQQFNLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 SIEQNIRYG--------RSDVsdEDIARA-LKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARALVRNPKILL 544
Cdd:COG1126 93 TVLENVTLApikvkkmsKAEA--EERAMElLERVGLADKADAYPA-----------QLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 545 LDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
383-597 |
2.72e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIRYG---RSDVSDEDIARALKEAnaadfiktFpeGLNTLVGDRGV-QMSGGQKQRIAIARALVR 538
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPfqlRERKFDRERALELLER--------L--GLPPDILDKPVeRLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 539 NPKILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAH--RLSTvRNADKIIVMKAGQV 597
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdpEQIE-RVADRVLTLEAGRL 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
383-597 |
3.70e-46 |
|
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: 165.36 E-value: 3.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPT-RADVKILKGVSLDAQPGQTVALVGSSGCGKST---IIQLLQRfynPDAGQILIDDIPIEDFN----I 454
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSekelA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 KYLRQLVGVVSQEPNLFNT-SIEQNIRY-----GRSDVSDEDIAR-ALKEANAADFIKTFPEglntlvgdrgvQMSGGQK 527
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEeLLERVGLGDRLNHYPS-----------ELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 528 QRIAIARALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTVRNADKIIVMKAGQV 597
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1047-1255 |
3.72e-46 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 165.82 E-value: 3.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYD-----PLEGAVTVDNNDLR--QMNPKHLRKHIALVSQEPILFD 1119
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIRENIVYGLQ-----PGEYTHEQIETACSKAnihkfidELPDgyetRVGEK--GTQLSGGQKQRIAIARALIRNPKIL 1192
Cdd:cd03260 95 GSIYDNVAYGLRlhgikLKEELDERVEEALRKA-------ALWD----EVKDRlhALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1193 LLDEATSALDTESEKQVQVALDAAAKDRTCIVVAH------RLSTIVnagCIMVvkNGQVVEQGTHNEL 1255
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRVADRT---AFLL--NGRLVEFGPTEQI 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
383-609 |
7.97e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 165.24 E-value: 7.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYlRQLVG 462
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNT-SIEQNIR-----YGRS-DVSDEDIARALKEANAADFiktfpegLNTLVGdrgvQMSGGQKQRIAIARA 535
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPrKEARERIDELLELFGLTDA-------ADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 536 LVRNPKILLLDEATSALDAESESIVQSAL-ENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLrELAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1030-1259 |
1.60e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 164.04 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPErpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPI--LFDTSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIAR 1183
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEnlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVA-HRLSTIV-NAGCIMVVKNGQVVEQGTHNELIAKR 1259
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
383-606 |
2.48e-45 |
|
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: 164.21 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRA-DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLV 461
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEPNL-FN------TSIEQNIRYGRSDVSDEDIARALKEAN-AADFIKTFPEglntlvgdrgvQMSGGQKQRIAIA 533
Cdd:COG1124 82 QMVFQDPYAsLHprhtvdRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 534 RALVRNPKILLLDEATSALDAesesIVQSALEN------ASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETL 606
Cdd:COG1124 151 RALILEPELLLLDEPTSALDV----SVQAEILNllkdlrEERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
381-602 |
4.14e-45 |
|
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: 161.81 E-value: 4.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 381 GRISVNKVEFTYptRADV-KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQ 459
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEPNLFNTSIEQNI-RYGRsdVSDEDIARALKeanaadfiktfpeglntlVGDRGVQMSGGQKQRIAIARALVR 538
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 539 NPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGT 602
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1030-1256 |
4.23e-45 |
|
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: 163.68 E-value: 4.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPIL-FDTSIRENIVYGLQP-----GEYT---HEQIETACSKANIHKFIDelpdgyeTRVgekgTQLSGGQKQRIA 1180
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRYPhlglfGRPSaedREAVEEALERTGLEHLAD-------RPV----DELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESekQVQVaLD-----AAAKDRTCIVVAH------RLSTIvnagcIMVVKNGQVVEQ 1249
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAH--QLEV-LEllrrlARERGRTVVMVLHdlnlaaRYADR-----LVLLKDGRIVAQ 219
|
....*..
gi 17558664 1250 GTHNELI 1256
Cdd:COG1120 220 GPPEEVL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
383-594 |
4.44e-45 |
|
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: 162.26 E-value: 4.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPT-RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKylrqlV 461
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEPNLFN-TSIEQNIRYGrsdVSDEDIARALKEANAADFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNP 540
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELLELV--GLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 541 KILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLS-TVRNADKIIVMKA 594
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
382-595 |
4.82e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 163.72 E-value: 4.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 382 RISVNKVEFTYPTR-ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfnikyLRQL 460
Cdd:COG1116 7 ALELRGVSKRFPTGgGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLFN-TSIEQNIRYG------RSDVSDEDIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIA 533
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 534 RALVRNPKILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAH------RLstvrnADKIIVMKAG 595
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1032-1250 |
4.85e-45 |
|
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: 160.56 E-value: 4.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERPAvPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNpKHLRKHIALV 1111
Cdd:cd03247 3 INNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQEPILFDTSIRENIvyglqpgeytheqietacskanihkfidelpdgyetrvgekGTQLSGGQKQRIAIARALIRNPKI 1191
Cdd:cd03247 81 NQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1192 LLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQG 1250
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
399-1263 |
9.12e-45 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 178.05 E-value: 9.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiedfNIKYlrqlvgvVSQEPNLFNTSIEQN 478
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER------SIAY-------VPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 479 IRYgrsdVSDEDIARALK-------EANAAdfikTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:PTZ00243 741 ILF----FDEEDAARLADavrvsqlEADLA----QLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 552 LDAE-SESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVmevgthetliEQKGLYHELVHAQVFADV----- 625
Cdd:PTZ00243 813 LDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV----------EFSGSSADFMRTSLYATLaaelk 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 626 DDKPKKK-EAERRMSRQTSQRKGSVNFKTQESQVDEKPGAPPAPEAAEKEIKRLKKELEEEGAVKANLFKilRYARpewi 704
Cdd:PTZ00243 883 ENKDSKEgDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYV--AYLR---- 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 705 yiffAIIAALIQGAVMPAFslFFSQIINVFSNP-----DRDQMKKDGHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLT 779
Cdd:PTZ00243 957 ----FCGGLHAAGFVLATF--AVTELVTVSSGVwlsmwSTRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGS 1030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 780 MRIRSKVYRNVLRQDATYFDMpkhSP-GRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYygwQMAFLVMAI 858
Cdd:PTZ00243 1031 RNMHRDLLRSVSRGTMSFFDT---TPlGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSA---SQPFVLVAL 1104
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 859 FPFMAVGQALMMKYHggSATSDAKEMENAGKTAM-----EAIENIRTVQALTLQTKLYNIFCSHLDAPHG-GNISKAIIR 932
Cdd:PTZ00243 1105 VPCGYLYYRLMQFYN--SANREIRRIKSVAKSPVftlleEALQGSATITAYGKAHLVMQEALRRLDVVYScSYLENVANR 1182
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 933 --GLTYGFANSIQFFTYAaafrfglFLIFDKNVLMEPENVLrVLFAISFSFGTIGFAASYFPEYIKATFAAGL--IFNML 1008
Cdd:PTZ00243 1183 wlGVRVEFLSNIVVTVIA-------LIGVIGTMLRATSQEI-GLVSLSLTMAMQTTATLNWLVRQVATVEADMnsVERLL 1254
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1009 --------EEEPRID----------GM---------------TSSGTYPQLSGEVKLNKVFFRYpeRPAVP-ILQGLNVH 1054
Cdd:PTZ00243 1255 yytdevphEDMPELDeevdalerrtGMaadvtgtvviepaspTSAAPHPVQAGSLVFEGVQMRY--REGLPlVLRGVSFR 1332
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1055 VKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLqpgE 1134
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFL---E 1409
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1135 YTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALI-RNPKILLLDEATSALDTESEKQVQVAL 1213
Cdd:PTZ00243 1410 ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATV 1489
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 17558664 1214 DAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYF 1263
Cdd:PTZ00243 1490 MSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
383-596 |
1.61e-44 |
|
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: 159.27 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPI--EDFNIKYLRQL 460
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLFNT-SIEQNIRYGrsdvsdediaralkeanaadfiktfpeglntlvgdrgvqMSGGQKQRIAIARALVRN 539
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 540 PKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQ 596
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1023-1251 |
6.07e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 158.73 E-value: 6.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1023 YPQlSGEVKLNKVFFRY-PERPavPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNP 1101
Cdd:cd03369 1 WPE-HGEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1102 KHLRKHIALVSQEPILFDTSIRENivygLQP-GEYTHEQIETAcskanihkfidelpdgyeTRVGEKGTQLSGGQKQRIA 1180
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSN----LDPfDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGT 1251
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
383-602 |
9.20e-44 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 158.90 E-value: 9.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYP-TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL- 460
Cdd:cd03258 2 IELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 --VGVVSQEPNLFNT-SIEQNIRY-------GRSDVsDEDIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRI 530
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALpleiagvPKAEI-EERVLELLELVGLEDKADAYPA-----------QLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 531 AIARALVRNPKILLLDEATSALDAES-ESIVQSALE-NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGT 602
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETtQSILALLRDiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
383-612 |
1.14e-43 |
|
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: 159.90 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPtRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDI-PIEDFNIKYLRQLV 461
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEP-NLF-NTSIEQNIRYG-------RSDVsDEDIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAI 532
Cdd:TIGR04520 80 GMVFQNPdNQFvGATVEDDVAFGlenlgvpREEM-RKRVDEALKLVGMEDFRDREPHLL-----------SGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 533 ARALVRNPKILLLDEATSALDAES-ESIVQSALE-NASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGT------HE 604
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTpreifsQV 227
|
....*...
gi 17558664 605 TLIEQKGL 612
Cdd:TIGR04520 228 ELLKEIGL 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
383-596 |
1.57e-43 |
|
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: 157.25 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADV--KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLqrfynpdagqilIDDIPIEDFNIKYLRQl 460
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL------------LGELEKLSGSVSVPGS- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLFNTSIEQNIRYGrsdvSDEDIAR--------ALKEanaaDfIKTFPEGLNTLVGDRGVQMSGGQKQRIAI 532
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG----KPFDEERyekvikacALEP----D-LEILPDGDLTEIGEKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 533 ARALVRNPKILLLDEATSALDAE-SESIVQSAL-ENASRGRTTIVIAHRLSTVRNADKIIVMKAGQ 596
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
383-606 |
1.58e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.57 E-value: 1.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID-----DIPIEDfnikyl 457
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtGLPPEK------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 458 RQlVGVVSQEPNLF-NTSIEQNIRYG--RSDVSDEDIARALKEA----NAADFIKTFPEglntlvgdrgvQMSGGQKQRI 530
Cdd:COG3842 77 RN-VGMVFQDYALFpHLTVAENVAFGlrMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 531 AIARALVRNPKILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAHRLS---TVrnADKIIVMKAGQVMEVGTHET 605
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
.
gi 17558664 606 L 606
Cdd:COG3842 223 I 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
383-598 |
1.77e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 158.68 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPtrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-- 460
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 -VGVVSQEPNLF-NTSIEQNI-----------RYGRSDVSDEDIARALkeanaaDFIKTFpeGLNTLVGDRGVQMSGGQK 527
Cdd:COG3638 81 rIGMIFQQFNLVpRLSVLTNVlagrlgrtstwRSLLGLFPPEDRERAL------EALERV--GLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 528 QRIAIARALVRNPKILLLDEATSALDAESESIVQSAL--ENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVM 598
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrrIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1007-1257 |
2.65e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 166.23 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1007 MLEEEPRIDGMTSSGTYPQLSGE--VKLNKVFFRYPERP--AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLY 1082
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1083 DPLEGAVTVDNNDLRQMNP---KHLRKHIALVSQEPilfDTS------IRENIVYGLQpgeytheqIETACSKANIHKFI 1153
Cdd:COG1123 316 RPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDP---YSSlnprmtVGDIIAEPLR--------LHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1154 DE------LPDGYETRvgeKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESekQVQVA--LDAAAKDR--TCI 1223
Cdd:COG1123 385 AEllervgLPPDLADR---YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV--QAQILnlLRDLQRELglTYL 459
|
250 260 270
....*....|....*....|....*....|....*.
gi 17558664 1224 VVAHRLSTiVNAGC--IMVVKNGQVVEQGTHNELIA 1257
Cdd:COG1123 460 FISHDLAV-VRYIAdrVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
394-601 |
4.30e-43 |
|
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: 156.53 E-value: 4.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDD-----IPIEDFNIkylrqlvGVVSQEP 468
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgVPPERRNI-------GMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 469 NLF-NTSIEQNIRYG--RSDVSDEDIAR----ALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIARALVRNPK 541
Cdd:cd03259 82 ALFpHLTVAENIAFGlkLRGVPKAEIRArvreLLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 542 ILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVG 601
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1031-1245 |
4.85e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 156.09 E-value: 4.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPERpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIAL 1110
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQEP--ILFDTSIRENIVYGL----QPGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIARA 1184
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLenlgLPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1185 LIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVA-HRLStIVNAGC--IMVVKNGQ 1245
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLD-LLLELAdrVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1031-1258 |
5.42e-43 |
|
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: 156.97 E-value: 5.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFfrYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL---RKH 1107
Cdd:cd03258 6 NVSKVF--GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILFDT-SIRENIVYglqPGEYTHEqietacSKANIHKFIDELPD--GYETRVGEKGTQLSGGQKQRIAIARA 1184
Cdd:cd03258 84 IGMIFQHFNLLSSrTVFENVAL---PLEIAGV------PKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1185 LIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1030-1249 |
7.69e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 156.36 E-value: 7.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPE-RPAVPILQGLNVHVKPGQTLALVGPSGCGKST---VISLLERlydPLEGAVTVDNNDLRQMNPKHL- 1104
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1105 ---RKHIALVSQEPILFDT-SIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQK 1176
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALPLLlagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1177 QRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKD--RTCIVVAHRLSTIVNAGCIMVVKNGQVVEQ 1249
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
383-611 |
8.55e-43 |
|
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: 156.56 E-value: 8.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPtraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLvG 462
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLF-NTSIEQNIRY-GR-SDVSDEDIaralkEANAADFIKTF--PEGLNTLVGDrgvqMSGGQKQRIAIARALV 537
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRYfAElYGLFDEEL-----KKRIEELIELLglEEFLDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 538 RNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQKG 611
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
383-602 |
1.81e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 159.09 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTR-ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQ---LLQRfynPDAGQILIDDIPIEDFNIKYLR 458
Cdd:COG1135 2 IELENLSKTFPTKgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 459 QL---VGVVSQEPNLFNT-SIEQNIRY-----GrsdVSDEDIARALKEanaadfiktfpegLNTLVG--DRG----VQMS 523
Cdd:COG1135 79 AArrkIGMIFQHFNLLSSrTVAENVALpleiaG---VPKAEIRKRVAE-------------LLELVGlsDKAdaypSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 524 GGQKQRIAIARALVRNPKILLLDEATSALDAES-ESIvqsaLE-----NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQ 596
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETtRSI----LDllkdiNRELGLTIVLITHEMDVVRRiCDRVAVLENGR 218
|
....*.
gi 17558664 597 VMEVGT 602
Cdd:COG1135 219 IVEQGP 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
383-598 |
2.26e-42 |
|
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: 155.42 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-- 460
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 -VGVVSQEPNLFN-TSIEQNIRYGR-----------SDVSDEDIARALKEANAAdfiktfpeGLNTLVGDRGVQMSGGQK 527
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERV--------GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 528 QRIAIARALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTVR-NADKIIVMKAGQVM 598
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
384-596 |
3.30e-42 |
|
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: 151.63 E-value: 3.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGV 463
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQepnlfntsieqnirygrsdvsdediaralkeanaadfiktfpeglntlvgdrgvqMSGGQKQRIAIARALVRNPKIL 543
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 544 LLDEATSALDAESESIVQSAL-ENASRGRTTIVIAHRLSTVRNA-DKIIVMKAGQ 596
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1030-1270 |
3.73e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.45 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAVpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmNPKHLRKHIA 1109
Cdd:COG1131 1 IEVRGLTKRYGDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDT-SIRENI-----VYGLqPGEYTHEQIETACSKANIHKFIDelpdgyeTRVGekgtQLSGGQKQRIAIAR 1183
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGL-PRKEARERIDELLELFGLTDAAD-------RKVG----TLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLStIVNAGC--IMVVKNGQVVEQGTHNELIAKR- 1259
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELwELLRELAAEGKTVLLSTHYLE-EAERLCdrVAIIDKGRIVADGTPDELKARLl 223
|
250
....*....|..
gi 17558664 1260 -GAYFALTQKQS 1270
Cdd:COG1131 224 eDVFLELTGEEA 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1029-1250 |
5.76e-42 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 153.82 E-value: 5.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1029 EVK-LNKvffRYPERP-AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNP---KH 1103
Cdd:cd03257 3 EVKnLSV---SFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 LRKHIALVSQEPIL-FDT--SIRENIVYGLQP--GEYTHEQIETACSKANIH-----KFIDELPDgyetrvgekgtQLSG 1173
Cdd:cd03257 80 RRKEIQMVFQDPMSsLNPrmTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGvglpeEVLNRYPH-----------ELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1174 GQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLStIVNAGC--IMVVKNGQVVEQ 1249
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLG-VVAKIAdrVAVMYAGKIVEE 227
|
.
gi 17558664 1250 G 1250
Cdd:cd03257 228 G 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1032-1257 |
9.84e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 153.81 E-value: 9.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERpaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALV 1111
Cdd:COG1124 7 LSVSYGQGGRR--VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQEPIL-------FDTSIRENI-VYGLQPGEythEQIETACSKAnihkfidELPDGYETRVGEkgtQLSGGQKQRIAIAR 1183
Cdd:COG1124 85 FQDPYAslhprhtVDRILAEPLrIHGLPDRE---ERIAELLEQV-------GLPPSFLDRYPH---QLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLStIVNAGC--IMVVKNGQVVEQGTHNELIA 1257
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAHLCdrVAVMQNGRIVEELTVADLLA 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
383-609 |
4.78e-41 |
|
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: 154.06 E-value: 4.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRA-DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNP---DAGQILIDDIPIEDFNIKYLR 458
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 459 QL----VGVVSQEP-NLFN------TSIEQNIRYGRsDVSDED----IARALKE---ANAADFIKTFPeglntlvgdrgV 520
Cdd:COG0444 82 KIrgreIQMIFQDPmTSLNpvmtvgDQIAEPLRIHG-GLSKAEarerAIELLERvglPDPERRLDRYP-----------H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 521 QMSGGQKQRIAIARALVRNPKILLLDEATSALDAeseSIVQSALE-----NASRGRTTIVIAHRLSTVRN-ADKIIVMKA 594
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDV---TIQAQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMYA 226
|
250
....*....|....*
gi 17558664 595 GQVMEVGTHETLIEQ 609
Cdd:COG0444 227 GRIVEEGPVEELFEN 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1045-1250 |
5.40e-41 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 150.36 E-value: 5.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlRKHIALVSQEPILFDT-SIR 1123
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1124 ENIVYGLQPGEYTHEQIEtacskANIHKFIDELP-DGYETRvgeKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:cd03259 91 ENIAFGLKLRGVPKAEIR-----ARVRELLELVGlEGLLNR---YPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1203 TESEKQVQVALDA--AAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG 1250
Cdd:cd03259 163 AKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
376-611 |
6.08e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 165.68 E-value: 6.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 376 PSkiSGRISVNKVEFTYptRADVK-ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNI 454
Cdd:PLN03130 1233 PS--SGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 KYLRQLVGVVSQEPNLFNTSIEQNIRyGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIAR 534
Cdd:PLN03130 1309 MDLRKVLGIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 535 ALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKG 611
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
383-619 |
7.52e-41 |
|
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: 150.90 E-value: 7.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-- 460
Cdd:COG1127 6 IEVRNLTKSF---GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 -VGVVSQEPNLFNT-SIEQNIRYG---RSDVSDEDIAR----ALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIA 531
Cdd:COG1127 83 rIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRElvleKLELVGLPGAADKMPSEL-----------SGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 532 IARALVRNPKILLLDEATSALDAE-SESIVQSALE-NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIE 608
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPItSAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
250
....*....|.
gi 17558664 609 QKglyHELVHA 619
Cdd:COG1127 232 SD---DPWVRQ 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
109-619 |
7.99e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 165.15 E-value: 7.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 109 YVYLGCGIFAAGFlqASCFMVICEKL--SNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQ 186
Cdd:PLN03232 956 YALLGFGQVAVTF--TNSFWLISSSLhaAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMN 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 187 MMAQFIGGFAVAFTYDwllTLIMMSLSPFMMIcgLFLAKLLATAATKEAKQ---------YAVAGGiAEEVLTSIRTVIA 257
Cdd:PLN03232 1034 QLWQLLSTFALIGTVS---TISLWAIMPLLIL--FYAAYLYYQSTSREVRRldsvtrspiYAQFGE-ALNGLSSIRAYKA 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 258 FNGQeyeckryedALEHGKKTGIKKSFLIGAGLASFFVIIyasyclafwvgtnfvysgRLES-GTV---LTVFFSVMMGS 333
Cdd:PLN03232 1108 YDRM---------AKINGKSMDNNIRFTLANTSSNRWLTI------------------RLETlGGVmiwLTATFAVLRNG 1160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 334 MALGQAGqqFA-TIGTALGAAASLYEVI-----------DRIPEIDAYSTEGQTPSKISGRISVNKVEFTYPTRADVK-- 399
Cdd:PLN03232 1161 NAENQAG--FAsTMGLLLSYTLNITTLLsgvlrqaskaeNSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKfe 1238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ------------ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQE 467
Cdd:PLN03232 1239 dvhlryrpglppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS 1318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 PNLFNTSIEQNIRyGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDE 547
Cdd:PLN03232 1319 PVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 548 ATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKG-LYHELVHA 619
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHS 1470
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1030-1226 |
9.05e-41 |
|
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: 149.95 E-value: 9.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPE-RPAVPILQGLNVHVKPGQTLALVGPSGCGKST---VISLLERlydPLEGAVTVDNNDLRQMNPKHL- 1104
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1105 ---RKHIALVSQEPILFDT-SIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQK 1176
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELPLLlagvPKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1177 QRIAIARALIRNPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVA 1226
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVmELLRELNKEAGTTIVVV 197
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1014-1264 |
1.60e-40 |
|
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: 150.83 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1014 IDGMTSSGTYpQLSGEVKLNKVFFRYpERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDN 1093
Cdd:cd03288 5 ISGSSNSGLV-GLGGEIKIHDLCVRY-ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1094 NDLRQMNPKHLRKHIALVSQEPILFDTSIRENivygLQPG-EYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLS 1172
Cdd:cd03288 83 IDISKLPLHTLRSRLSIILQDPILFSGSIRFN----LDPEcKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1173 GGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTH 1252
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTP 238
|
250
....*....|..
gi 17558664 1253 NELIAKRGAYFA 1264
Cdd:cd03288 239 ENLLAQEDGVFA 250
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
383-597 |
2.32e-40 |
|
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: 148.45 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIED--FNIKYLRQL 460
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLF-NTSIEQNI------RYGRSDVSDEDIAR-ALKEANAADFIKTFPeglntlvgdrgVQMSGGQKQRIAI 532
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENItlapikVKGMSKAEAEERALeLLEKVGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 533 ARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQV 597
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1037-1257 |
3.99e-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: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1037 FRYPERpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDP---LEGAVTVDNNDLRQMNPKHLRKHIALVSQ 1113
Cdd:COG1123 12 VRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRRIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1114 EPI--LFDTSIRENIVYGLQPGEYTHEQIetacsKANIHKFIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIRNPKI 1191
Cdd:COG1123 91 DPMtqLNPVTVGDQIAEALENLGLSRAEA-----RARVLELLEAV--GLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1192 LLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
384-601 |
5.94e-40 |
|
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: 146.04 E-value: 5.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGV 463
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQepnlfntsieqnirygrsdvsdediarALKEANAADFIktfpeglntlvgDRGV-QMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLA------------DRPFnELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 543 LLLDEATSALDAESESIVQSAL--ENASRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVG 601
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
383-609 |
7.79e-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: 155.83 E-value: 7.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPtRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDA---GQILIDDIPIEDFNIKYLRQ 459
Cdd:COG1123 5 LEVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEP--NLFNTSIEQNIRYG--RSDVSDEDIARALKEANAAdfiktfpEGLNTLVGDRGVQMSGGQKQRIAIARA 535
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEA-------VGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 536 LVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1017-1250 |
2.65e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.11 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1017 MTSSGTYPQLSGEVK-LNkvfFRYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYD--P---LEGAVT 1090
Cdd:COG1117 1 MTAPASTLEPKIEVRnLN---VYYGDKQA---LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1091 VDNNDL--RQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLQ-----PGEYTHEQIETACSKANIHkfiDELPDgyetR 1163
Cdd:COG1117 75 LDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRlhgikSKSELDEIVEESLRKAALW---DEVKD----R 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1164 VGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAH------RLSTIVnagc 1237
Cdd:COG1117 148 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVSDYT---- 223
|
250
....*....|...
gi 17558664 1238 iMVVKNGQVVEQG 1250
Cdd:COG1117 224 -AFFYLGELVEFG 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
135-616 |
2.88e-39 |
|
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: 160.11 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 135 SNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREgtgdkvgLAFQMMAQFIGGFavaFTYDWLLTLIMMSLSP 214
Cdd:TIGR00957 1037 SRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDS-------MIPPVIKMFMGSL---FNVIGALIVILLATPI 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 215 FMMIC---GL--FLAKLLATAATKEAKQYAVAGGIA-----EEVLTSIRTVIAFNGQEyeckRYEdalehgkktgIKKSF 284
Cdd:TIGR00957 1107 AAVIIpplGLlyFFVQRFYVASSRQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQE----RFI----------HQSDL 1172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 285 LIGAGLASFFVIIYASYCLAfwVGTNFVysgrlesGTVLTVF---FSVM-MGSMALGQAG-------QQFATIGTALGAA 353
Cdd:TIGR00957 1173 KVDENQKAYYPSIVANRWLA--VRLECV-------GNCIVLFaalFAVIsRHSLSAGLVGlsvsyslQVTFYLNWLVRMS 1243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 354 ASLYEVIDRIPEIDAYS-TEGQTPSKI------SGRISVNKVEF---TYPTRADVK-ILKGVSLDAQPGQTVALVGSSGC 422
Cdd:TIGR00957 1244 SEMETNIVAVERLKEYSeTEKEAPWQIqetappSGWPPRGRVEFrnyCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGA 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 423 GKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRyGRSDVSDEDIARALKEANAAD 502
Cdd:TIGR00957 1324 GKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKT 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 503 FIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLST 582
Cdd:TIGR00957 1403 FVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT 1482
|
490 500 510
....*....|....*....|....*....|....
gi 17558664 583 VRNADKIIVMKAGQVMEVGTHETLIEQKGLYHEL 616
Cdd:TIGR00957 1483 IMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
110-353 |
4.99e-39 |
|
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: 147.32 E-value: 4.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 110 VYLGCGIFAagFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMA 189
Cdd:cd18557 45 IYLLQSVFT--FVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 190 QFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYE 269
Cdd:cd18557 123 QVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 270 DALEHGKKTGIKKSFLIG--AGLASFFviIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIG 347
Cdd:cd18557 203 EALDRSYRLARKKALANAlfQGITSLL--IYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIM 280
|
....*.
gi 17558664 348 TALGAA 353
Cdd:cd18557 281 KALGAS 286
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1017-1202 |
1.20e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 145.23 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1017 MTSSGTYpqlsgeVKLNKVFFRYPERP-AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNND 1095
Cdd:COG1116 1 MSAAAPA------LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1096 LRQMNPKhlrkhIALVSQEPILFD-TSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQ 1170
Cdd:COG1116 75 VTGPGPD-----RGVVFQEPALLPwLTVLDNVALGLElrgvPKAERRERARELLELVGLAGFEDAYPH-----------Q 138
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 1171 LSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALD 170
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
383-609 |
1.28e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 147.99 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiEDFNIKyL----R 458
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---RDLFTN-LppreR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 459 QlVGVVSQEPNLF-NTSIEQNIRYG--RSDVSDEDI-ARA---LKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIA 531
Cdd:COG1118 76 R-VGFVFQHYALFpHMTVAENIAFGlrVRPPSKAEIrARVeelLELVQLEGLADRYPS-----------QLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 532 IARALVRNPKILLLDEATSALDAEsesiVQSALEN------ASRGRTTIVIAH-RLSTVRNADKIIVMKAGQVMEVGTHE 604
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAK----VRKELRRwlrrlhDELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPD 219
|
....*
gi 17558664 605 TLIEQ 609
Cdd:COG1118 220 EVYDR 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1045-1260 |
1.58e-38 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 144.23 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmNPKHLRKHIALVSQEPILFDT-SIR 1123
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1124 ENI-----VYGLqPGEYTHEQIETAcskanIHKFidELPDGYETRVGEkgtqLSGGQKQRIAIARALIRNPKILLLDEAT 1198
Cdd:COG4555 93 ENIryfaeLYGL-FDEELKKRIEEL-----IELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1199 SALDTESEKQVQVALDAAAKDRTCIVVA-HRLSTIVN-AGCIMVVKNGQVVEQGTHNELIAKRG 1260
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1030-1227 |
1.79e-38 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 143.38 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPE-RPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPkhlrkHI 1108
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1109 ALVSQEPILFD-TSIRENIVYGLQPGEYTHEQIetacsKANIHKFIDElpdgyetrVGEKGT------QLSGGQKQRIAI 1181
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEA-----RERAEELLEL--------VGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17558664 1182 ARALIRNPKILLLDEATSALDTESEKQVQVAL-DAAAKDR-TCIVVAH 1227
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELlDIWRETGkTVLLVTH 190
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1030-1255 |
1.79e-38 |
|
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: 144.88 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDnnDLRQMNPKHL---RK 1106
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD--GLDTLDEENLweiRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 HIALVSQEPilfD-----TSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQ 1177
Cdd:TIGR04520 78 KVGMVFQNP---DnqfvgATVEDDVAFGLEnlgvPREEMRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1178 RIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNEL 1255
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1037-1245 |
2.07e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 140.84 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1037 FRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQepi 1116
Cdd:cd00267 7 FRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 lfdtsirenivyglqpgeytheqietacskanihkfidelpdgyetrvgekgtqLSGGQKQRIAIARALIRNPKILLLDE 1196
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1197 ATSALDTESEKQVQVAL-DAAAKDRTCIVVAHRLSTIVNAG-CIMVVKNGQ 1245
Cdd:cd00267 107 PTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
383-660 |
2.47e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.16 E-value: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPtRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEP-NLF-NTSIEQNIRYGRSDVS---DEDIAR---ALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIAR 534
Cdd:PRK13635 85 MVFQNPdNQFvGATVQDDVAFGLENIGvprEEMVERvdqALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 535 ALVRNPKILLLDEATSALDAESEsivQSALE-----NASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 610 KglyHELVhaQVFADVDDKPKKKEAERRMSRQTsqrkgSVNFKTQESQVDE 660
Cdd:PRK13635 231 G---HMLQ--EIGLDVPFSVKLKELLKRNGILL-----PNTYLTMESLVDE 271
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1030-1257 |
3.08e-38 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 143.41 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPK---HLRK 1106
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 HIALVSQEPILFDT-SIRENIVYGLqpgeYTHeqieTACSKANIHKFIDE-LpdgyeTRVGEKGT------QLSGGQKQR 1178
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPL----REH----TRLSEEEIREIVLEkL-----EAVGLRGAedlypaELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1179 IAIARALIRNPKILLLDEATSALD-TESEKQVQVALD-AAAKDRTCIVVAHRLSTIVNAG-CIMVVKNGQVVEQGTHNEL 1255
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIAdRIAVLYDGKIVAEGTPEEL 224
|
..
gi 17558664 1256 IA 1257
Cdd:cd03261 225 RA 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
383-597 |
3.12e-38 |
|
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: 141.00 E-value: 3.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYlRQLVG 462
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV-KRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNT-SIEQNIRYgrsdvsdediaralkeanaadfiktfpeglntlvgdrgvqmSGGQKQRIAIARALVRNPK 541
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 542 ILLLDEATSALDAES-ESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQV 597
Cdd:cd03230 116 LLILDEPTSGLDPESrREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1031-1250 |
3.87e-38 |
|
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: 141.03 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIAL 1110
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQepilfdtsirenivyglqpgeytheqietACSKANIHKFIDElpdgyetRVgekgTQLSGGQKQRIAIARALIRNPK 1190
Cdd:cd03214 78 VPQ-----------------------------ALELLGLAHLADR-------PF----NELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1191 ILLLDEATSALDTESekQVQVaLD-----AAAKDRTCIVVAHRLStIVNAGC--IMVVKNGQVVEQG 1250
Cdd:cd03214 118 ILLLDEPTSHLDIAH--QIEL-LEllrrlARERGKTVVMVLHDLN-LAARYAdrVILLKDGRIVAQG 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
382-606 |
4.59e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 143.64 E-value: 4.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 382 RISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFY--NPDA---GQILIDDIPI--EDFNI 454
Cdd:COG1117 11 KIEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 KYLRQLVGVVSQEPNLFNTSIEQNIRYG--------RSDVsDEDIARALKEANAADfiktfpEglntlVGDR----GVQM 522
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSEL-DEIVEESLRKAALWD------E-----VKDRlkksALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 523 SGGQKQRIAIARALVRNPKILLLDEATSALDAES-----ESIVQsaLenasRGRTTIVI-------AHRLStvrnaDKII 590
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakieELILE--L----KKDYTIVIvthnmqqAARVS-----DYTA 224
|
250
....*....|....*.
gi 17558664 591 VMKAGQVMEVGTHETL 606
Cdd:COG1117 225 FFYLGELVEFGPTEQI 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
383-606 |
4.70e-38 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 142.64 E-value: 4.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-- 460
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 -VGVVSQEPNLFNT-SIEQNIRYG---RSDVSDEDIARALKEANAAdfiktfpeglntlVGDRGV------QMSGGQKQR 529
Cdd:cd03261 78 rMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEKLEA-------------VGLRGAedlypaELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 530 IAIARALVRNPKILLLDEATSALD-AESESIVQSALE-NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
95-353 |
1.04e-37 |
|
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: 143.45 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 95 RAEFSHEVIqnCLKYVYLGCGIFaaGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVR 174
Cdd:cd18572 32 REAFYRAVL--LLLLLSVLSGLF--SGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 175 EGTGDKVGLAFQMMAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRT 254
Cdd:cd18572 108 DPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 255 VIAFNGQEYECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLT-VFFSVMMGS 333
Cdd:cd18572 188 VRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTfMLYQQQLGE 267
|
250 260
....*....|....*....|
gi 17558664 334 mALGQAGQQFATIGTALGAA 353
Cdd:cd18572 268 -AFQSLGDVFSSLMQAVGAA 286
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
383-602 |
1.46e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.44 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:PRK13632 8 IKVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEP-NLF-NTSIEQNIRYG-------RSDVSDEdIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIA 533
Cdd:PRK13632 87 IIFQNPdNQFiGATVEDDIAFGlenkkvpPKKMKDI-IDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 534 RALVRNPKILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGT 602
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
383-601 |
2.34e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN---IKYLRQ 459
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEPNL-FNTSIEQNIRY-----GRS-DVSDEDIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAI 532
Cdd:COG2884 80 RIGVVFQDFRLlPDRTVYENVALplrvtGKSrKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 533 ARALVRNPKILLLDEATSALDAE-SESIVQsALENASRGRTTIVIA-HRLSTVRNADK-IIVMKAGQVMEVG 601
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPEtSWEIME-LLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1030-1257 |
2.84e-37 |
|
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: 140.50 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL---RK 1106
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 HIALVSQEPILFDT-SIRENIVYGLQpgEYTHeqietaCSKANIHKFIDELPDgyetRVGEKGT------QLSGGQKQRI 1179
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPLR--EHTD------LSEAEIRELVLEKLE----LVGLPGAadkmpsELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1180 AIARALIRNPKILLLDEATSALDTESE-------KQVQVALDAaakdrTCIVVAHRLSTIVNAGC-IMVVKNGQVVEQGT 1251
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSavideliRELRDELGL-----TSVVVTHDLDSAFAIADrVAVLADGKIIAEGT 225
|
....*.
gi 17558664 1252 HNELIA 1257
Cdd:COG1127 226 PEELLA 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1030-1257 |
2.84e-37 |
|
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: 140.90 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILF-DTSIRENIVYGLQPGEYTHEQIETAcskanihkfIDEL-------PDGYETRVGEkgtQLSGGQKQRIAI 1181
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRER---------ADELlalvgldPAEFADRYPH---ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1182 ARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKD--RTCIVVAHRL-STIVNAGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
394-609 |
4.31e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 142.95 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL---VGVVSQEPnl 470
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 471 fntsieqnirYG----RSDVSD---E--DIARALKEANAADFIKTFPE--GLNTLVGDRGVQM-SGGQKQRIAIARALVR 538
Cdd:COG4608 105 ----------YAslnpRMTVGDiiaEplRIHGLASKAERRERVAELLElvGLRPEHADRYPHEfSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 539 NPKILLLDEATSALDAeseSIvQSALEN------ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:COG4608 175 NPKLIVCDEPVSALDV---SI-QAQVLNlledlqDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1044-1251 |
6.88e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 139.36 E-value: 6.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1044 AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDL--RQMNPKHLRKHIALVSQEPILF-DT 1120
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYGLQpgeyTHEQIetacSKANIHKFIDELPDgyetRVG--EKG----TQLSGGQKQRIAIARALIRNPKILLL 1194
Cdd:COG1126 93 TVLENVTLAPI----KVKKM----SKAEAEERAMELLE----RVGlaDKAdaypAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1195 DEATSALDTESEKQV-QVALDAAAKDRTCIVVAH----------RlstivnagcIMVVKNGQVVEQGT 1251
Cdd:COG1126 161 DEPTSALDPELVGEVlDVMRDLAKEGMTMVVVTHemgfarevadR---------VVFMDGGRIVEEGP 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
400-619 |
6.94e-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: 140.04 E-value: 6.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQNI 479
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 RYGRSdVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESI 559
Cdd:cd03288 116 DPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 560 VQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQK-GLYHELVHA 619
Cdd:cd03288 195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1030-1245 |
8.86e-37 |
|
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: 136.93 E-value: 8.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH--LRKH 1107
Cdd:cd03229 1 LELKNVSKRYGQKTV---LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILFDT-SIRENIVYGLqpgeytheqietacskanihkfidelpdgyetrvgekgtqlSGGQKQRIAIARALI 1186
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALGL-----------------------------------------SGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1187 RNPKILLLDEATSALDTESEKQVQvALDAAAKDR---TCIVVAHRLSTIVN-AGCIMVVKNGQ 1245
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVR-ALLKSLQAQlgiTVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
381-602 |
8.88e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 142.90 E-value: 8.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 381 GRISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID-----DIPIEDFNIk 455
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvtDLPPKDRNI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 456 ylrqlvGVVSQEPNLF-NTSIEQNIRYG--RSDVSDEDIARALKEAnaADfiktfpeglntLVG-----DRGV-QMSGGQ 526
Cdd:COG3839 78 ------AMVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREA--AE-----------LLGledllDRKPkQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 527 KQRIAIARALVRNPKILLLDEATSALDAESEsiVQSALE----NASRGRTTIVIAH------RLstvrnADKIIVMKAGQ 596
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKLR--VEMRAEikrlHRRLGTTTIYVTHdqveamTL-----ADRIAVMNDGR 211
|
....*.
gi 17558664 597 VMEVGT 602
Cdd:COG3839 212 IQQVGT 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1030-1251 |
2.10e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAVpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPkHLRkHIA 1109
Cdd:COG3842 6 LELENVSKRYGDVTAL---DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKR-NVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILF-DTSIRENIVYGLQpgeytheqiETACSKANIHKFIDELPD-----GYETRvgeKGTQLSGGQKQRIAIAR 1183
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGLR---------MRGVPKAEIRARVAELLElvgleGLADR---YPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAH------RLS-TIVnagcimVVKNGQVVEQGT 1251
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHdqeealALAdRIA------VMNDGRIEQVGT 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
383-609 |
4.52e-36 |
|
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: 136.98 E-value: 4.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIkYLRQlVG 462
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-HKRP-VN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLF-NTSIEQNIRYG------RSDVSDEDIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARA 535
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 536 LVRNPKILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLS---TVrnADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
383-618 |
5.45e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.14 E-value: 5.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfnikyLRQLVG 462
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNL---FNTSIEQNI------------RYGRSDvsDEDIARALKEANAADFiktfpegLNTLVGdrgvQMSGGQK 527
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRAD--REAVDEALERVGLEDL-------ADRPIG----ELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 528 QRIAIARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVR-NADKIIVMK-----AGQVMEV 600
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNrglvaHGPPEEV 225
|
250
....*....|....*...
gi 17558664 601 GTHETLIEQKGLYHELVH 618
Cdd:COG1121 226 LTPENLSRAYGGPVALLA 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1032-1251 |
7.49e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 139.83 E-value: 7.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFfrYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKST---VISLLERlydPLEGAVTVDNNDLRQMNPKHL---R 1105
Cdd:COG1135 7 LSKTF--PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1106 KHIALVSQEPILFDT-SIRENIVYGLqpgEYTHeqietaCSKANIHKFIDELPDgyetRVG--EKG----TQLSGGQKQR 1178
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPL---EIAG------VPKAEIRKRVAELLE----LVGlsDKAdaypSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1179 IAIARALIRNPKILLLDEATSALDTESEKQVqVALDAAAKDR---TCIVVAHRLStivnagcimVVK----------NGQ 1245
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSI-LDLLKDINRElglTIVLITHEMD---------VVRricdrvavleNGR 218
|
....*.
gi 17558664 1246 VVEQGT 1251
Cdd:COG1135 219 IVEQGP 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
629-1281 |
8.36e-36 |
|
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: 148.56 E-value: 8.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 629 PKKKEAERRMSRQTSQRKGSVNF-KTQESQVDEKPGAPPAPEAAEKEIKRLKKELeeegavKANLFKILrYAR--PEWIY 705
Cdd:TIGR00957 249 PVLVENWKKECKKTRKQPVSAVYgKKDPSKPKGSSQLDANEEVEALIVKSPHKPR------KPSLFKVL-YKTfgPYFLM 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAiiaALIQGAVMPAFSLFFSQIINVFSNPDRDQMKkdGHFWALMFLVLAAVQgTSMLFQ----CSLFGvaaerltMR 781
Cdd:TIGR00957 322 SFCF---KAIHDLMMFIGPQILSLLIRFVNDPMAPDWQ--GYFYTGLLFVCACLQ-TLILHQyfhiCFVSG-------MR 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 782 IRSKVYRNVLRQDATYFDMPKHSP--GRITTRLATDAPNIKSaidyrLGSIFNAIASVGGGLGIAFYYGWQ--------- 850
Cdd:TIGR00957 389 IKTAVMGAVYRKALVITNSARKSStvGEIVNLMSVDAQRFMD-----LATYINMIWSAPLQVILALYFLWLnlgpsvlag 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 851 MAFLVMAIfPFMAVGQALMMKYHggsaTSDAKEMENAGKTAMEAIENIRTVqaltlqtKLYNIFCSHLDAPHGgnISKAI 930
Cdd:TIGR00957 464 VAVMVLMV-PLNAVMAMKTKTYQ----VAHMKSKDNRIKLMNEILNGIKVL-------KLYAWELAFLDKVEG--IRQEE 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 931 IRGL-TYGFANSIQFFTYAAAFRFGLFLIFDKNVLMEPENVLRVLFA-ISFS-FGTIGFAASYFPEYIKATFAAGLIFNM 1007
Cdd:TIGR00957 530 LKVLkKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAfVSLAlFNILRFPLNILPMVISSIVQASVSLKR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1008 LE-----EEPRIDGMTSSGTYPQLSGEVKLNKVFFRYPeRPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLY 1082
Cdd:TIGR00957 610 LRiflshEELEPDSIERRTIKPGEGNSITVHNATFTWA-RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1083 DPLEGAVtvdnndlrqmnpkHLRKHIALVSQEPILFDTSIRENIVYGLQPGEYTHEQIETACSkanIHKFIDELPDGYET 1162
Cdd:TIGR00957 689 DKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA---LLPDLEILPSGDRT 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1163 RVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQV---QVALDAAAKDRTCIVVAHRLSTIVNAGCIM 1239
Cdd:TIGR00957 753 EIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfehVIGPEGVLKNKTRILVTHGISYLPQVDVII 832
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17558664 1240 VVKNGQVVEQGTHNELIAKRGAYFALTQKQSSNQSGGAFDTS 1281
Cdd:TIGR00957 833 VMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDS 874
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1031-1259 |
1.30e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 135.77 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPErpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL---RKH 1107
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILFD-TSIRENIVYGLQP---------GEYTHEQIETACS---KANIHKFidelpdgYETRVGekgtQLSGG 1174
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGrrstwrslfGLFPKEEKQRALAaleRVGLLDK-------AYQRAD----QLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1175 QKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVAL--DAAAKDRTCIVVAHRLSTIV-NAGCIMVVKNGQVVEQGT 1251
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGP 228
|
....*...
gi 17558664 1252 HNELIAKR 1259
Cdd:cd03256 229 PAELTDEV 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1030-1248 |
1.54e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.18 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPerPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPK---HLRK 1106
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 HIALVSQE-PILFDTSIRENI-----VYGLQPGEYtHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIA 1180
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENValplrVTGKSRKEI-RRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVA-HRLStIVNA--GCIMVVKNGQVVE 1248
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1032-1258 |
4.84e-35 |
|
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: 135.08 E-value: 4.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERpAVPILQG-------------------LNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVD 1092
Cdd:cd03294 6 LYKIFGKNPQK-AFKLLAKgkskeeilkktgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1093 NNDLRQMNPKHL----RKHIALVSQEPILF-DTSIRENIVYGL----QPGEYTHEQIETACSKANIHKFIDELPDgyetr 1163
Cdd:cd03294 85 GQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENVAFGLevqgVPRAEREERAAEALELVGLEGWEHKYPD----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1164 vgekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQ---VALDAAAKdRTCIVVAHRLSTIVNAGC-IM 1239
Cdd:cd03294 160 ------ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQdelLRLQAELQ-KTIVFITHDLDEALRLGDrIA 232
|
250
....*....|....*....
gi 17558664 1240 VVKNGQVVEQGTHNELIAK 1258
Cdd:cd03294 233 IMKDGRLVQVGTPEEILTN 251
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1028-1255 |
5.18e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.51 E-value: 5.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1028 GEVKLNKVFFRYPErpaVPILQGLNVHVKPGQTLALVGPSGCGKST---VISLLErlyDPLEGAVTVDNNDLRQMNPKHl 1104
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLE---DPTSGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1105 RkHIALVSQEPILFDT-SIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRI 1179
Cdd:COG3839 75 R-NIAMVFQSYALYPHmTVYENIAFPLKlrkvPKAEIDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1180 AIARALIRNPKILLLDEATSALD------TESE-KQVQVALDAaakdrTCIVVAHRLS---TIvnAGCIMVVKNGQVVEQ 1249
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRLGT-----TTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215
|
....*.
gi 17558664 1250 GTHNEL 1255
Cdd:COG3839 216 GTPEEL 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1030-1229 |
5.19e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.41 E-value: 5.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERpaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH-- 1107
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 -IALVSQEPILFD-TSIRENIVYGLQP---------GEYTHEQIETAcskaniHKFIDE--LPDGYETRVGekgtQLSGG 1174
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVLAGRLGrtstwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1175 QKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRL 1229
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQV 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
394-609 |
6.20e-35 |
|
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: 141.36 E-value: 6.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKST----IIQLLqrfynPDAGQILIDDIPIEDFNIKYLRQL---VGVVSQ 466
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 467 EPnlFNT-----SIEQNIRYG----RSDVSDED----IARALKEAN-AADFIKTFPEglntlvgdrgvQMSGGQKQRIAI 532
Cdd:COG4172 370 DP--FGSlsprmTVGQIIAEGlrvhGPGLSAAErrarVAEALEEVGlDPAARHRYPH-----------EFSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 533 ARALVRNPKILLLDEATSALDAeseSIVQSALE-----NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDV---SVQAQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQV 513
|
...
gi 17558664 607 IEQ 609
Cdd:COG4172 514 FDA 516
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
383-607 |
1.01e-34 |
|
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: 133.19 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRAdvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLF-NTSIEQNIrygrSDV-SDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNP 540
Cdd:cd03295 79 YVIQQIGLFpHMTVEENI----ALVpKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 541 KILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRL-STVRNADKIIVMKAGQVMEVGTHETLI 607
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
404-609 |
1.46e-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: 133.92 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 404 VSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL----VGVVSQEPNLF-NTSIEQN 478
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 479 IRYG------RSDVSDEDIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARALVRNPKILLLDEATSAL 552
Cdd:cd03294 123 VAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 553 DAESESIVQSALEN--ASRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:cd03294 192 DPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1031-1259 |
2.87e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.80 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPERPavpiLQgLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPkHLRKhIAL 1110
Cdd:COG3840 3 RLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERP-VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQEPILFD-TSIRENIVYGLQPG----EYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIARAL 1185
Cdd:COG3840 76 LFQENNLFPhLTVAQNIGLGLRPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1186 IRNPKILLLDEATSALDTeSEKQVQVAL-DAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIAKR 1259
Cdd:COG3840 145 VRKRPILLLDEPFSALDP-ALRQEMLDLvDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1029-1257 |
3.01e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 134.41 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1029 EVK-LNKVFFRypERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPL---EGAVTVDNNDLRQMNPKHL 1104
Cdd:COG0444 3 EVRnLKVYFPT--RRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1105 R----KHIALVSQEPIlfdTS------IRENIVYGLQpgeyTHEQIetacSKANIHKFIDE------LPDGyETRVGEKG 1168
Cdd:COG0444 81 RkirgREIQMIFQDPM---TSlnpvmtVGDQIAEPLR----IHGGL----SKAEARERAIEllervgLPDP-ERRLDRYP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1169 TQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVqvaLD-----AAAKDRTCIVVAHRLSTIVN-AGCIMVVK 1242
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQI---LNllkdlQRELGLAILFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*
gi 17558664 1243 NGQVVEQGTHNELIA 1257
Cdd:COG0444 226 AGRIVEEGPVEELFE 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1030-1246 |
3.35e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 129.44 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmNPKHLRKHIA 1109
Cdd:cd03230 1 IEVRNLSKRYGKKTA---LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDT-SIRENIvyglqpgeytheqietacskanihkfidelpdgyetrvgekgtQLSGGQKQRIAIARALIRN 1188
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1189 PKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQV 1246
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFwELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
399-597 |
5.38e-34 |
|
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: 130.49 E-value: 5.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQ---PGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYL----RQLVGVVSQEPNLF 471
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 -NTSIEQNIRYG---RSDVSDEDIARALKEAnaadfiktfpEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDE 547
Cdd:cd03297 88 pHLNVRENLAFGlkrKRNREDRISVDELLDL----------LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 548 ATSALDAESESIVQSALEN--ASRGRTTIVIAHRLSTV-RNADKIIVMKAGQV 597
Cdd:cd03297 158 PFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRL 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
398-605 |
7.47e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.46 E-value: 7.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-VGVVSQEPNLFNT-SI 475
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNI-------RYGRSDVsdediaRALKEAnAADFIKTF--PEGLNTLVGDrgvqMSGGQKQRIAIARALVRNPKILLLD 546
Cdd:COG1129 97 AENIflgreprRGGLIDW------RAMRRR-ARELLARLglDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 547 EATSAL-DAESE---SIVQSaLenASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVmeVGTHET 605
Cdd:COG1129 166 EPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL--VGTGPV 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1251 |
1.39e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAvPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPilfD-----TSIRENIVYGLQPGEYTHEQ----IETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIA 1180
Cdd:PRK13632 87 IIFQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVNAGCIMVVKNGQVVEQGT 1251
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
383-607 |
2.67e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.72 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPT---RADVKIlkgvsldaQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIkYLRQ 459
Cdd:COG3840 2 LRLDDLTYRYGDfplRFDLTI--------AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 lVGVVSQEPNLFN-TSIEQNIRYGRSD---VSDED---IARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAI 532
Cdd:COG3840 73 -VSMLFQENNLFPhLTVAQNIGLGLRPglkLTAEQraqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 533 ARALVRNPKILLLDEATSALD----AESESIVQSAleNASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLI 607
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDEL--CRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1030-1238 |
3.59e-33 |
|
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: 127.60 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmNPKHLRKHIA 1109
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDT-SIRENIVY--GLQPGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIARALI 1186
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFwaALYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1187 RNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVA-HRLSTIVNAGCI 1238
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1034-1247 |
5.35e-33 |
|
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: 126.99 E-value: 5.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1034 KVFFRYPERPAvpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLrqmNPKHLRKHIALVSQ 1113
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1114 EP--ILFDTSIRENIVYGLQPGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIARALIRNPKI 1191
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1192 LLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHR---LSTIVNAgcIMVVKNGQVV 1247
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVgELIRELAAQGKAVIVITHDyefLAKVCDR--VLLLANGAIV 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
383-602 |
9.54e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 130.69 E-value: 9.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRA-DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL- 460
Cdd:PRK11153 2 IELKNISKVFPQGGrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 --VGVVSQEPNLFNtsieqnirygrSDVSDEDIARALKEAN-AADFIKTFPEGLNTLVG-----DR-GVQMSGGQKQRIA 531
Cdd:PRK11153 82 rqIGMIFQHFNLLS-----------SRTVFDNVALPLELAGtPKAEIKARVTELLELVGlsdkaDRyPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 532 IARALVRNPKILLLDEATSALDAESesiVQSALE-----NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGT 602
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPAT---TRSILEllkdiNRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1047-1227 |
1.74e-32 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 125.72 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVD----NNDLRQMNpkHLRKHIALVSQEPILF-DTS 1121
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglklTDDKKNIN--ELRQKVGMVFQQFNLFpHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1122 IRENIVYGLQP--GEYTHEQIETAcskanihkfIDELpdgyeTRVG--EKGT----QLSGGQKQRIAIARALIRNPKILL 1193
Cdd:cd03262 93 VLENITLAPIKvkGMSKAEAEERA---------LELL-----EKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 17558664 1194 LDEATSALDTESEKQV-QVALDAAAKDRTCIVVAH 1227
Cdd:cd03262 159 FDEPTSALDPELVGEVlDVMKDLAEEGMTMVVVTH 193
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1030-1256 |
2.04e-32 |
|
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: 127.12 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGA-VTVDNNDLRQMNPKHLRKHI 1108
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1109 ALVS---QEPILFDTSIRENIVYGLQ-----PGEYTHEQIETAcskaniHKFIDELpdGYETRVGEKGTQLSGGQKQRIA 1180
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFdsiglYREPTDEQRERA------RELLELL--GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESEKQVQVALD--AAAKDRTCIVVAHRLSTIVNagCI---MVVKNGQVVEQGTHNEL 1255
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDklAAEGAPTLVLVTHHVEEIPP--GIthvLLLKDGRVVAAGPKEEV 230
|
.
gi 17558664 1256 I 1256
Cdd:COG1119 231 L 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
401-608 |
2.18e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 126.30 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKylRQLVGVVSQEPNLF-NTSIEQNI 479
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 RYG--RSDVSDEDIARALKEAnaADFIktfpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESE 557
Cdd:cd03299 93 AYGlkKRKVDKKEIERKVLEI--AEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 558 SIVQSALENASR--GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIE 608
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
383-602 |
3.38e-32 |
|
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: 125.31 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRaDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfNIKYLRQLVG 462
Cdd:cd03263 1 LQIRNLTKTYKKG-TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNT-SIEQNIRY-----GRSDVS-DEDIARALKEANAADFiktfpegLNTLVGDrgvqMSGGQKQRIAIARA 535
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEiKEEVELLLRVLGLTDK-------ANKRART----LSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 536 LVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGT 602
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1030-1257 |
3.44e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.05 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPE--RPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH 1107
Cdd:PRK13635 6 IRVEHISFRYPDaaTYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPilfD-----TSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQR 1178
Cdd:PRK13635 83 VGMVFQNP---DnqfvgATVQDDVAFGLEnigvPREEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1179 IAIARALIRNPKILLLDEATSALDTESEKQV--QVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELI 1256
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVleTVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
.
gi 17558664 1257 A 1257
Cdd:PRK13635 229 K 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
397-601 |
3.65e-32 |
|
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: 125.06 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID-----DIPIEDFNIkylrqlvGVVSQEPNLF 471
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtDLPPKDRDI-------AMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 -NTSIEQNIRYG--RSDVSDEDIARALKEAnaADFIktfpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEA 548
Cdd:cd03301 85 pHMTVYDNIAFGlkLRKVPKDEIDERVREV--AELL-----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 549 TSALDAESESIVQSALENASR--GRTTIVIAH-RLSTVRNADKIIVMKAGQVMEVG 601
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
384-597 |
3.82e-32 |
|
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: 124.68 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYptRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiEDFNIKYLRQLVGV 463
Cdd:cd03226 1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQEPN--LFNTSIEQNIRYGRSDVSD--EDIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIARALVRN 539
Cdd:cd03226 76 VMQDVDyqLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHPLSL-----------SGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 540 PKILLLDEATSALDAES-ESIVQSALENASRGRTTIVIAHR---LSTVrnADKIIVMKAGQV 597
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITHDyefLAKV--CDRVLLLANGAI 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1030-1251 |
5.33e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.59 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNndlrqMNPKHLRKHIA 1109
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPIL---FDTSIRENIVYGLQ--------PGEYTHEQIETACSKANIHKFIDelpdgyeTRVGEkgtqLSGGQKQR 1178
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLMGRYgrrglfrrPSRADREAVDEALERVGLEDLAD-------RPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1179 IAIARALIRNPKILLLDEATSALDTESEKQVQVALDA-AAKDRTCIVVAHRLSTIV-NAGCIMVVkNGQVVEQGT 1251
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGP 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
971-1228 |
6.44e-32 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 132.62 E-value: 6.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 971 LRVLFAISFSFGTIGFAASYFPEYIK--ATFAAGLI----FNMLEEEPRIDGMTSSGTYPQLSGEVKLNKVFFRYPERpa 1044
Cdd:COG4178 298 LGGLMQAASAFGQVQGALSWFVDNYQslAEWRATVDrlagFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDG-- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVdnndlrqmnPKHLRkhIALVSQEPILFDTSIRE 1124
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGAR--VLFLPQRPYLPLGTLRE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGLQPGEYTHEQIETACSKANIHKFIDELpdgyeTRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTE 1204
Cdd:COG4178 445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
250 260
....*....|....*....|....
gi 17558664 1205 SEKQVQVALDAAAKDRTCIVVAHR 1228
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHR 543
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1046-1256 |
8.09e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 125.51 E-value: 8.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPIL-FDTSIRE 1124
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGLQP--------GEYTHEQIETACSKANihkfIDELPDgyetrvgEKGTQLSGGQKQRIAIARALIRNPKILLLDE 1196
Cdd:PRK11231 96 LVAYGRSPwlslwgrlSAEDNARVNQAMEQTR----INHLAD-------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1197 ATSALDTESekqvQVAL-----DAAAKDRTCIVVAHRLstivNAGC-----IMVVKNGQVVEQGTHNELI 1256
Cdd:PRK11231 165 PTTYLDINH----QVELmrlmrELNTQGKTVVTVLHDL----NQASrycdhLVVLANGHVMAQGTPEEVM 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
396-606 |
9.39e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 127.39 E-value: 9.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiEDF------NIKYLRQLVGVVSQEPn 469
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG---QDLlkadpeAQKLLRQKIQIVFQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 470 lfntsieqnirYG----RSDVSD---------EDIARALKEANAADFIKTFpeGLNTLVGDRGVQM-SGGQKQRIAIARA 535
Cdd:PRK11308 102 -----------YGslnpRKKVGQileepllinTSLSAAERREKALAMMAKV--GLRPEHYDRYPHMfSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 536 LVRNPKILLLDEATSALDAEsesiVQSALEN------ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVS----VQAQVLNlmmdlqQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
397-602 |
1.91e-31 |
|
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: 121.00 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEdfnikylrqlvgvvsqepnlFNTSIE 476
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------------FASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 477 qnirygrsdvsdediARALKeanaadfIKTFPeglntlvgdrgvQMSGGQKQRIAIARALVRNPKILLLDEATSAL-DAE 555
Cdd:cd03216 72 ---------------ARRAG-------IAMVY------------QLSVGERQMVEIARALARNARLLILDEPTAALtPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17558664 556 SESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVmeVGT 602
Cdd:cd03216 118 VERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV--VGT 163
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1048-1229 |
2.04e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.12 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYD-----PLEGAVTVDNNDL--RQMNPKHLRKHIALVSQEPILFDT 1120
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYGL-----QPGEYTHEQIETACSKANIHkfiDELPDgyetRVGEKGTQLSGGQKQRIAIARALIRNPKILLLD 1195
Cdd:PRK14239 101 SIYENVVYGLrlkgiKDKQVLDEAVEKSLKGASIW---DEVKD----RLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 17558664 1196 EATSALDTESEKQVQVALDAAAKDRTCIVVAHRL 1229
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
383-604 |
2.41e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.59 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDD------IPIEDFNIKY 456
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 LRQLVGVVSQEPNLF------NTSIEQNIRY-GRSDvsDEDIARA---LKEANAADFIKTFPeglntlvgdrgVQMSGGQ 526
Cdd:PRK11124 80 LRRNVGMVFQQYNLWphltvqQNLIEAPCRVlGLSK--DQALARAeklLERLRLKPYADRFP-----------LHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 527 KQRIAIARALVRNPKILLLDEATSALDAE-SESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHE 604
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
84-357 |
2.76e-31 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 125.05 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 84 PNSTASEKAAARAEFSHEVIQncLKYVYLGCGIFAagFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLS 163
Cdd:cd18780 27 TNHSGSGGEEALRALNQAVLI--LLGVVLIGSIAT--FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 164 NKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGG 243
Cdd:cd18780 103 NRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAAST 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 244 IAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTvL 323
Cdd:cd18780 183 VAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGL-L 261
|
250 260 270
....*....|....*....|....*....|....
gi 17558664 324 TVFfsvMMGSMalgqagqqfaTIGTALGAAASLY 357
Cdd:cd18780 262 TSF---LLYTL----------TVAMSFAFLSSLY 282
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
384-593 |
2.91e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 122.26 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFnikylRQLVGV 463
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQEPNL---FNTSIEQNIRYGR----------SDVSDEDIARALKEANAADFIktfpeglntlvgDRGV-QMSGGQKQR 529
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLyghkglfrrlSKADKAKVDEALERVGLSELA------------DRQIgELSGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 530 IAIARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTV-RNADKIIVMK 593
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLN 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
383-599 |
3.07e-31 |
|
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: 122.93 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRA-DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPI----EDFNIKYL 457
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 458 RQLVGVVSQE----PNLfnTSIEqNI-----RYGRSDvsDEDIARALKEAnaadfiktfpEGLNTLVGDRGVQMSGGQKQ 528
Cdd:COG4181 89 ARHVGFVFQSfqllPTL--TALE-NVmlpleLAGRRD--ARARARALLER----------VGLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 529 RIAIARALVRNPKILLLDEATSALD-AESESIVQSALE-NASRGRTTIVIAHRLSTVRNADKIIVMKAGQVME 599
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDaATGEQIIDLLFElNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1032-1255 |
3.09e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.41 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKST---VISLLERlydPLEGAVTVDNNDLRQMNPKHLRkHI 1108
Cdd:COG1118 5 VRNISKRFGSFTL---LDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDLFTNLPPRER-RV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1109 ALVSQEPILF-DTSIRENIVYGLQPGEYTHEQIetacsKANIHKFIDE--LpDGYETRvgeKGTQLSGGQKQRIAIARAL 1185
Cdd:COG1118 78 GFVFQHYALFpHMTVAENIAFGLRVRPPSKAEI-----RARVEELLELvqL-EGLADR---YPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1186 IRNPKILLLDEATSALDTESEKQVQVAL----DAAakDRTCIVVAH------RLstivnagC--IMVVKNGQVVEQGTHN 1253
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLrrlhDEL--GGTTVFVTHdqeealEL-------AdrVVVMNQGRIEQVGTPD 219
|
..
gi 17558664 1254 EL 1255
Cdd:COG1118 220 EV 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
383-612 |
3.96e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 123.71 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADVKiLKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEP-NLFNTSIEQ-NIRYGRSD--VSDEDIAR----ALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIAR 534
Cdd:PRK13648 87 IVFQNPdNQFVGSIVKyDVAFGLENhaVPYDEMHRrvseALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 535 ALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIE-QKG 611
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDhAEE 235
|
.
gi 17558664 612 L 612
Cdd:PRK13648 236 L 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
399-602 |
4.15e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.39 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKY--LRQLVGVVSQEP--NLFNTS 474
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIRYGRSD--VSDEDIARALKEAnaadfIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSAL 552
Cdd:PRK13637 101 IEKDIAFGPINlgLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 553 D--AESESIVQSALENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGT 602
Cdd:PRK13637 176 DpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
400-606 |
5.82e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 5.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN--------IKYLRQLVGVVSQEPNLF 471
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 -NTSIEQNIRYGRSDVSDEDIARALKEANAadfiktfpegLNTLVGDRGVQ------MSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK11264 98 pHRTVLENIIEGPVIVKGEPKEEATARARE----------LLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 545 LDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
383-604 |
5.89e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.43 E-value: 5.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiEDFN--------- 453
Cdd:COG4161 3 IQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG---HQFDfsqkpseka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 454 IKYLRQLVGVVSQEPNLF-NTSIEQNIRYGRSDV----SDEDIARA---LKEANAADFIKTFPeglntlvgdrgVQMSGG 525
Cdd:COG4161 77 IRLLRQKVGMVFQQYNLWpHLTVMENLIEAPCKVlglsKEQAREKAmklLARLRLTDKADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 526 QKQRIAIARALVRNPKILLLDEATSALDAE-SESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTH 603
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
.
gi 17558664 604 E 604
Cdd:COG4161 226 S 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1030-1244 |
5.96e-31 |
|
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: 121.67 E-value: 5.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPerPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL----R 1105
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1106 KHIALVSQEPILFDTSIRENIVYGLQPGEYTHEQIETACSkanIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARAL 1185
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1186 IRNPKILLLDEATSALDTE-SEKQVQVALDAAAKD--RTCIVVAHRLSTIVNAGCIMVVKNG 1244
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1035-1251 |
6.08e-31 |
|
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: 129.42 E-value: 6.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1035 VFFRYPERpaVPILQGLNVHVKPGQTLALVGPSGCGKSTV-ISLLeRLyDPLEGAVTVDNNDLRQMNPK---HLRKHIAL 1110
Cdd:COG4172 291 LFRRTVGH--VKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDGLSRRalrPLRRRMQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQEPilFDT-----SIRENIVYGL---QPGEYTHEQIETAC--------SKANIHKFIDELpdgyetrvgekgtqlSGG 1174
Cdd:COG4172 367 VFQDP--FGSlsprmTVGQIIAEGLrvhGPGLSAAERRARVAealeevglDPAARHRYPHEF---------------SGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1175 QKQRIAIARALIRNPKILLLDEATSALDTESEKQVqVALDAAAKDR---TCIVVAHRLStIVNAGC--IMVVKNGQVVEQ 1249
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQI-LDLLRDLQREhglAYLFISHDLA-VVRALAhrVMVMKDGKVVEQ 507
|
..
gi 17558664 1250 GT 1251
Cdd:COG4172 508 GP 509
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
377-602 |
6.23e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 123.22 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 377 SKISGRISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFyNPDAGQILIDDiPIEDF---- 452
Cdd:PRK14258 2 SKLIPAIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEG-RVEFFnqni 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 453 -----NIKYLRQLVGVVSQEPNLFNTSIEQNIRYG------RSDVSDEDIAR-ALKEANAADFIKTfpeglntLVGDRGV 520
Cdd:PRK14258 77 yerrvNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVEsALKDADLWDEIKH-------KIHKSAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 521 QMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENAS-RGRTTIVI-AHRLSTV-RNADKIIVMKA--- 594
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIvSHNLHQVsRLSDFTAFFKGnen 229
|
250
....*....|
gi 17558664 595 --GQVMEVGT 602
Cdd:PRK14258 230 riGQLVEFGL 239
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1030-1257 |
7.00e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.00 E-value: 7.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlRKHIA 1109
Cdd:PRK10771 2 LKLTDITWLYHHLP-----MRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFD-TSIRENIVYGLQPG----EYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIARA 1184
Cdd:PRK10771 75 MLFQENNLFShLTVAQNIGLGLNPGlklnAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1185 LIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLStivNAGCI----MVVKNGQVVEQGTHNELIA 1257
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLS 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
394-589 |
8.23e-31 |
|
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: 120.66 E-value: 8.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLvGVVSQEPNLFNT 473
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL-AYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 -SIEQNIR-----YGRsDVSDEDIARALKEANAADFiktfpegLNTLVGdrgvQMSGGQKQRIAIARALVRNPKILLLDE 547
Cdd:COG4133 90 lTVRENLRfwaalYGL-RADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17558664 548 ATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRNADKI 589
Cdd:COG4133 158 PFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1057-1250 |
9.27e-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: 9.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1057 PGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDN---NDLRQ-MN-PKHlRKHIALVSQEPILF-DTSIRENIVYGL 1130
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkINlPPQ-QRKIGLVFQQYALFpHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1131 QpgeytheqietACSKANIHKFIDELPD--GYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQ 1208
Cdd:cd03297 101 K-----------RKRNREDRISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17558664 1209 VQVALDAAAKD--RTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG 1250
Cdd:cd03297 170 LLPELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1032-1251 |
1.04e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 124.91 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFfrYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRK----- 1106
Cdd:PRK11153 7 ISKVF--PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrqi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 -----HIALVSQEPIlFDtsireNIVYGLqpgeytheqiETA-CSKANIHKFIDELPDgyetRVG--EKG----TQLSGG 1174
Cdd:PRK11153 85 gmifqHFNLLSSRTV-FD-----NVALPL----------ELAgTPKAEIKARVTELLE----LVGlsDKAdrypAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1175 QKQRIAIARALIRNPKILLLDEATSALDTESEKQVqvaLDAAAK-DR----TCIVVAHRLSTIVN-AGCIMVVKNGQVVE 1248
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSI---LELLKDiNRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
...
gi 17558664 1249 QGT 1251
Cdd:PRK11153 222 QGT 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
399-610 |
1.13e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 122.19 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRF--YNPD---AGQILID--DIPIEDFNIKYLRQLVGVVSQEPNLF 471
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNghNIYSPRTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 NTSIEQNIRYG-------RSDVSDEDIARALKEANAADFIKTfpeglntLVGDRGVQMSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK14239 99 PMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 545 LDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVG-THETLIEQK 610
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNdTKQMFMNPK 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1046-1251 |
3.05e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.29 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHlrKHIALVSQEPILF-DTSIRE 1124
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGLQPGEYTHEQIETACSKA----NIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIARALIRNPKILLLDEATSA 1200
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEAlrmvQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1201 LDTESEKQVQVALDAAAKDR--TCIVVAH-RLSTIVNAGCIMVVKNGQVVEQGT 1251
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
393-597 |
3.33e-30 |
|
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: 118.81 E-value: 3.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 393 PTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL--QRFYNPDAGQILIDDIPIEDFNIKYLrqlVGVVSQEPNL 470
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRKI---IGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 471 FNT-SIEQNIRYgrsdvsdediARALKeanaadfiktfpeGLntlvgdrgvqmSGGQKQRIAIARALVRNPKILLLDEAT 549
Cdd:cd03213 94 HPTlTVRETLMF----------AAKLR-------------GL-----------SGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 550 SALDAESESIVQSALEN-ASRGRTTIVIAHRLST--VRNADKIIVMKAGQV 597
Cdd:cd03213 140 SGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
383-597 |
3.49e-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: 119.43 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPtrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN---IKYLRQ 459
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEPNLF-NTSIEQNIRYGR--SDVSDEDIAR----ALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAI 532
Cdd:cd03292 79 KIGVVFQDFRLLpDRNVYENVAFALevTGVPPREIRKrvpaALELVGLSHKHRALPAEL-----------SGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 533 ARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIA-HRLSTVRNADK-IIVMKAGQV 597
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAKELVDTTRHrVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1031-1250 |
3.99e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.18 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnpkhlRKHIAL 1110
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQEPIL---FDTSIRENIVYGLQP-----GEYTHEQ---IETACSKANIHKFIDElpdgyetRVGEkgtqLSGGQKQRI 1179
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGhkglfRRLSKADkakVDEALERVGLSELADR-------QIGE----LSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1180 AIARALIRNPKILLLDEATSALDTESEKQVQVALDA-AAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQG 1250
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1043-1258 |
4.01e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.29 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1043 PAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH-IALVSQEPILFDT- 1120
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYGLQPGEY-------THEQIETACSKANIHkfIDelPDgyeTRVGEkgtqLSGGQKQRIAIARALIRNPKILL 1193
Cdd:COG1129 95 SVAENIFLGREPRRGglidwraMRRRARELLARLGLD--ID--PD---TPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1194 LDEATSAL-DTESEKQVQVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG-----THNELIAK 1258
Cdd:COG1129 164 LDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
388-608 |
4.32e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.81 E-value: 4.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 388 VEFTYPTR--ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIED--FNIKYLRQLVGV 463
Cdd:PRK09493 2 IEFKNVSKhfGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQEPNLFN--TSIEqNIRYGRSDVsdediaRALKEANAADFIKTFPE--GLNTLVGDRGVQMSGGQKQRIAIARALVRN 539
Cdd:PRK09493 82 VFQQFYLFPhlTALE-NVMFGPLRV------RGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 540 PKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIE 608
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1044-1257 |
5.89e-30 |
|
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: 119.08 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1044 AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNP-KHLRKHIALVSQEPILFDT-S 1121
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1122 IRENIVYGLQPGEYTHEqietacsKANIHKFIDELPDGYEtRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSAL 1201
Cdd:cd03224 92 VEENLLLGAYARRRAKR-------KARLERVYELFPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1202 DTESEKQVQVALDAAAKDRTCIVV----AHRLSTIVNAGCIMVvkNGQVVEQGTHNELIA 1257
Cdd:cd03224 164 APKIVEEIFEAIRELRDEGVTILLveqnARFALEIADRAYVLE--RGRVVLEGTAAELLA 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1042-1209 |
6.16e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 118.35 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1042 RPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDP---LEGAVTVDNNDLRQMNPkhLRKHIALVSQEPILF 1118
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1119 D-TSIRENIVYGLQP---GEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIARALIRNPKILLL 1194
Cdd:COG4136 89 PhLSVGENLAFALPPtigRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLL 157
|
170
....*....|....*
gi 17558664 1195 DEATSALDTESEKQV 1209
Cdd:COG4136 158 DEPFSKLDAALRAQF 172
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
397-602 |
8.62e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.75 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID-----DIPIEDfnikylRQlVGVVSQEPNLF 471
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqditHVPAEN------RH-VNTVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 -NTSIEQNIRYG--RSDVSDEDIAR----ALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK09452 99 pHMTVFENVAFGlrMQKTPAAEITPrvmeALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 545 LDEATSALDAESESIVQSALENASR--GRTTIVIAH----RLSTvrnADKIIVMKAGQVMEVGT 602
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGT 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1048-1258 |
9.60e-30 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 118.59 E-value: 9.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlRKHIALVSQEPILF-DTSIRENI 1126
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1127 VYGLQPGEYtheqietacSKANIHKFIDELPD--GYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTE 1204
Cdd:cd03299 93 AYGLKKRKV---------DKKEIERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1205 SEKQVQVALDAAAK--DRTCIVVAHRLSTI-VNAGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:cd03299 164 TKEKLREELKKIRKefGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1036-1258 |
1.29e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1036 FFRYPeRPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNP---KHLRKHIALVS 1112
Cdd:COG4608 23 LFGRT-VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1113 QEPilfdtsirenivYG-LQP----GEYTHE--QIETACSKANIHKFIDELPDgyetRVGEKGT-------QLSGGQKQR 1178
Cdd:COG4608 102 QDP------------YAsLNPrmtvGDIIAEplRIHGLASKAERRERVAELLE----LVGLRPEhadryphEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1179 IAIARALIRNPKILLLDEATSALDTESEKQVqVALDAAAKDR---TCIVVAHRLStivnagcimVVKN----------GQ 1245
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQV-LNLLEDLQDElglTYLFISHDLS---------VVRHisdrvavmylGK 235
|
250
....*....|...
gi 17558664 1246 VVEQGTHNELIAK 1258
Cdd:COG4608 236 IVEIAPRDELYAR 248
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
395-602 |
1.63e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.72 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNL-FNT 473
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 SIEQNIRYGRSDVS------DEDIARALKEANAADFiktfpeglntlvGDRGV-QMSGGQKQRIAIARALVR------NP 540
Cdd:PRK13548 92 TVEEVVAMGRAPHGlsraedDALVAAALAQVDLAHL------------AGRDYpQLSGGEQQRVQLARVLAQlwepdgPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 541 KILLLDEATSALD-AESESIVQSALENA-SRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVGT 602
Cdd:PRK13548 160 RWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
383-606 |
1.88e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.45 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEP-NLF-NTSIEQNIRYGRSD--VSDEDIARALKEA----NAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIAR 534
Cdd:PRK13650 85 MVFQNPdNQFvGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREPARL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 535 ALVRNPKILLLDEATSALDAESE----SIVQSALEnaSRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETL 606
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRD--DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
706-960 |
2.26e-29 |
|
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: 119.58 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIIN-VFSNPDRDQMkkdgHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRS 784
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDdVIPAGDLSLL----LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 785 KVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAV 864
Cdd:cd07346 77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 865 GQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGLTYGFANSIQF 944
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250
....*....|....*.
gi 17558664 945 FTYAAAFRFGLFLIFD 960
Cdd:cd07346 235 LGTALVLLYGGYLVLQ 250
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
394-606 |
2.48e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 122.26 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNL-FN 472
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 473 TSIEQNIRYGRS------DVSDEDIARALKEANAADFIKTFpeglntlvGDRGV-QMSGGQKQRIAIARALVRNPKILLL 545
Cdd:PRK09536 92 FDVRQVVEMGRTphrsrfDTWTETDRAAVERAMERTGVAQF--------ADRPVtSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 546 DEATSALDAESE-SIVQSALENASRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVG------THETL 606
Cdd:PRK09536 164 DEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGppadvlTADTL 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
383-601 |
3.11e-29 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 116.52 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTvALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfNIKYLRQLVG 462
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLF-NTSIEQNIRY-----GRSDV-SDEDIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIARA 535
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYiawlkGIPSKeVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 536 LVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVG 601
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
109-619 |
4.30e-29 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 126.82 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 109 YVYLGC---GIFAAGFLQASCFMVIcEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDkvglAF 185
Cdd:PTZ00243 1002 YVYLGIvllGTFSVPLRFFLSYEAM-RRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPM----SY 1076
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 186 QMMAQFIGGFAVAFtydwlltLIMMSLSPFMMI----CGLFLAKLLA--TAATKEAKQYA-VAGG----IAEEVLTSIRT 254
Cdd:PTZ00243 1077 LYLLQCLFSICSSI-------LVTSASQPFVLValvpCGYLYYRLMQfyNSANREIRRIKsVAKSpvftLLEEALQGSAT 1149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 255 VIAFNGQE-------------YECKRYEDAleHGKKTGIKKSFLigaGLASFFVIIYASyclafwVGTNFVYSGRLESGT 321
Cdd:PTZ00243 1150 ITAYGKAHlvmqealrrldvvYSCSYLENV--ANRWLGVRVEFL---SNIVVTVIALIG------VIGTMLRATSQEIGL 1218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 322 VLTVFFSVMMGSMALGQAGQQFATIGTALGAAASLYEVIDRIP---------EIDAYSTEGQTPSKISGRISVNKVEFT- 391
Cdd:PTZ00243 1219 VSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPhedmpeldeEVDALERRTGMAADVTGTVVIEPASPTs 1298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 392 ---YPTRA------DVK---------ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN 453
Cdd:PTZ00243 1299 aapHPVQAgslvfeGVQmryreglplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG 1378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 454 IKYLRQLVGVVSQEPNLFNTSIEQNIRyGRSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIA 533
Cdd:PTZ00243 1379 LRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 534 RALV-RNPKILLLDEATS----ALDAESESIVQSALENasrgRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIE 608
Cdd:PTZ00243 1458 RALLkKGSGFILMDEATAnidpALDRQIQATVMSAFSA----YTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
570
....*....|..
gi 17558664 609 QK-GLYHELVHA 619
Cdd:PTZ00243 1534 NRqSIFHSMVEA 1545
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1030-1255 |
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: 116.45 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmNPKHLRKHIA 1109
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDT-SIRENIVY-----GLqPGEYTHEQIETACSKANIHKFIDelpdgyeTRVGekgtQLSGGQKQRIAIAR 1183
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGL-PKSEIKEEVELLLRVLGLTDKAN-------KRAR----TLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAH------RLSTIVnagCIMVvkNGQVVEQGTHNEL 1255
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeALCDRI---AIMS--DGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1030-1258 |
4.65e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 118.30 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEP--ILFDTSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIAR 1183
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLEnkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
383-602 |
4.74e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.87 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIeDFNIKYL---RQ 459
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEPN--LFNTSIEQNIRYGRSDV--SDEDIARALKEANAA----DFIKTFPEGLntlvgdrgvqmSGGQKQRIA 531
Cdd:PRK13639 79 TVGIVFQNPDdqLFAPTVEEDVAFGPLNLglSKEEVEKRVKEALKAvgmeGFENKPPHHL-----------SGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 532 IARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIA-HRLSTV-RNADKIIVMKAGQVMEVGT 602
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
401-602 |
4.97e-29 |
|
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: 116.67 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYlRQlVGVVSQEPNLF-NTSIEQNI 479
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RN-VGFVFQHYALFrHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 RYG-----RSDVSDEDIARA-----LKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARALVRNPKILLLDEAT 549
Cdd:cd03296 96 AFGlrvkpRSERPPEAEIRAkvhelLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 550 SALDAEsesiVQSALENASR------GRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVGT 602
Cdd:cd03296 165 GALDAK----VRKELRRWLRrlhdelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGT 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
399-606 |
5.42e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 119.83 E-value: 5.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQ---PGQTV-ALVGSSGCGKSTIIQLLQRFYNPDAGQILIDD-----------IPIEdfnikylRQLVGV 463
Cdd:TIGR02142 7 KRLGDFSLDADftlPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgifLPPE-------KRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQEPNLF-NTSIEQNIRYGRSDVSDEDiaRALKEANAADFIktfpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKI 542
Cdd:TIGR02142 80 VFQEARLFpHLSVRGNLRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 543 LLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETL 606
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
383-610 |
5.98e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.96 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYP--TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPI----EDFNIKY 456
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 LRQLVGVVSQ--EPNLFNTSIEQNIRYGrsdvsDEDIARALKEANAADFIKTFPEGLNTLVGDRG-VQMSGGQKQRIAIA 533
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFG-----PKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 534 RALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIEQK 610
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1030-1250 |
6.00e-29 |
|
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: 115.67 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAVPILQglnvhVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlRKHIA 1109
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT-----FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILF-DTSIRENIVYGLQPG----EYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIARA 1184
Cdd:cd03298 74 MLFQENNLFaHLTVEQNVGLGLSPGlkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1185 LIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG 1250
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1030-1250 |
6.34e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 115.81 E-value: 6.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHlrKHIA 1109
Cdd:cd03301 1 VELENVTKRFGNVTA---LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILF-DTSIRENIVYGL----QPGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIARA 1184
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLklrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1185 LIRNPKILLLDEATSALD------TESE-KQVQVALDAaakdrTCIVVAH-RLSTIVNAGCIMVVKNGQVVEQG 1250
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRLGT-----TTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1034-1235 |
7.03e-29 |
|
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: 115.58 E-value: 7.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1034 KVFFRYPerPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDN---NDLRQMNPKHLRKHIAL 1110
Cdd:cd03292 5 NVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvSDLRGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQE-PILFDTSIRENIVYGLQPGEYTHEQIETACSKAnihkfIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIRNP 1189
Cdd:cd03292 83 VFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LELV--GLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNA 1235
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDT 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
398-602 |
7.64e-29 |
|
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: 116.00 E-value: 7.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIkYLRQLVGVVS--QEPNLF-NTS 474
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-HEIARLGIGRtfQIPRLFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIR-----YGRSDVSDEDIARALKEAN--AADFIKTFpeGL----NTLVGDrgvqMSGGQKQRIAIARALVRNPKIL 543
Cdd:cd03219 92 VLENVMvaaqaRTGSGLLLARARREEREARerAEELLERV--GLadlaDRPAGE----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 544 LLDEATSAL-DAESESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGT 602
Cdd:cd03219 166 LLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
383-627 |
7.66e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.81 E-value: 7.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRA--DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIE----DFNIKY 456
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 LRQLVGVVSQ--EPNLFNTSIEQNIRYGRSD--VSDEDiaralKEANAADFIKTFpeGLNTLVGDRG-VQMSGGQKQRIA 531
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEED-----AKQKAREMIELV--GLPEELLARSpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 532 IARALVRNPKILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHEtlie 608
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR---- 231
|
250
....*....|....*....
gi 17558664 609 qkglyhelvhaQVFADVDD 627
Cdd:PRK13634 232 -----------EIFADPDE 239
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1046-1227 |
1.02e-28 |
|
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: 115.80 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlRKHIALVSQEPILF-DTSIRE 1124
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFpHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGLqpgeyTHEQIETACSKANIHKFIDELP-DGYETRvgeKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDT 1203
Cdd:cd03300 92 NIAFGL-----RLKKLPKAEIKERVAEALDLVQlEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180
....*....|....*....|....*.
gi 17558664 1204 ESEKQVQVALDAAAKDR--TCIVVAH 1227
Cdd:cd03300 164 KLRKDMQLELKRLQKELgiTFVFVTH 189
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
390-606 |
1.05e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 116.86 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 390 FTYPT----RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVS 465
Cdd:COG4167 14 FKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 466 QEPNlfnTSIEQNIRYGRsdvsdediaralkeanaadfIKTFPEGLNT----------------LVG------DRGVQM- 522
Cdd:COG4167 94 QDPN---TSLNPRLNIGQ--------------------ILEEPLRLNTdltaeereerifatlrLVGllpehaNFYPHMl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 523 SGGQKQRIAIARALVRNPKILLLDEATSALDAESES-IVQSALENASR-GRTTIVIAHRLSTVRN-ADKIIVMKAGQVME 599
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLELQEKlGISYIYVSQHLGIVKHiSDKVLVMHQGEVVE 230
|
....*...
gi 17558664 600 VG-THETL 606
Cdd:COG4167 231 YGkTAEVF 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
383-601 |
3.29e-28 |
|
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: 113.74 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTY---PTRADVKILKGvsldaqpgQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKylRQ 459
Cdd:cd03298 1 VRLDKIRFSYgeqPMHFDLTFAQG--------EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEPNLF-NTSIEQNIRYGRS------DVSDEDIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAI 532
Cdd:cd03298 71 PVSMLFQENNLFaHLTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 533 ARALVRNPKILLLDEATSALD-AESESIVQSALE-NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVG 601
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDpALRAEMLDLVLDlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
381-617 |
3.61e-28 |
|
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: 115.34 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 381 GRISVNKVEFTYpTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDaGQILIDDIPIEDFNIKYLRQL 460
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLFNTSIEQNIR-YGRSdvSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRN 539
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 540 PKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELV 617
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
115-356 |
4.06e-28 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 115.66 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 115 GIFAA----GFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQ 190
Cdd:cd18576 44 GLFLLqavfSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 191 FIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYED 270
Cdd:cd18576 124 LIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 271 ALEHGKKTGIKKSfLIGAGLASFFV-IIYASYCLAFWVGTNFVYSGRLESGTVLT-VFFSVMMGsMALGQAGQQFATIGT 348
Cdd:cd18576 204 ALERVVKLALKRA-RIRALFSSFIIfLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIA-GSIGSLADLYGQLQK 281
|
....*...
gi 17558664 349 ALGAAASL 356
Cdd:cd18576 282 ALGASERV 289
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
383-645 |
4.22e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.22 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPN--LFNTSIEQNIRYG------RSDVSDEDIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIAR 534
Cdd:PRK13647 83 LVFQDPDdqVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 535 ALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIA-HRLSTVRN-ADKIIVMKAGQVMEVG-----THETLI 607
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17558664 608 EQKGLYHELVhAQVFADV-----DDKPKKKEAERRMSRQTSQR 645
Cdd:PRK13647 232 EQAGLRLPLV-AQIFEDLpelgqSKLPLTVKEAVQIIRKLLTK 273
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
676-1259 |
5.09e-28 |
|
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: 123.10 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 676 KRLKKELEEEGAVKANLFKILRYARP--EWIYIFFAIIAALIQG--AVMPafsLFFSQIINVFsNPDRDQMKKDGHFWAL 751
Cdd:TIGR01271 51 ERLEREWDRELASAKKNPKLLNALRRcfFWRFVFYGILLYFGEAtkAVQP---LLLGRIIASY-DPFNAPEREIAYYLAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 752 MFLVLAAVQgtSMLFQCSLFGVAAERLTMRIR--SKVYRNVLRQDATYFDmpKHSPGRITTRLATDApnikSAIDYRLG- 828
Cdd:TIGR01271 127 GLCLLFIVR--TLLLHPAIFGLHHLGMQMRIAlfSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNL----NKFDEGLAl 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 829 SIFNAIASVGGGLGIAFYygWQM----AFLVMAIFPFMAVGQA----LMMKYHGGSAtsdAKEMENAGKTAmEAIENIRT 900
Cdd:TIGR01271 199 AHFVWIAPLQVILLMGLI--WELlevnGFCGLGFLILLALFQAclgqKMMPYRDKRA---GKISERLAITS-EIIENIQS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 901 VQALTLQTKLYNIFcshldaphgGNISKAIIRgLTYGFAnSIQFFTYAAAFRFGLFLIFDKNV---LMEPENVLRVLFAI 977
Cdd:TIGR01271 273 VKAYCWEEAMEKII---------KNIRQDELK-LTRKIA-YLRYFYSSAFFFSGFFVVFLSVVpyaLIKGIILRRIFTTI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 978 SFSFGTIGFAASYFPEYIKATF-AAGLI----------------FNMLEEEPRIDGMTSSGT--YPQLSGEVKLNK---- 1034
Cdd:TIGR01271 342 SYCIVLRMTVTRQFPGAIQTWYdSLGAItkiqdflckeeyktleYNLTTTEVEMVNVTASWDegIGELFEKIKQNNkark 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1035 -------VFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVtvdnndlrqmnpKHlRKH 1107
Cdd:TIGR01271 422 qpngddgLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------KH-SGR 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILFDTSIRENIVYGLQPGEYTHEQIETACskaNIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIR 1187
Cdd:TIGR01271 489 ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKAC---QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYK 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1188 NPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKR 1259
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1032-1208 |
5.45e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 113.27 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALV 1111
Cdd:PRK10247 10 LQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQEPILFDTSIRENIVYglqPGEYTHEQIETACSKANIHKFidELPdgyETRVGEKGTQLSGGQKQRIaiarALIRN--- 1188
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIF---PWQIRNQQPDPAIFLDDLERF--ALP---DTILTKNIAELSGGEKQRI----SLIRNlqf 154
|
170 180
....*....|....*....|.
gi 17558664 1189 -PKILLLDEATSALDtESEKQ 1208
Cdd:PRK10247 155 mPKVLLLDEITSALD-ESNKH 174
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
397-606 |
6.59e-28 |
|
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: 112.91 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN-IKYLRQLVGVVSQEPNLF-NTS 474
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIRYGRSDVSDEDIARALKEAnaadfIKTFP---EGLNTLVGdrgvQMSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:cd03224 92 VEENLLLGAYARRRAKRKARLERV-----YELFPrlkERRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 552 LdaeSESIVQ---SALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:cd03224 163 L---APKIVEeifEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
405-606 |
7.12e-28 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 116.74 E-value: 7.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 405 SLDAQ---PGQTV-ALVGSSGCGKSTIIQL---LQRfynPDAGQILIDD-----------IPIEdfnikylRQLVGVVSQ 466
Cdd:COG4148 15 TLDVDftlPGRGVtALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlqdsargifLPPH-------RRRIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 467 EPNLFNT-SIEQNIRYGRSdvsdediaRALKEANAADF---IKTFpeGLNTLVgDRGV-QMSGGQKQRIAIARALVRNPK 541
Cdd:COG4148 85 EARLFPHlSVRGNLLYGRK--------RAPRAERRISFdevVELL--GIGHLL-DRRPaTLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 542 ILLLDEATSALDAESESIVQSALEN-ASRGRTTIV-IAHRLSTV-RNADKIIVMKAGQVMEVGT-HETL 606
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPlAEVL 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
326-596 |
7.95e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 120.30 E-value: 7.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 326 FFSvmmGSMALG---QAGQQFATIGTAL-------GAAASLYEVIDRIPE----IDAYSTEGQTPSKI----SGRISVNK 387
Cdd:COG4178 291 YFA---GEITLGglmQAASAFGQVQGALswfvdnyQSLAEWRATVDRLAGfeeaLEAADALPEAASRIetseDGALALED 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 388 VEFTypTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQIlidDIPiEDFNIKYLrqlvgvvSQE 467
Cdd:COG4178 368 LTLR--TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI---ARP-AGARVLFL-------PQR 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 PNLFNTSIEQNIRY--GRSDVSDEDIARALKEANAADFIktfpEGLNTlVGDRGVQMSGGQKQRIAIARALVRNPKILLL 545
Cdd:COG4178 435 PYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLA----ERLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 546 DEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQ 596
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
383-599 |
8.21e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.01 E-value: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPT------RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN--- 453
Cdd:PRK10419 4 LNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 454 IKYLRQLVGVVSQE-PNLFN------TSIEQNIRYGRSDVSDEDIARALKEANAADFIktfPEGLNTLVGdrgvQMSGGQ 526
Cdd:PRK10419 84 RKAFRRDIQMVFQDsISAVNprktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLD---DSVLDKRPP----QLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 527 KQRIAIARALVRNPKILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVME 599
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
396-626 |
8.51e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 8.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYL-RQLVGVVSQEPNLFNTS 474
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLaRRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIRYGRS-------DVSDED---IARALKEAnaadfiktfpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK11231 93 VRELVAYGRSpwlslwgRLSAEDnarVNQAMEQT-----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 545 LDEATSALD----AESESIVQsalENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIEQKGLyhelvhA 619
Cdd:PRK11231 162 LDEPTTYLDinhqVELMRLMR---ELNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPGLL------R 232
|
....*..
gi 17558664 620 QVFaDVD 626
Cdd:PRK11231 233 TVF-DVE 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
109-646 |
9.95e-28 |
|
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: 122.33 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 109 YVYLGCG--IFAAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVregtGDKVGLAF- 185
Cdd:TIGR01271 929 YIYVGTAdsVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAII----DDMLPLTLf 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 186 ---QMMAQFIGGFAVAFTydwLLTLIMMSLSPFMMICGLFLAKLLATAatKEAKQYAVAG--GIAEEVLTSIR---TVIA 257
Cdd:TIGR01271 1005 dfiQLTLIVLGAIFVVSV---LQPYIFIAAIPVAVIFIMLRAYFLRTS--QQLKQLESEArsPIFSHLITSLKglwTIRA 1079
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 258 FNGQEYeckrYEDALEHGKKTGIKKSFLIGAGLASF-------FVIIYASYCLaFWVGTNFVYSGRLesGTVLTVFFSVM 330
Cdd:TIGR01271 1080 FGRQSY----FETLFHKALNLHTANWFLYLSTLRWFqmridiiFVFFFIAVTF-IAIGTNQDGEGEV--GIILTLAMNIL 1152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 331 MgsmALGQAGQQFATIGTALGAAASLYEVIDrIPEIDAYSTEGQTPSKIS-----------------GRISVNKVEFTYp 393
Cdd:TIGR01271 1153 S---TLQWAVNSSIDVDGLMRSVSRVFKFID-LPQEEPRPSGGGGKYQLStvlvienphaqkcwpsgGQMDVQGLTAKY- 1227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDaGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNT 473
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 SIEQNIR-YGRsdVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSAL 552
Cdd:TIGR01271 1307 TFRKNLDpYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 553 DAESESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGLYHELVHAQvfadvdDKPKKK 632
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAA------DRLKLF 1458
|
570
....*....|....
gi 17558664 633 EAERRMSrqtSQRK 646
Cdd:TIGR01271 1459 PLHRRNS---SKRK 1469
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1030-1255 |
1.05e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 113.59 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDpLEGAVTVD------NNDL--RQMNP 1101
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEgrveffNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1102 KHLRKHIALVSQEPILFDTSIRENIVYGLQ-----PGEYTHEQIETACSKAnihkfidELPDGYETRVGEKGTQLSGGQK 1176
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrPKLEIDDIVESALKDA-------DLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1177 QRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAA--KDRTCIVVAHRLSTIVNAGCIMVV------KNGQVVE 1248
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFfkgnenRIGQLVE 236
|
....*..
gi 17558664 1249 QGTHNEL 1255
Cdd:PRK14258 237 FGLTKKI 243
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
107-356 |
1.06e-27 |
|
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: 114.53 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 107 LKYVYLGC-GIFAAG----FLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKV 181
Cdd:cd18573 40 LKTFALALlGVFVVGaaanFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 182 GLAFQMMAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQ 261
Cdd:cd18573 120 SDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 262 EYECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTvLTVF--FSVMMGSmALGQA 339
Cdd:cd18573 200 RKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGD-LTSFlmYAVYVGS-SVSGL 277
|
250
....*....|....*..
gi 17558664 340 GQQFATIGTALGAAASL 356
Cdd:cd18573 278 SSFYSELMKGLGASSRL 294
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
390-596 |
1.29e-27 |
|
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: 112.53 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 390 FTYPTRADVKI--LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDD----IPI---EDFNIKYLRQ- 459
Cdd:COG4778 14 FTLHLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLaqaSPREILALRRr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQ---------------EPnLfntsIEQNIrygrsdvsDEDIARAlkeaNAADFIKTF--PEGL-----NTLvgd 517
Cdd:COG4778 94 TIGYVSQflrviprvsaldvvaEP-L----LERGV--------DREEARA----RARELLARLnlPERLwdlppATF--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 518 rgvqmSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIV-IAHRLSTV-RNADKIIVMKAG 595
Cdd:COG4778 154 -----SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVReAVADRVVDVTPF 228
|
.
gi 17558664 596 Q 596
Cdd:COG4778 229 S 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1038-1255 |
1.37e-27 |
|
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: 112.82 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1038 RYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlRKHIALVSQEPIL 1117
Cdd:cd03296 11 RFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1118 F-DTSIRENIVYGLQPgeythEQIETACSKANIHKFIDELP-----DGYETRVGekgTQLSGGQKQRIAIARALIRNPKI 1191
Cdd:cd03296 86 FrHMTVFDNVAFGLRV-----KPRSERPPEAEIRAKVHELLklvqlDWLADRYP---AQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1192 LLLDEATSALDTESEKQVQVALdAAAKDR---TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWL-RRLHDElhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1032-1247 |
2.14e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.44 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFfryperPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH-IAL 1110
Cdd:cd03216 6 ITKRF------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQepilfdtsirenivyglqpgeytheqietacskanihkfidelpdgyetrvgekgtqLSGGQKQRIAIARALIRNPK 1190
Cdd:cd03216 80 VYQ---------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1191 ILLLDEATSAL-DTESEKQVQVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVV 1247
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
411-609 |
2.14e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.20 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 411 GQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiEDFNIKYLRQL-VGVVSQEPNLF-NTSIEQNIRYGRS--DV 486
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFpHMSLGENVGYGLKmlGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 487 SDEDIARALKEANAadfiktfpegLNTLVG--DRGV-QMSGGQKQRIAIARALVRNPKILLLDEATSALDAE-----SES 558
Cdd:PRK11432 109 PKEERKQRVKEALE----------LVDLAGfeDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANlrrsmREK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 559 I--VQSALenasrGRTTIVIAHRLS---TVrnADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:PRK11432 179 IreLQQQF-----NITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1045-1255 |
2.15e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.31 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYD-----PLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFD 1119
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 T-SIRENIVYGLQPGEYT------HEQIETACSKAnihkfidELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKIL 1192
Cdd:PRK14247 96 NlSIFENVALGLKLNRLVkskkelQERVRWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1193 LLDEATSALDTESEKQVQVALDAAAKDRTCIVVAH------RLSTIVnagciMVVKNGQVVEQGTHNEL 1255
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRISDYV-----AFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
383-612 |
2.33e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDA---GQILIDDIPIEDFNIKYLRQ 459
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEP-NLF-NTSIEQNIRYGRSD--VSDED----IARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIA 531
Cdd:PRK13640 85 KVGIVFQNPdNQFvGATVGDDVAFGLENraVPRPEmikiVRDVLADVGMLDYIDSEPANL-----------SGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 532 IARALVRNPKILLLDEATSALDAESE----SIVQSALENasRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGT----- 602
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveif 231
|
250
....*....|.
gi 17558664 603 -HETLIEQKGL 612
Cdd:PRK13640 232 sKVEMLKEIGL 242
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1046-1250 |
5.47e-27 |
|
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: 109.56 E-value: 5.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLL--ERLYDPLEGAVTVDNndlRQMNPKHLRKHIALVSQEPILFDT-SI 1122
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1123 RENIVYglqpgeytheqieTACSKanihkfidelpdgyetrvgekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:cd03213 100 RETLMF-------------AAKLR-----------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1203 TESEKQVQVALDAAAKD-RTCIVVAHRLSTIVNAGC--IMVVKNGQVVEQG 1250
Cdd:cd03213 144 SSSALQVMSLLRRLADTgRTIICSIHQPSSEIFELFdkLLLLSQGRVIYFG 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
383-599 |
6.95e-27 |
|
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: 111.44 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPT------RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN--- 453
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 454 IKYLRQLVGVVSQE-PNLFN--TSIEQNIRYGRSDVSDEDIARalKEANAADFIKTFpeGLNTLVGDR-GVQMSGGQKQR 529
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNprMTVRQIIGEPLRHLTSLDESE--QKARIAELLDMV--GLRSEDADKlPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 530 IAIARALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVME 599
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
110-353 |
1.45e-26 |
|
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: 111.10 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 110 VYLGCGIFAAGFLQASCFMV---ICEKLSNRF----RRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVG 182
Cdd:cd07346 39 LWIALLLLLLALLRALLSYLrryLAARLGQRVvfdlRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 183 LAFQMMAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQE 262
Cdd:cd07346 119 QLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 263 YECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQ 342
Cdd:cd07346 199 REIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANL 278
|
250
....*....|.
gi 17558664 343 FATIGTALGAA 353
Cdd:cd07346 279 YNQLQQALASL 289
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
376-602 |
2.41e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.48 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 376 PSKISGRISVN----KVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIED 451
Cdd:PRK13631 13 PNPLSDDIILRvknlYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 452 F----------------NIKYLRQLVGVVSQEP--NLFNTSIEQNIRYGrsdvsdeDIARALKEANAADFIKTFPE--GL 511
Cdd:PRK13631 93 KknnhelitnpyskkikNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFG-------PVALGVKKSEAKKLAKFYLNkmGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 512 NTLVGDRG-VQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESES-IVQSALENASRGRTTIVIAHRLSTVRN-ADK 588
Cdd:PRK13631 166 DDSYLERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADE 245
|
250
....*....|....
gi 17558664 589 IIVMKAGQVMEVGT 602
Cdd:PRK13631 246 VIVMDKGKILKTGT 259
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
398-609 |
2.71e-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: 115.17 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKS----TIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL----VGVVSQEP- 468
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnrIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 469 ---N-LFntSIEQNIR------YGRSDVSDEDIARALKE----ANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIAR 534
Cdd:COG4172 103 tslNpLH--TIGKQIAevlrlhRGLSGAAARARALELLErvgiPDPERRLDAYPH-----------QLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 535 ALVRNPKILLLDEATSALDAesesIVQSA-LE-----NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLI 607
Cdd:COG4172 170 ALANEPDLLIADEPTTALDV----TVQAQiLDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELF 245
|
..
gi 17558664 608 EQ 609
Cdd:COG4172 246 AA 247
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1048-1229 |
2.72e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.49 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGA-----VTVDNNDL--RQMNPKHLRKHIALVSQEPILFDT 1120
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYGLQPGEYT---HEQIETACSKANIHkfiDELPDgyetRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEA 1197
Cdd:PRK14243 106 SIYDNIAYGARINGYKgdmDELVERSLRQAALW---DEVKD----KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 1198 TSALDTESEKQVQVALDAAAKDRTCIVVAHRL 1229
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
706-1001 |
3.53e-26 |
|
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: 109.96 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAvMPafsLFFSQIINVFSNPDRDQMKKDghfWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSK 785
Cdd:cd18557 2 LLFLLISSAAQLL-LP---YLIGRLIDTIIKGGDLDVLNE---LALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 786 VYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVG 865
Cdd:cd18557 75 LFSSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 866 qalmMKYHGGSATSDAKEME----NAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGLTYGFANS 941
Cdd:cd18557 153 ----SKIYGRYIRKLSKEVQdalaKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 942 IQFFTYAAAFRFGLFLIFDKNvlMEPENVLR-VLFAIS--FSFGTIGfaaSYFPEYIKATFAA 1001
Cdd:cd18557 229 LIYLSLLLVLWYGGYLVLSGQ--LTVGELTSfILYTIMvaSSVGGLS---SLLADIMKALGAS 286
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
398-602 |
5.12e-26 |
|
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: 108.59 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIED--------------F-NIKYLRQL-- 460
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphriarlgiartFqNPRLFPELtv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 -----VGVVSQEPNLFNTSIEQNIRYGRSDVSDEDIARALkeanaADFIktfpeGLNTLVGDRGVQMSGGQKQRIAIARA 535
Cdd:COG0411 97 lenvlVAAHARLGRGLLAALLRLPRARREEREARERAEEL-----LERV-----GLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 536 LVRNPKILLLDEATSAL-DAESESIVQSALE-NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGT 602
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1030-1250 |
5.15e-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: 107.28 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAvpiLQGLNVHVKPGQTlALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnPKHLRKHIA 1109
Cdd:cd03264 1 LQLENLTKRYGKKRA---LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDT-SIRENIVY-----GLQPGEyTHEQIETACSKANihkfideLPDGYETRVGekgtQLSGGQKQRIAIAR 1183
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKE-VKARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTI-VNAGCIMVVKNGQVVEQG 1250
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1044-1256 |
6.24e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.87 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1044 AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLR--QMNPKHLRKHIALVSQEPILFD-- 1119
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPhl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIrENIVYGlqPgeythEQIETAcSKANIHKFIDELPD--GYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEA 1197
Cdd:PRK09493 93 TAL-ENVMFG--P-----LRVRGA-SKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1198 TSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVNAGC-IMVVKNGQVVEQGTHNELI 1256
Cdd:PRK09493 164 TSALDPELRHEVlKVMQDLAEEGMTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
396-601 |
7.56e-26 |
|
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: 106.60 E-value: 7.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNikylRQLVGVVSQEPNLFN--T 473
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPkmK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 SIEQNIRYGR-SDVSDEDIARalkeaNAADFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSAL 552
Cdd:cd03269 87 VIDQLVYLAQlKGLKKEEARR-----RIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 553 DAESESIVQSAL-ENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVG 601
Cdd:cd03269 160 DPVNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1062-1257 |
9.42e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 110.58 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1062 ALVGPSGCGKSTVISL---LERlydPLEGAVTVDNNDL-----RQMNPKHLRkHIALVSQEPILFDT-SIRENIVYGLQ- 1131
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLqdsarGIFLPPHRR-RIGYVFQEARLFPHlSVRGNLLYGRKr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1132 -PGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQ 1210
Cdd:COG4148 105 aPRAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1211 VALDAAAKD-RTCIV-VAH------RLstivnAGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:COG4148 174 PYLERLRDElDIPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
389-612 |
1.27e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.97 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 389 EFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEP 468
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 469 N--LFNTSIEQNIRYGRSD--VSDEDIARALKEAnaadfIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK13652 88 DdqIFSPTVEQDIAFGPINlgLDEETVAHRVSSA-----LHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 545 LDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQKGL 612
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
400-1246 |
1.29e-25 |
|
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: 115.39 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILiddipiEDFNIKYlrqlvgvVSQEPNLFNTSIEQNI 479
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK------HSGRISF-------SPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 RYGRSdvSDEDIARA-LKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESE- 557
Cdd:TIGR01271 508 IFGLS--YDEYRYTSvIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEk 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 558 SIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQK--------------------------- 610
Cdd:TIGR01271 586 EIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfsslllgleafdnfsaerrnsilte 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 611 -------------GLYHELVHAQV-------------------------FADVDDKPKKKEA-----------ERRMS-- 639
Cdd:TIGR01271 666 tlrrvsidgdstvFSGPETIKQSFkqpppefaekrkqsiilnpiasarkFSFVQMGPQKAQAttiedavrepsERKFSlv 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 640 ---------------------RQTSQRKGSVNFKTQESQVDEKPGAPPAPEAAEKEI--------------KRLKK---- 680
Cdd:TIGR01271 746 pedeqgeeslprgnqyhhglqHQAQRRQSVLQLMTHSNRGENRREQLQTSFRKKSSItqqnelaseldiysRRLSKdsvy 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 681 ----ELEEEGAVKA------NLFKI------LRYARPEWIYIFFAIIAALIQGAVMPAFSLFFSQIINVFSNPDRDqmkK 744
Cdd:TIGR01271 826 eiseEINEEDLKECfadereNVFETttwntyLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNYV---D 902
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 745 DGHFWALMFLVLAAV--QGTSMLFQCSLF-GVAAERLTM-----------------RIRSKVYRNVLRQDATYFDMPKhs 804
Cdd:TIGR01271 903 QQHANASSPDVQKPViiTPTSAYYIFYIYvGTADSVLALgffrglplvhtlltvskRLHEQMLHSVLQAPMAVLNTMK-- 980
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 805 PGRITTRLATDAPNIKSAIDYrlgSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVgqALMMKYHGGSATSDAKEM 884
Cdd:TIGR01271 981 AGRILNRFTKDMAIIDDMLPL---TLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVI--FIMLRAYFLRTSQQLKQL 1055
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 885 ENAGKTAM-----EAIENIRTVQALTLQTKLYNIFCSHLDApHGGN--ISKAIIRGLTYGFANSIQFFTYAAAF------ 951
Cdd:TIGR01271 1056 ESEARSPIfshliTSLKGLWTIRAFGRQSYFETLFHKALNL-HTANwfLYLSTLRWFQMRIDIIFVFFFIAVTFiaigtn 1134
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 952 -----RFGLFLIFDKNVLMEPE-------NVLRVLFAISFSFGTIGFAASYfPEYIKATFAAGLIFNMLEEEPRIDGMTS 1019
Cdd:TIGR01271 1135 qdgegEVGIILTLAMNILSTLQwavnssiDVDGLMRSVSRVFKFIDLPQEE-PRPSGGGGKYQLSTVLVIENPHAQKCWP 1213
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1020 SGtypqlsGEVKLNKVFFRYPErPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPlEGAVTVDNNDLRQM 1099
Cdd:TIGR01271 1214 SG------GQMDVQGLTAKYTE-AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSV 1285
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1100 NPKHLRKHIALVSQEPILFDTSIRENivygLQPGE-YTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQR 1178
Cdd:TIGR01271 1286 TLQTWRKAFGVIPQKVFIFSGTFRKN----LDPYEqWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQL 1361
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1179 IAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQV 1246
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1047-1255 |
1.30e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 107.44 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNN------DLRQMNPKHLRKHIALVSQEPILF-D 1119
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIRENIVY-----GLQPGEYTHEQIETACSKANIHKFIDElpdgyetRVGEKGTQLSGGQKQRIAIARALIRNPKILLL 1194
Cdd:PRK14246 105 LSIYDNIAYplkshGIKEKREIKKIVEECLRKVGLWKEVYD-------RLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1195 DEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1046-1249 |
1.45e-25 |
|
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: 107.58 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNP---KHLRKHIALVSQE-PILFD-- 1119
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrRAFRRDVQLVFQDsPSAVNpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIRENIVyglQPGEYtHEQIETACSKANIHKFID--ELPDGYETRVGEkgtQLSGGQKQRIAIARALIRNPKILLLDEA 1197
Cdd:TIGR02769 105 MTVRQIIG---EPLRH-LTSLDESEQKARIAELLDmvGLRSEDADKLPR---QLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 1198 TSALDTESEKQVQVALDA--AAKDRTCIVVAHRLStIVNAGC--IMVVKNGQVVEQ 1249
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLR-LVQSFCqrVAVMDKGQIVEE 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
383-597 |
2.70e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 106.69 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRAdvkILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfnikyLRQLVG 462
Cdd:PRK11247 13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFN-TSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIARALVRNPK 541
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 542 ILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLS-TVRNADKIIVMKAGQV 597
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
383-612 |
2.90e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.00 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN-IKYLRQLV 461
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEP--NLFNTSIEQNIRYGRSDVS------DEDIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIA 533
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLClppieiRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 534 RALVRNPKILLLDEATSALDAES-ESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKGL 612
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
397-605 |
2.91e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-VGVVSQEPNLFNT-S 474
Cdd:COG3845 17 GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHFMLVPNlT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIRYGRSDVSDE--DIARALKEAnaADFIKTFpeGL----NTLVGDrgvqMSGGQKQRIAIARALVRNPKILLLDEA 548
Cdd:COG3845 97 VAENIVLGLEPTKGGrlDRKAARARI--RELSERY--GLdvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 549 TSAL-DAESESIVQsALEN-ASRGRTTIVIAHRLSTVR-NADKIIVMKAGQVmeVGTHET 605
Cdd:COG3845 169 TAVLtPQEADELFE-ILRRlAAEGKSIIFITHKLREVMaIADRVTVLRRGKV--VGTVDT 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1057-1271 |
3.12e-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: 109.05 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1057 PGQTL-ALVGPSGCGKSTVISLLERLYDPLEGAVTVDN---NDLRQ--MNPKHLRKhIALVSQEPILF-DTSIRENIVYG 1129
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgiFLPPEKRR-IGYVFQEARLFpHLSVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1130 LQ--PGEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEK 1207
Cdd:TIGR02142 100 MKraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1208 QVQVALD--AAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQKQSS 1271
Cdd:TIGR02142 169 EILPYLErlHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGS 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1047-1227 |
3.48e-25 |
|
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: 105.43 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKST---VISLLERLYDPLEGAVTVDNndlRQMNPKHLRKHIALVSQEPILFDT-SI 1122
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1123 RENIVYGLQpgeytheQIETACSKANIHKFIDE---LPDGYETRVG-EKGTQLSGGQKQRIAIARALIRNPKILLLDEAT 1198
Cdd:cd03234 99 RETLTYTAI-------LRLPRKSSDAIRKKRVEdvlLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 17558664 1199 SALDTESEKQVQVAL-DAAAKDRTCIVVAH 1227
Cdd:cd03234 172 SGLDSFTALNLVSTLsQLARRNRIVILTIH 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1047-1257 |
3.76e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.99 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDN---NDLRQMNP-----KHLRKHIALVSQEPILF 1118
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitiDTARSLSQqkgliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1119 -DTSIRENIVYGlqPGEYTHEQIETACSKANihkfidELPdgyeTRVGEKGTQ------LSGGQKQRIAIARALIRNPKI 1191
Cdd:PRK11264 98 pHRTVLENIIEG--PVIVKGEPKEEATARAR------ELL----AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1192 LLLDEATSALDTESEKQVQVALDAAAKD-RTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1044-1257 |
5.62e-25 |
|
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: 105.06 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1044 AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL-RKHIALVSQEPILFDT-S 1121
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1122 IRENivygLQPGEYTHEqietacSKANIHKFIDELpdgYET------RVGEKGTQLSGGQKQRIAIARALIRNPKILLLD 1195
Cdd:COG0410 95 VEEN----LLLGAYARR------DRAEVRADLERV---YELfprlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1196 EAtsaldteSE-------KQVQVALDAAAKDRTCIVV----AHRLSTIVNAGCIMVvkNGQVVEQGTHNELIA 1257
Cdd:COG0410 162 EP-------SLglaplivEEIFEIIRRLNREGVTILLveqnARFALEIADRAYVLE--RGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
397-621 |
6.12e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.86 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIeDFNIK---YLRQLVGVVSQEPN--LF 471
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVFQDPEqqIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 NTSIEQNIRYGRSD--VSDEDIARALKEAnaadfiktfpeglNTLVGDRGVQ------MSGGQKQRIAIARALVRNPKIL 543
Cdd:PRK13638 92 YTDIDSDIAFSLRNlgVPEAEITRRVDEA-------------LTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 544 LLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVM------EVGTHETLIEQKGLYHE 615
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILthgapgEVFACTEAMEQAGLTQP 238
|
....*....
gi 17558664 616 L---VHAQV 621
Cdd:PRK13638 239 WlvkLHTQL 247
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
382-554 |
6.39e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.71 E-value: 6.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 382 RISVNKVEFTYP-TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIE----Dfniky 456
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 lRqlvGVVSQEPNLFN-TSIEQNIRYG---RSdvsdedIARALKEANAADFIKtfpeglntLVGDRGV------QMSGGQ 526
Cdd:COG4525 78 -R---GVVFQKDALLPwLNVLDNVAFGlrlRG------VPKAERRARAEELLA--------LVGLADFarrriwQLSGGM 139
|
170 180
....*....|....*....|....*...
gi 17558664 527 KQRIAIARALVRNPKILLLDEATSALDA 554
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1046-1251 |
7.81e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPIL-FDTSIRE 1124
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGLQPGeyTHEQIETacskanihkfiDELPDGYETRVGEKG------TQLSGGQKQRIAIARALIR------NPKIL 1192
Cdd:PRK13548 96 VVAMGRAPH--GLSRAED-----------DALVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1193 LLDEATSALDTeseKQVQVALDAA---AKDR--TCIVVAHRLstivN-----AGCIMVVKNGQVVEQGT 1251
Cdd:PRK13548 163 LLDEPTSALDL---AHQHHVLRLArqlAHERglAVIVVLHDL----NlaaryADRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
383-602 |
8.94e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.70 E-value: 8.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYP--TRAdvkiLKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIeDFNIK---YL 457
Cdd:PRK13636 6 LKVEELNYNYSdgTHA----LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 458 RQLVGVVSQEPN--LFNTSIEQNIRYGRSDVS--DEDIARALKEANAadfiKTfpeGLNTLVGDRGVQMSGGQKQRIAIA 533
Cdd:PRK13636 81 RESVGMVFQDPDnqLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALK----RT---GIEHLKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 534 RALVRNPKILLLDEATSALDAESES-IVQSALENASRGRTTIVIA-HRLSTVR-NADKIIVMKAGQVMEVGT 602
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSeIMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
387-621 |
9.49e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.61 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 387 KVEFtyptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYN--PDA---GQILIDDIPIEDFNIKYLRQLV 461
Cdd:PRK14247 10 KVSF-----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEPN-LFNTSIEQNIRYG---------RSDVsDEDIARALKEANAADFIKtfpEGLNTLVGdrgvQMSGGQKQRIA 531
Cdd:PRK14247 85 QMVFQIPNpIPNLSIFENVALGlklnrlvksKKEL-QERVRWALEKAQLWDEVK---DRLDAPAG----KLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 532 IARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAH-RLSTVRNADKIIVMKAGQVMEVG-THETLIEQ 609
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGpTREVFTNP 236
|
250
....*....|..
gi 17558664 610 KglyHELVHAQV 621
Cdd:PRK14247 237 R---HELTEKYV 245
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
397-608 |
9.70e-25 |
|
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: 104.29 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-VGVVSQEPNLF-NTS 474
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFpSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIR---YGRSDVSD--EDIARALKeanaadfikTFPEgLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEAT 549
Cdd:COG0410 95 VEENLLlgaYARRDRAEvrADLERVYE---------LFPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 550 SALdaeSESIVQ---SALENASRGRTTIVI----AHRLSTVrnADKIIVMKAGQVMEVGTHETLIE 608
Cdd:COG0410 165 LGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
380-602 |
1.03e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.86 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 380 SGRISVNKVEFTYPTRA--DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPI-----EDF 452
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 453 NIKYLRQLVGVVSQEP--NLFNTSIEQNIRYGRSDVSdediaralkeANAADFIKTFPEGLNTL------VGDRGVQMSG 524
Cdd:PRK13645 84 EVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG----------ENKQEAYKKVPELLKLVqlpedyVKRSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 525 GQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVG 601
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErlNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
|
.
gi 17558664 602 T 602
Cdd:PRK13645 234 S 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1047-1250 |
1.34e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.79 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYdPLEGAVTVDNNDLRQMNPKHL---RKHIALVSQEPilfDTSI- 1122
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1123 -RENIVYGLQPGEYTHEQIETACSK-ANIHKFIDELPDGYETRvGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSA 1200
Cdd:PRK15134 377 pRLNVLQIIEEGLRVHQPTLSAAQReQQVIAVMEEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1201 LDTESEKQVQVALDAAAKDR--TCIVVAHRLStIVNAGC--IMVVKNGQVVEQG 1250
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHqlAYLFISHDLH-VVRALChqVIVLRQGEVVEQG 508
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
396-604 |
1.35e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.64 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSI 475
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNIRYG---RSDVSDEDIaralkeanAADFIKTFPEGLNTLvgDRGV-QMSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:PRK10247 98 YDNLIFPwqiRNQQPDPAI--------FLDDLERFALPDTIL--TKNIaELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 552 LDAESESIVQSALENASRGRTTIVI--AHRLSTVRNADKIIVMKA-GQVMEVGTHE 604
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITLQPhAGEMQEARYE 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
383-599 |
1.42e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.17 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPN--LFNTSIEQNIRYGRSD--VSDEDIARALKEA----NAADFIKTFPeglntlvgdrgVQMSGGQKQRIAIAR 534
Cdd:PRK13642 85 MVFQNPDnqFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 535 ALVRNPKILLLDEATSALDAESESIVQSALENASRGR--TTIVIAHRLSTVRNADKIIVMKAGQVME 599
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
401-588 |
1.56e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.48 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYN--PDA---GQILIDDIPIEDFNIK--YLRQLVGVVSQEPNLFNT 473
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 SIEQNIRYG------RSDVsDEDIARALKEANAADFIKtfpEGLNtlvgDRGVQMSGGQKQRIAIARALVRNPKILLLDE 547
Cdd:PRK14243 106 SIYDNIAYGaringyKGDM-DELVERSLRQAALWDEVK---DKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17558664 548 ATSALDAESESIVQSALENASRGRTTIVIAHRLSTV-RNADK 588
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDM 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1047-1264 |
1.62e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNN--DLRQ-MNPKH---LRKHIALVSQE----PI 1116
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKtPSDKAireLRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 LfdtSIRENI------VYGLQPGEyTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIARALIRNPK 1190
Cdd:PRK11124 97 L---TVQQNLieapcrVLGLSKDQ-ALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 1191 ILLLDEATSALDTESEKQ-VQVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIAKRGAYFA 1264
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQiVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASCFTQPQTEAFK 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1030-1250 |
1.86e-24 |
|
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: 102.68 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRqmNPKHLRKHIA 1109
Cdd:cd03268 1 LKTNDLTKTYGKKRV---LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDT-SIRENI-VYGLQPGeytheqietaCSKANIHKFIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIR 1187
Cdd:cd03268 76 ALIEAPGFYPNlTARENLrLLARLLG----------IRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1188 NPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG 1250
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELrELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1032-1205 |
1.96e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVdnndlrqmnPKHLRkhIALV 1111
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQEPILFDT-SIRENIVYGLQP-----GEYTHEQIETACSKANIHKF------IDELpDGY--ETRVGE--KG------- 1168
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAElraleAELEELEAKLAEPDEDLERLaelqeeFEAL-GGWeaEARAEEilSGlgfpeed 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17558664 1169 -----TQLSGGQKQRIAIARALIRNPKILLLDEATSALDTES 1205
Cdd:COG0488 146 ldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1030-1257 |
1.98e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEP--ILFDTSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIAR 1183
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMEnqgiPREEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALDaAAKDR---TCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1047-1227 |
2.02e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.77 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYD-----PLEGAVTVDNNDL--RQMNPKHLRKHIALVSQEPILF- 1118
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1119 DTSIRENIVYGLQ------PGEYTHEQIETACSKANIHkfiDELPDgyetRVGEKGTQLSGGQKQRIAIARALIRNPKIL 1192
Cdd:PRK14267 99 HLTIYDNVAIGVKlnglvkSKKELDERVEWALKKAALW---DEVKD----RLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 17558664 1193 LLDEATSALDTESEKQVQVALDAAAKDRTCIVVAH 1227
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1040-1250 |
2.13e-24 |
|
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: 102.83 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1040 PERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmNPKHLRKHIALVSQEPILFD 1119
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 -TSIRENIVY-----GLQPGEYtHEQIETACSKANIHKFIDElpdgyetRVGEkgtqLSGGQKQRIAIARALIRNPKILL 1193
Cdd:cd03266 92 rLTARENLEYfaglyGLKGDEL-TARLEELADRLGMEELLDR-------RVGG----FSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1194 LDEATSALDTESEKQVQVALDAAAKDRTCIVVA-HRLSTiVNAGC--IMVVKNGQVVEQG 1250
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQE-VERLCdrVVVLHRGRVVYEG 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1046-1228 |
2.19e-24 |
|
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: 101.08 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTvdnndlrqmnpKHLRKHIALVSQEPILFDTSIREN 1125
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLLFLPQRPYLPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1126 IVYGLQpgeytheqietacskanihkfidelpdgyetrvgekgTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTES 1205
Cdd:cd03223 84 LIYPWD-------------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....
gi 17558664 1206 EKQV-QVALDAAAkdrTCIVVAHR 1228
Cdd:cd03223 127 EDRLyQLLKELGI---TVISVGHR 147
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
383-595 |
2.21e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 102.79 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQIL----IDDIPIEDFNIKYLR 458
Cdd:cd03290 1 VQVTNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 459 QLVGVVSQEPNLFNTSIEQNIRYGrSDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVR 538
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 539 NPKILLLDEATSALDAE-SESIVQSALENASRG--RTTIVIAHRLSTVRNADKIIVMKAG 595
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
395-606 |
2.29e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 103.63 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQilidDIPI--EDF---NIKYLRQLVGVVS---Q 466
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN----DVRLfgERRggeDVWELRKRIGLVSpalQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 467 EPNLFNTSIEQNIRYGRSD-------VSDEDIARA---LKEANAADFI-KTFPeglntlvgdrgvQMSGGQKQRIAIARA 535
Cdd:COG1119 89 LRFPRDETVLDVVLSGFFDsiglyrePTDEQRERArelLELLGLAHLAdRPFG------------TLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 536 LVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIV-IAHRLSTVRNA-DKIIVMKAGQVMEVG-THETL 606
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGpKEEVL 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
383-602 |
2.58e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.44 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYP--TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPI----EDFNIKY 456
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 LRQLVGVVSQ--EPNLFNTSIEQNIRYGRSD--VSDEDIARALKEANAADFIKtfpeglNTLVGDRGVQMSGGQKQRIAI 532
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 533 ARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIV-IAHRLSTVRN-ADKIIVMKAGQVMEVGT 602
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
404-608 |
2.76e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.46 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 404 VSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNiKYLRQlVGVVSQEPNLF-NTSIEQNIRYG 482
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-INMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 483 -------RSDVSDEdIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARALVRNPKILLLDEATSALDAE 555
Cdd:PRK11607 116 lkqdklpKAEIASR-VNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 556 SESIVQ----SALENAsrGRTTIVIAH-RLSTVRNADKIIVMKAGQVMEVGTHETLIE 608
Cdd:PRK11607 184 LRDRMQlevvDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1255 |
3.65e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPAVpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEP--ILFDTSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPDGyetrvgekgtqLSGGQKQRIAIAR 1183
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLEnhavPYDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQ--VALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLdlVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
393-601 |
3.72e-24 |
|
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: 102.06 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 393 PTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDI-----PIEdfnikyLRQLVGVVSQE 467
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkePAE------ARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 PNLFN-TSIEQNIRYgrsdvsdedIAR--ALKEANAADFIKTFPE--GLNTLVGDRGVQMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03266 87 TGLYDrLTARENLEY---------FAGlyGLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 543 LLLDEATSALDAESESIVQSALENASRGRTTIVIA-HRLSTV-RNADKIIVMKAGQVMEVG 601
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1030-1256 |
3.87e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.85 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILfdTS---IRENIVYGLQP---GEYT---HEQIETACSKANI----HKFIDELpdgyetrvgekgtqlSGGQK 1176
Cdd:COG4604 79 ILRQENHI--NSrltVRELVAFGRFPyskGRLTaedREIIDEAIAYLDLedlaDRYLDEL---------------SGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1177 QRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKD--RTCIVVAHRLstivN-AGC----IMVVKNGQVVEQ 1249
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHDI----NfASCyadhIVAMKDGRVVAQ 217
|
....*..
gi 17558664 1250 GTHNELI 1256
Cdd:COG4604 218 GTPEEII 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1029-1256 |
4.47e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 106.27 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1029 EVK-LNKVFFRYPERPAVPILQGLN------------------VHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAV 1089
Cdd:PRK10070 6 EIKnLYKIFGEHPQRAFKYIEQGLSkeqilektglslgvkdasLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1090 TVDNNDLRQMNPKHLR----KHIALVSQE-PILFDTSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPDgy 1160
Cdd:PRK10070 86 LIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMTVLDNTAFGMElagiNAEERREKALDALRQVGLENYAHSYPD-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1161 etrvgekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALD--TESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAG-C 1237
Cdd:PRK10070 164 ---------ELSGGMRQRVGLARALAINPDILLMDEAFSALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGdR 234
|
250
....*....|....*....
gi 17558664 1238 IMVVKNGQVVEQGTHNELI 1256
Cdd:PRK10070 235 IAIMQNGEVVQVGTPDEIL 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1029-1264 |
5.89e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1029 EVKLNKVFFRYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNN--DLRQ-MNPKH-- 1103
Cdd:COG4161 2 SIQLKNINCFYGSHQA---LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQkPSEKAir 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 -LRKHIALVSQE----PILfdtSIRENI------VYGLqPGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLS 1172
Cdd:COG4161 79 lLRQKVGMVFQQynlwPHL---TVMENLieapckVLGL-SKEQAREKAMKLLARLRLTDKADRFP-----------LHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1173 GGQKQRIAIARALIRNPKILLLDEATSALDTESEKQ-VQVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG 1250
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQvVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQG 223
|
250
....*....|....
gi 17558664 1251 THNELIAKRGAYFA 1264
Cdd:COG4161 224 DASHFTQPQTEAFA 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1048-1251 |
6.10e-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: 102.13 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPkHLRKH--IALVSQEPILFDT-SIRE 1124
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-HEIARlgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGLQPGeyTHEQIETACSKANIHKFIDE---------LPDGYETRVGEkgtqLSGGQKQRIAIARALIRNPKILLLD 1195
Cdd:cd03219 95 NVMVAAQAR--TGSGLLLARARREEREARERaeellervgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1196 EATSAL-DTESEKQVQVALDAAAKDRTCIVVAHRLStIVNAGC--IMVVKNGQVVEQGT 1251
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMD-VVMSLAdrVTVLDQGRVIAEGT 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
401-602 |
6.18e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.24 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDF-NIKYLRQLVGVVSQEPN--LFNTSIEQ 477
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAGMVFQNPDnqIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 478 NIRYGRSD--VSDEDIAR----ALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:PRK13633 106 DVAFGPENlgIPPEEIRErvdeSLKKVGMYEYRRHAPHLL-----------SGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 552 LDAESESIVQSALE--NASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGT 602
Cdd:PRK13633 175 LDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1036-1258 |
6.19e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 104.28 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1036 FFRYPERpaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNP---KHLRKHIALVS 1112
Cdd:PRK11308 21 LFKPERL--VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1113 QEPilfdtsirenivYG-LQP----GEYTHE--QIETACSKANIHKFIDELpdgyETRVGEKGTQ-------LSGGQKQR 1178
Cdd:PRK11308 99 QNP------------YGsLNPrkkvGQILEEplLINTSLSAAERREKALAM----MAKVGLRPEHydryphmFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1179 IAIARALIRNPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIV-VAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVlNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
...
gi 17558664 1256 IAK 1258
Cdd:PRK11308 243 FNN 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
397-601 |
9.55e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 9.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfnIKYLRQLVGVVSQEPNLF-NTSI 475
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMVFQSYALYpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNIRYGR--SDVSDEDIARALKeaNAADFIKtfpegLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALD 553
Cdd:PRK11000 93 AENMSFGLklAGAKKEEINQRVN--QVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 554 AESEsiVQSALEnASR-----GRTTIVIAH-RLSTVRNADKIIVMKAGQVMEVG 601
Cdd:PRK11000 166 AALR--VQMRIE-ISRlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1042-1257 |
1.00e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 102.46 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1042 RPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMN---PKHLRKHIALVSQEPI-L 1117
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIsA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1118 FD--TSIRENIVYGLQpgeytHEqieTACSKANIHKFIDELPDGYETRVG---EKGTQLSGGQKQRIAIARALIRNPKIL 1192
Cdd:PRK10419 102 VNprKTVREIIREPLR-----HL---LSLDKAERLARASEMLRAVDLDDSvldKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1193 LLDEATSALDTESEKQVqVALDAAAKDRT---CIVVAHRLStIVNAGC--IMVVKNGQVVEQGTHNELIA 1257
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGV-IRLLKKLQQQFgtaCLFITHDLR-LVERFCqrVMVMDNGQIVETQPVGDKLT 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1047-1202 |
1.10e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.03 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlRKHIALVSQEPILF-DTSIREN 1125
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1126 IVYGLQ----PGEYTHEQIETACskanihkfidELPD--GYETRVGEkgtQLSGGQKQRIAIARALIRNPKILLLDEATS 1199
Cdd:PRK11432 99 VGYGLKmlgvPKEERKQRVKEAL----------ELVDlaGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLS 165
|
...
gi 17558664 1200 ALD 1202
Cdd:PRK11432 166 NLD 168
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1051-1255 |
1.19e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.53 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1051 LNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPkhLRKHIALVSQEPILF-DTSIRENIVYG 1129
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1130 LQpgeytheqiETACSKANIHKFIDELPDGYETR--VGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEK 1207
Cdd:PRK11607 116 LK---------QDKLPKAEIASRVNEMLGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1208 QVQV-ALDAAAK-DRTCIVVAH-RLSTIVNAGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK11607 187 RMQLeVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
383-601 |
1.21e-23 |
|
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: 100.37 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfNIKYLRQlVG 462
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRR-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLF-NTSIEQNIRYGRS--DVSDEDIARALKEANAADfiktfpeglntlVGDRGV-QMSGGQKQRIAIARALVR 538
Cdd:cd03268 76 ALIEAPGFYpNLTARENLRLLARllGIRKKRIDEVLDVVGLKD------------SAKKKVkGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 539 NPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVG 601
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSlRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1259 |
1.33e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPErpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNN--DLRQMNPKHLRKH 1107
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEP--ILFDTSIRENIVYG---LQ-PGEYTHEQIETACSKANIHKFIDelpdgyetrvgeKGTQ-LSGGQKQRIA 1180
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavnLKlPEDEVRKRVDNALKRTGIEHLKD------------KPTHcLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESEKQVQVALDAAAK--DRTCIVVAHRLStIVNAGC--IMVVKNGQVVEQGTHNELI 1256
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDID-IVPLYCdnVFVMKEGRVILQGNPKEVF 230
|
...
gi 17558664 1257 AKR 1259
Cdd:PRK13636 231 AEK 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
401-600 |
1.57e-23 |
|
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: 100.62 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLrqlvgVVSQEPNLFN-TSIEQNI 479
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 rYGRSDVSDEDIARALKEANAADFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESI 559
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17558664 560 VQSALEN--ASRGRTTIVIAHRL-STVRNADKIIVM------KAGQVMEV 600
Cdd:TIGR01184 153 LQEELMQiwEEHRVTVLMVTHDVdEALLLSDRVVMLtngpaaNIGQILEV 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1033-1259 |
1.59e-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: 102.24 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1033 NKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVtvdnndlrqmnpKHlRKHIALVS 1112
Cdd:cd03291 38 NNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KH-SGRISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1113 QEPILFDTSIRENIVYGLQPGEYTHEQIETACskaNIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKIL 1192
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSYDEYRYKSVVKAC---QLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1193 LLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKR 1259
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1259 |
2.38e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPErpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEP--ILFDTSIRENIVYG-----LQPGEyTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIA 1182
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmgLDKDE-VERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1183 RALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVA-HRLSTIVN-AGCIMVVKNGQVVEQGThNELIAKR 1259
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDE 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
400-621 |
2.75e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRF--YNPDA---GQILI--DDIPIEDFNIKYLRQLVGVVSQEPNLF- 471
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLfgRNIYSPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 NTSIEQNIRYG--------RSDVSDEDIARALKEANAADFIKtfpEGLNtlvgDRGVQMSGGQKQRIAIARALVRNPKIL 543
Cdd:PRK14267 99 HLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVK---DRLN----DYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 544 LLDEATSALDAESESIVQSALENASRGRTTIVIAHR-LSTVRNADKIIVMKAGQVMEVGTHETLIEQKglYHELVHAQV 621
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENP--EHELTEKYV 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1034-1257 |
2.95e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.54 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1034 KVFFRYPERpAVPILQGLNVHVKPGQTLALVGPSGCGKS----TVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRK--- 1106
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 -HIALVSQEPIlfdTSIreNIVY--GLQPGE--YTHEQIetacSKANIHKFIDEL------PDGyETRVGEKGTQLSGGQ 1175
Cdd:COG4172 92 nRIAMIFQEPM---TSL--NPLHtiGKQIAEvlRLHRGL----SGAAARARALELlervgiPDP-ERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1176 KQRIAIARALIRNPKILLLDEATSALDTESEKQVqVALDAAAKDRT-----------CIV--VAHRLstivnagCIMvvK 1242
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQI-LDLLKDLQRELgmalllithdlGVVrrFADRV-------AVM--R 231
|
250
....*....|....*
gi 17558664 1243 NGQVVEQGTHNELIA 1257
Cdd:COG4172 232 QGEIVEQGPTAELFA 246
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1038-1255 |
3.25e-23 |
|
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: 99.37 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1038 RYPERPAVpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmNPKHLRKHIALVSQEPIL 1117
Cdd:cd03265 9 KYGDFEAV---RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1118 FDT-SIRENI-----VYGLqPGEYTHEQIETACSKANIHKFIDELPDGYetrvgekgtqlSGGQKQRIAIARALIRNPKI 1191
Cdd:cd03265 85 DDElTGWENLyiharLYGV-PGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1192 LLLDEATSALDTESEKQVQVALDA--AAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1044-1227 |
5.97e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 99.05 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1044 AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMN----PKHLRKHIALVSQEPILFD 1119
Cdd:COG4181 24 ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLRARHVGFVFQSFQLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 T-SIRENIvygLQPGEYTHEQieTACSKAnihkfIDELpdgyeTRVGEKG------TQLSGGQKQRIAIARALIRNPKIL 1192
Cdd:COG4181 104 TlTALENV---MLPLELAGRR--DARARA-----RALL-----ERVGLGHrldhypAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 17558664 1193 LLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAH 1227
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTH 205
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1031-1213 |
6.08e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.94 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYP-ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmnPKHLRkhiA 1109
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFD-TSIRENIVYGLQ-PGEytheqietacSKANIHKFIDElpdgYETRVGEKGT------QLSGGQKQRIAI 1181
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRlRGV----------PKAERRARAEE----LLALVGLADFarrriwQLSGGMRQRVGI 145
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 1182 ARALIRNPKILLLDEATSALDTESEKQVQVAL 1213
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
383-607 |
7.21e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.39 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNlFNT--SIEQNI---RY----GRSDVSDED-IARALKEANAADFIKTFpegLNTLvgdrgvqmSGGQKQRIAI 532
Cdd:COG4604 79 ILRQENH-INSrlTVRELVafgRFpyskGRLTAEDREiIDEAIAYLDLEDLADRY---LDEL--------SGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 533 ARALVRNPKILLLDEATSALD-AESESIVQsALENASR--GRTTIVIAHRLstvrN-----ADKIIVMKAGQVMEVGTHE 604
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDmKHSVQMMK-LLRRLADelGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPE 221
|
...
gi 17558664 605 TLI 607
Cdd:COG4604 222 EII 224
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
709-939 |
8.35e-23 |
|
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: 100.28 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 709 AIIAALIQGAVMPAFSLFFSQIINVFSNPDRDQ---MKKDGHFWALMFLVLAaVQGTSMLFQCSLFGVAAERLTMRIRSK 785
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIeifGLSLKTFALALLGVFV-VGAAANFGRVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 786 VYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVG 865
Cdd:cd18573 80 LFKSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 866 qalMMKYhGGSATSDAKEMENA----GKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGLTYGFA 939
Cdd:cd18573 158 ---AVFY-GRYVRKLSKQVQDAladaTKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGST 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
385-578 |
9.63e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 9.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 385 VNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDdipiedfniKYLRqlVGVV 464
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 465 SQEPNLF-NTSIEQNIRYGRSDV----------------SDEDIARALK-------------EANAADFIKTFpeGLNTL 514
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAELraleaeleeleaklaePDEDLERLAElqeefealggweaEARAEEILSGL--GFPEE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 515 VGDRGV-QMSGGQKQRIAIARALVRNPKILLLDEATSALDAesESIVqsALEN--ASRGRTTIVIAH 578
Cdd:COG0488 145 DLDRPVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--ESIE--WLEEflKNYPGTVLVVSH 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1030-1258 |
9.82e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGA---VTVDNNDLRQMNPKHLRK 1106
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 HIALVSQEP--ILFDTSIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIA 1180
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLEnravPRPEMIKIVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1032-1208 |
9.87e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.98 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQmnpkhLRKHIALV 1111
Cdd:PRK11247 15 LNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQEPILFD-TSIRENIVYGLQpGEYtheqietacsKANIHKFIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIRNPK 1190
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLK-GQW----------RDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180
....*....|....*....|
gi 17558664 1191 ILLLDEATSALD--TESEKQ 1208
Cdd:PRK11247 154 LLLLDEPLGALDalTRIEMQ 173
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
373-602 |
1.07e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.36 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 373 GQTPSKISGRISVNKVEFTYPTRADVK-ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQrFYNPD----AGQILIDDI 447
Cdd:TIGR00955 12 GRVAQDGSWKQLVSRLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 448 PIedfNIKYLRQLVGVVSQEPNLFNT-------SIEQNIRYGRSDVSDEDIAR------ALKEANAAdfiktfpeglNTL 514
Cdd:TIGR00955 91 PI---DAKEMRAISAYVQQDDLFIPTltvrehlMFQAHLRMPRRVTKKEKRERvdevlqALGLRKCA----------NTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 515 VGDRGVQ--MSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLST--VRNADKI 589
Cdd:TIGR00955 158 IGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKI 237
|
250
....*....|...
gi 17558664 590 IVMKAGQVMEVGT 602
Cdd:TIGR00955 238 ILMAEGRVAYLGS 250
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
383-597 |
1.27e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.12 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTY---PTRADvkilkgvsLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiEDF-NIKYLR 458
Cdd:PRK10771 2 LKLTDITWLYhhlPMRFD--------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHtTTPPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 459 QLVGVVSQEPNLFN-TSIEQNIRYG-----RSDVSD----EDIARalkEANAADFIKTFPEglntlvgdrgvQMSGGQKQ 528
Cdd:PRK10771 71 RPVSMLFQENNLFShLTVAQNIGLGlnpglKLNAAQreklHAIAR---QMGIEDLLARLPG-----------QLSGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 529 RIAIARALVRNPKILLLDEATSALD----AESESIVQSALENasRGRTTIVIAHRLS-TVRNADKIIVMKAGQV 597
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEdAARIAPRSLVVADGRI 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
385-597 |
1.39e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.62 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 385 VNKVeFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIpiedfNIKYLR-----Q 459
Cdd:COG1101 7 LSKT-FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-----DVTKLPeykraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 460 LVGVVSQEPNL---FNTSIEQNI--------RYGrsdvsdedIARALKEANAADF---IKTFPEGL----NTLVGdrgvQ 521
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENLalayrrgkRRG--------LRRGLTKKRRELFrelLATLGLGLenrlDTKVG----L 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 522 MSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAHRLS-TVRNADKIIVMKAGQV 597
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1048-1254 |
1.45e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.35 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDL--RQMNPKHLRKHIALVSQEP--ILFDTSIR 1123
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1124 ENIVYGLQPGEYTHEQIETACSKAnihkfIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDT 1203
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1204 ESEKQV--QVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNE 1254
Cdd:PRK13637 178 KGRDEIlnKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1034-1250 |
1.53e-22 |
|
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: 97.79 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1034 KVFFRyPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKhIALV-- 1111
Cdd:cd03267 24 KSLFK-RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQEPILFDTSIRENI-----VYGLQPGEYThEQIETACSKANIHKFIDElpdgyETRvgekgtQLSGGQKQRIAIARALI 1186
Cdd:cd03267 102 QKTQLWWDLPVIDSFyllaaIYDLPPARFK-KRLDELSELLDLEELLDT-----PVR------QLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1187 RNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG 1250
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
395-597 |
1.62e-22 |
|
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: 97.73 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL-QRFYNPDA--GQILIDDIPIE----DFNIKYLRQlvgvvsQE 467
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGTtsGQILFNGQPRKpdqfQKCVAYVRQ------DD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 PNLFNTSIEQNIRY------------GRSDVSDEDIAraLKEANaadfiktfpeglNTLVGDRGVQ-MSGGQKQRIAIAR 534
Cdd:cd03234 91 ILLPGLTVRETLTYtailrlprkssdAIRKKRVEDVL--LRDLA------------LTRIGGNLVKgISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 535 ALVRNPKILLLDEATSALDAESE-SIVQSALENASRGRTTIVIAH--RLSTVRNADKIIVMKAGQV 597
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1048-1258 |
1.73e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.08 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDnnDLRQMNP------KHLRKHIALVSQ--EPILFD 1119
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD--DITITHKtkdkyiRPVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIRENIVYGLQPGEYTHEQIetacsKANIHKFIDELpdGYETRVGEKGT-QLSGGQKQRIAIARALIRNPKILLLDEAT 1198
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDEV-----KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1199 SALDTESEKQVQVALDA--AAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
401-607 |
1.80e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL----VGVVSQEPNLF-NTSI 475
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNIRYGrsdVSDEDIARALKEANAADFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAE 555
Cdd:PRK10070 124 LDNTAFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 556 SESIVQSALE--NASRGRTTIVIAHRL-STVRNADKIIVMKAGQVMEVGTHETLI 607
Cdd:PRK10070 199 IRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
400-606 |
1.91e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 103.25 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDaGQILIDDIPIEDFNIKYL---RQLVGVVSQEPN-LFNT-- 473
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsSLNPrl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 SIEQNIRYGRSdVSDEDIARALKEANAadfIKTFPE-GLNTLVGDR-GVQMSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:PRK15134 380 NVLQIIEEGLR-VHQPTLSAAQREQQV---IAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 552 LDAESESIVQSALE--NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:PRK15134 456 LDKTVQAQILALLKslQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1038-1227 |
2.41e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1038 RYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVdnndlrqmnpkHLRKHIALVSQEPIL 1117
Cdd:NF040873 1 GYGGRPV---LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR-----------AGGARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1118 FDT---SIRENIVYGLQP-----GEYTHEQ---IETACSKANIHKFIDElpdgyetRVGEkgtqLSGGQKQRIAIARALI 1186
Cdd:NF040873 67 PDSlplTVRDLVAMGRWArrglwRRLTRDDraaVDDALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17558664 1187 RNPKILLLDEATSALDTESEKQVQVAL-DAAAKDRTCIVVAH 1227
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTH 177
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
394-555 |
2.54e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.40 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDA---GQILIDDIPIEDFNIkYLRQlVGVVSQEPNL 470
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPA-EQRR-IGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 471 F-NTSIEQNIRYG-RSDVSDED----IARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARALVRNPKILL 544
Cdd:COG4136 88 FpHLSVGENLAFAlPPTIGRAQrrarVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 17558664 545 LDEATSALDAE 555
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1045-1224 |
3.01e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 96.73 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNN----DLRQMNPK---HLRKH-IALVSQ--- 1113
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRtIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1114 ------------EPiLFDTSIREnivyglqpgeytheqiETACSKA-------NIHKFIDELPDgyetrvgekgTQLSGG 1174
Cdd:COG4778 104 viprvsaldvvaEP-LLERGVDR----------------EEARARArellarlNLPERLWDLPP----------ATFSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1175 QKQRIAIARALIRNPKILLLDEATSALDTESeKQVQVALDAAAKDR-TCIV 1224
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAAN-RAVVVELIEEAKARgTAII 206
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
390-606 |
3.04e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.94 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 390 FTYPT----RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVS 465
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 466 QEPNlfnTSIEQNIRYGR---------SDVSDED----IARALKEANA-ADFIKTFPEGLntlvgdrgvqmSGGQKQRIA 531
Cdd:PRK15112 94 QDPS---TSLNPRQRISQildfplrlnTDLEPEQrekqIIETLRQVGLlPDHASYYPHML-----------APGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 532 IARALVRNPKILLLDEATSALDAESES-IVQSALE-NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVG-THETL 606
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGsTADVL 238
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1047-1227 |
4.75e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.39 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH---LR-KHIALVSQEPILFDT-S 1121
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRaKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1122 IRENI-VYGLQPGEYTHEqietacSKANIHKFIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSA 1200
Cdd:PRK10584 105 ALENVeLPALLRGESSRQ------SRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180
....*....|....*....|....*....
gi 17558664 1201 LDTESEKQVQVALDAAAKDR--TCIVVAH 1227
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
706-969 |
4.99e-22 |
|
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: 98.00 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQgAVMPAFSlffSQIIN-VFSNPDRDQMKKDghfwALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRS 784
Cdd:cd18572 2 FVFLVVAALSE-LAIPHYT---GAVIDaVVADGSREAFYRA----VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 785 KVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMav 864
Cdd:cd18572 74 DLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVI-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 865 gqALMMKYHGGSATSDAKEMEN----AGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGLTYGFAN 940
Cdd:cd18572 150 --ALITKVYGRYYRKLSKEIQDalaeANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNT 227
|
250 260
....*....|....*....|....*....
gi 17558664 941 SIQFFTYAAAFRFGLFLIFDKnvLMEPEN 969
Cdd:cd18572 228 LLQNGTQVLVLFYGGHLVLSG--RMSAGQ 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
383-608 |
5.78e-22 |
|
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: 96.07 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-V 461
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEPNLF-NTSIEQNIRyGRSDVSDEDIARALKEANAadFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNP 540
Cdd:cd03218 78 GYLPQEASIFrKLTVEENIL-AVLEIRGLSKKEREEKLEE--LLEEF--HITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 541 KILLLDEATSALDAESESIVQSALENASRGRTTIVIA-HRLS-TVRNADKIIVMKAGQVMEVGTHETLIE 608
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
383-624 |
6.87e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.50 E-value: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRADV--KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN----IKY 456
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 LRQLVGVVSQEP--NLFNTSIEQNIRYGRSDVSdedIARALKEANAADFIKTFpeGLNTLVGDRG-VQMSGGQKQRIAIA 533
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFG---IPKEKAEKIAAEKLEMV--GLADEFWEKSpFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 534 RALVRNPKILLLDEATSALDAESESIVQSALENASR-GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQKG 611
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEVD 236
|
250
....*....|....*..
gi 17558664 612 LY--HEL--VHAQVFAD 624
Cdd:PRK13643 237 FLkaHELgvPKATHFAD 253
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
110-354 |
7.51e-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: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 110 VYLGCGIFaaGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMA 189
Cdd:cd18542 48 VALLRGVF--RYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 190 QFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYE 269
Cdd:cd18542 126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 270 DALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTvLTVFFS-VMMGSMALGQAGQQFATIGT 348
Cdd:cd18542 206 KENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFISyLWMLIWPVRQLGRLINDMSR 284
|
....*.
gi 17558664 349 ALGAAA 354
Cdd:cd18542 285 ASASAE 290
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
383-660 |
7.94e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYP--TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIE----DFNIKY 456
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 LRQLVGVVSQ--EPNLFNTSIEQNIRYGRSD--VSDEDiaralKEANAADFIKTFpeGLNTLVGDRG-VQMSGGQKQRIA 531
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDE-----AKEKALKWLKKV--GLSEDLISKSpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 532 IARALVRNPKILLLDEATSALDAES-ESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEvgtHETLIEq 609
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIK---HASPKE- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17558664 610 kglyhelvhaqVFADVDDKPKKKEAERRMSRQTSQ-RKGSVNFKTQESQVDE 660
Cdd:PRK13641 232 -----------IFSDKEWLKKHYLDEPATSRFASKlEKGGFKFSEMPLTIDE 272
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
396-637 |
1.58e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNikylRQLVGVVSQEPNLF-NTS 474
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIRY-GR-SDVSDEDIARALKEanaadFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSAL 552
Cdd:COG4152 88 VGEQLVYlARlKGLSKAEAKRRADE-----WLERL--GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 553 DAESESIVQSAL-ENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIEQ-KGLYHELVHAQVFADVDDKP 629
Cdd:COG4152 161 DPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLEADGDAGWLRALP 240
|
....*...
gi 17558664 630 KKKEAERR 637
Cdd:COG4152 241 GVTVVEED 248
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1030-1255 |
2.04e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.92 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRY---PERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQM-NPKHLR 1105
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1106 KHIALVSQEPilfDTSIRENIV----------YGLQPGEyTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQ 1175
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATIVeedvafgpenLGIPPEE-IRERVDESLKKVGMYEYRRHAPH-----------LLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1176 KQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHN 1253
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
..
gi 17558664 1254 EL 1255
Cdd:PRK13633 230 EI 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1035-1258 |
2.21e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 95.46 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1035 VFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNN--DLRQMNPKHLRKHIALVS 1112
Cdd:PRK13638 7 LWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1113 QEP--ILFDTSIRENIVYGLQpgeytheqiETACSKANIHKFIDE---LPDGYETRvgEKGTQ-LSGGQKQRIAIARALI 1186
Cdd:PRK13638 84 QDPeqQIFYTDIDSDIAFSLR---------NLGVPEAEITRRVDEaltLVDAQHFR--HQPIQcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1187 RNPKILLLDEATSALDTESEKQ-VQVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQmIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1048-1227 |
3.07e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.07 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLrkhiaLVSQEPILFD-TSIRENI 1126
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1127 VYGLqpgeythEQIETACSKANIHKFIDELPD--GYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALD-- 1202
Cdd:TIGR01184 76 ALAV-------DRVLPDLSKSERRAIVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDal 148
|
170 180
....*....|....*....|....*
gi 17558664 1203 TESEKQVQVALDAAAKDRTCIVVAH 1227
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTH 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1041-1266 |
3.15e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1041 ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPIL-FD 1119
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIRENIVYGLQP--------GEYTHEQIETACSKANIHKFIDelpdgyetrvgEKGTQLSGGQKQRIAIARALIRNPKI 1191
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfdtwTETDRAAVERAMERTGVAQFAD-----------RPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1192 LLLDEATSALDTESEKQ-VQVALDAAAKDRTCIVVAHRLStIVNAGC--IMVVKNGQVVEQG------THNELIAKRGAY 1262
Cdd:PRK09536 161 LLLDEPTASLDINHQVRtLELVRRLVDDGKTAVAAIHDLD-LAARYCdeLVLLADGRVRAAGppadvlTADTLRAAFDAR 239
|
....
gi 17558664 1263 FALT 1266
Cdd:PRK09536 240 TAVG 243
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
129-354 |
3.64e-21 |
|
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: 95.30 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 129 VICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLfdnlervregTGD--KVGLAFQM--------MAQFIGGFAVA 198
Cdd:cd18574 68 VVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRL----------TADvqEFKSSFKQcvsqglrsVTQTVGCVVSL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 199 FTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKT 278
Cdd:cd18574 138 YLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 279 GIKKSFLIGA--GLASFFViiyasYCLA---FWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIGTALGAA 353
Cdd:cd18574 218 NEKLGLGIGIfqGLSNLAL-----NGIVlgvLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAG 292
|
.
gi 17558664 354 A 354
Cdd:cd18574 293 A 293
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
400-610 |
4.19e-21 |
|
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: 93.74 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYL-RQLVGVVSQEPNLFNT-SIEQ 477
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 478 NIRYGRSdvsdediARALKEANAADFIKT-FPEgLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAes 556
Cdd:TIGR03410 95 NLLTGLA-------ALPRRSRKIPDEIYElFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP-- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 557 eSIVQ---SALE--NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQK 610
Cdd:TIGR03410 165 -SIIKdigRVIRrlRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1257 |
4.31e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.76 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1037 FRYPERPAVpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL--RKHIALVSQE 1114
Cdd:PRK13639 9 YSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1115 P--ILFDTSIRENIVYGLQPGEYTHEQIETACSKAniHKFIDElpDGYETRVGEkgtQLSGGQKQRIAIARALIRNPKIL 1192
Cdd:PRK13639 87 PddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA--LKAVGM--EGFENKPPH---HLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1193 LLDEATSALDTESEKQVQVAL-DAAAKDRTCIVVAHRLSTI-VNAGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
382-612 |
4.61e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 382 RISVNKVEFTY--PTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILI-------------DD 446
Cdd:PRK13651 2 QIKVKNIVKIFnkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkeKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 447 IPIEDF-----------NIKYLRQLVGVVSQ--EPNLFNTSIEQNIRYG-RS-DVSDEDiarALKEAnaADFIKtfpegl 511
Cdd:PRK13651 82 KVLEKLviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpVSmGVSKEE---AKKRA--AKYIE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 512 ntLVG------DRG-VQMSGGQKQRIAIARALVRNPKILLLDEATSALDAE-SESIVQSALENASRGRTTIVIAHRLSTV 583
Cdd:PRK13651 151 --LVGldesylQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNV 228
|
250 260 270
....*....|....*....|....*....|.
gi 17558664 584 -RNADKIIVMKAGQVMEVG-THETLIEQKGL 612
Cdd:PRK13651 229 lEWTKRTIFFKDGKIIKDGdTYDILSDNKFL 259
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
115-331 |
4.66e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 95.18 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 115 GIFA----AGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQ 190
Cdd:cd18552 47 GLFLlrglASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 191 FIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYED 270
Cdd:cd18552 127 VIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRK 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 271 ALEHGKKTGIKKSFLigAGLASFFV--IIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVMM 331
Cdd:cd18552 207 ANERLRRLSMKIARA--RALSSPLMelLGAIAIALVLWYGGYQVISGELTPGEFISFITALLL 267
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
96-356 |
4.92e-21 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 96 AEFSHEVIQNCLkyVYLGCGIFAAgfLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVRE 175
Cdd:cd18784 33 DKFSRAIIIMGL--LAIASSVAAG--IRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 176 GTGDKVGLAFQMMAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTV 255
Cdd:cd18784 109 TVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 256 IAFNGQEYECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLT-VFFSVMMGSm 334
Cdd:cd18784 189 RSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISfILYQLELGS- 267
|
250 260
....*....|....*....|..
gi 17558664 335 ALGQAGQQFATIGTALGAAASL 356
Cdd:cd18784 268 CLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1044-1250 |
5.02e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 92.73 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1044 AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNndlRQMNPKHlRKHIALVSQEPILF-DTSI 1122
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1123 RENIVYGLQPGEYTHEQIetacsKANIHKFID--ELPDGYETRVgekgTQLSGGQKQRIAIARALIRNPKILLLDEATSA 1200
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEA-----RRRIDEWLErlELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1201 LDTESEKQV-QVALDAAAKDRTCIVVAHRLSTiVNAGC--IMVVKNGQVVEQG 1250
Cdd:cd03269 159 LDPVNVELLkDVIRELARAGKTVILSTHQMEL-VEELCdrVLLLNKGRAVLYG 210
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
709-961 |
5.63e-21 |
|
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: 95.01 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 709 AIIAALIQGAVMPAFSLFFSQIINVFSNPDRDQMKKDGHF---WALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSK 785
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRAlnqAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 786 VYRNVLRQDATYFDMpkHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVG 865
Cdd:cd18780 81 LFSAIIAQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 866 QALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGLTYGFANSIQFF 945
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250
....*....|....*.
gi 17558664 946 TYAAAFRFGLFLIFDK 961
Cdd:cd18780 239 AIVLVLWYGGRLVIDG 254
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
397-611 |
5.74e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.59 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL--QRFYNPDAGQILID--DI---PIEDfnikylRQLVGV-VS-QE 467
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDgeDIlelSPDE------RARAGIfLAfQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 P---------NLFNTSIEqnirygrsdvsdediARALKEANAADFIKTFPEGLnTLVG------DRGVQ--MSGGQKQRI 530
Cdd:COG0396 86 PveipgvsvsNFLRTALN---------------ARRGEELSAREFLKLLKEKM-KELGldedflDRYVNegFSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 531 AIARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAH--RLSTVRNADKIIVMKAGQVMEVGTHE--T 605
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElaL 229
|
....*.
gi 17558664 606 LIEQKG 611
Cdd:COG0396 230 ELEEEG 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
399-606 |
5.90e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.88 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPI-------------EDFNIKYLRQLVGVVS 465
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 466 QEPNLFN-TSIEQNIRYGRSDV----SDEDIARALKEANAAdfiktfpeGLNTLVGDR-GVQMSGGQKQRIAIARALVRN 539
Cdd:PRK10619 99 QHFNLWShMTVLENVMEAPIQVlglsKQEARERAVKYLAKV--------GIDERAQGKyPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 540 PKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1032-1253 |
6.07e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.00 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFryPERP-AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnPKHLR-KHIA 1109
Cdd:COG1101 7 LSKTFN--PGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRaKYIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPIL---FDTSIRENIV--------YGLQPGEytheqietacSKANIHKFIDELPD---GYETRVGEKGTQLSGGQ 1175
Cdd:COG1101 84 RVFQDPMMgtaPSMTIEENLAlayrrgkrRGLRRGL----------TKKRRELFRELLATlglGLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1176 KQRIAIARALIRNPKILLLDEATSALDTESEKQVqvaLDAAAKdrtcIVVAHRLSTivnagcIMVvkngqvveqgTHN 1253
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALV---LELTEK----IVEENNLTT------LMV----------THN 208
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1047-1246 |
6.12e-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: 94.54 E-value: 6.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDpLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENi 1126
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1127 vygLQP-GEYTHEQIETACSKANIHKFIDELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTES 1205
Cdd:cd03289 97 ---LDPyGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17558664 1206 EKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQV 1246
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
401-592 |
7.48e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 7.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipieDFNIKYLRQLvgvvSQEPNLFNTSIEQNI- 479
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQR----SEVPDSLPLTVRDLVa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 -----------RYGRSDVSDedIARALKEANAADFIKtfpEGLNTLvgdrgvqmSGGQKQRIAIARALVRNPKILLLDEA 548
Cdd:NF040873 80 mgrwarrglwrRLTRDDRAA--VDDALERVGLADLAG---RQLGEL--------SGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17558664 549 TSALDAESESIVQSAL-ENASRGRTTIVIAHRLSTVRNADKIIVM 592
Cdd:NF040873 147 TTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1032-1213 |
7.79e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.61 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNdlRQMNPKHLRkhiALV 1111
Cdd:PRK11248 4 ISHLYADYGGKPA---LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPGAER---GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQ-EPILFDTSIRENIVYGLQPGEYTHEQIETACSKAniHKFIDElpDGYETRvgeKGTQLSGGQKQRIAIARALIRNPK 1190
Cdd:PRK11248 76 FQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQM--LKKVGL--EGAEKR---YIWQLSGGQRQRVGIARALAANPQ 148
|
170 180
....*....|....*....|...
gi 17558664 1191 ILLLDEATSALDTESEKQVQVAL 1213
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLL 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
383-602 |
8.28e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPtrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQL---LQRFynpDAGQILIDDIPIEDF-----NI 454
Cdd:PRK11650 4 LKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNELepadrDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 kylrqlvGVVSQEPNLF-NTSIEQNIRYG---RSdVSDEDIARALKEAnaADFIKtfpegLNTLVGDRGVQMSGGQKQRI 530
Cdd:PRK11650 79 -------AMVFQNYALYpHMSVRENMAYGlkiRG-MPKAEIEERVAEA--ARILE-----LEPLLDRKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 531 AIARALVRNPKILLLDEATSALDAESEsiVQSALE----NASRGRTTIVIAH-RLSTVRNADKIIVMKAGQVMEVGT 602
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAKLR--VQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
377-610 |
9.21e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.28 E-value: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 377 SKISGRISVNKVEFTYPTRA--DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfNI 454
Cdd:PRK13536 31 ASIPGSMSTVAIDLAGVSKSygDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 KYLRQLVGVVSQEPNL---FnTSIEQNIRYGRS-DVSDEDIARALkeANAADFIKtfpegLNTLVGDRGVQMSGGQKQRI 530
Cdd:PRK13536 110 RLARARIGVVPQFDNLdleF-TVRENLLVFGRYfGMSTREIEAVI--PSLLEFAR-----LESKADARVSDLSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 531 AIARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIE 608
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALID 261
|
..
gi 17558664 609 QK 610
Cdd:PRK13536 262 EH 263
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
401-597 |
9.97e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.25 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID--DIP-IEDFNIKYLRQLVGVVSQEPNLF-NTSIE 476
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDITrLKNREVPFLRRQIGMIFQDHHLLmDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 477 QNIRYGR--SDVSDEDIAR----ALKEANAADFIKTFPeglntlvgdrgVQMSGGQKQRIAIARALVRNPKILLLDEATS 550
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIRRrvsaALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17558664 551 ALD-AESESIVQSALENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQV 597
Cdd:PRK10908 167 NLDdALSEGILRLFEEFNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
119-353 |
1.11e-20 |
|
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: 93.70 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 119 AGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVA 198
Cdd:cd18575 52 ASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVML 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 199 FTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKT 278
Cdd:cd18575 132 FITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 279 GIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLT-VFFSVMMGSmALGQAGQQFATIGTALGAA 353
Cdd:cd18575 212 ALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQfVFYAVLAAG-SVGALSEVWGDLQRAAGAA 286
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1029-1259 |
1.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.55 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1029 EVKLNKVFFRY----P-ERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDN----NDLRQM 1099
Cdd:PRK13634 2 DITFQKVEHRYqyktPfERRA---LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1100 NPKHLRKHIALVSQ--EPILFDTSIRENIVYGLQPGEYTHEQietacSKANIHKFIDE--LPDGYETRvgeKGTQLSGGQ 1175
Cdd:PRK13634 79 KLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEED-----AKQKAREMIELvgLPEELLAR---SPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1176 KQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTH 1252
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
....*..
gi 17558664 1253 NELIAKR 1259
Cdd:PRK13634 231 REIFADP 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
386-598 |
1.64e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.87 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 386 NKVEFTYPT-RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL---- 460
Cdd:PRK10535 8 KDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrreh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLF-NTSIEQNIR----YGrsdvsdeDIARALKEANAADFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARA 535
Cdd:PRK10535 88 FGFIFQRYHLLsHLTAAQNVEvpavYA-------GLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 536 LVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRNADKIIVMKAGQVM 598
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1030-1257 |
1.79e-20 |
|
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: 91.84 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKvffRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnPKHLRKH-- 1107
Cdd:cd03218 4 ENLSK---RYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILF-DTSIRENIVYGLqpgEYTHEqietacSKANIHKFIDELPD--GYETRVGEKGTQLSGGQKQRIAIARA 1184
Cdd:cd03218 77 IGYLPQEASIFrKLTVEENILAVL---EIRGL------SKKEREEKLEELLEefHITHLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1185 LIRNPKILLLDEATSALDTESEKQVQvALDAAAKDRTCIVV-----AHRLSTIVNAGCIMvvKNGQVVEQGTHNELIA 1257
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQ-KIIKILKDRGIGVLitdhnVRETLSITDRAYII--YEGKVLAEGTPEEIAA 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1045-1258 |
1.96e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.52 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTV---ISLLERLydpLEGAVTVDNNDLRQMNPKHlrKHIALVSQEPILF-DT 1120
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRVVNELEPAD--RDIAMVFQNYALYpHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYGLQ----PGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIARALIRNPKILLLDE 1196
Cdd:PRK11650 92 SVRENMAYGLKirgmPKAEIEERVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1197 ATSALDTE------SE-KQVQVALDAaakdrTCIVV----------AHRlstivnagciMVVKNGQVVEQ-GTHNELIAK 1258
Cdd:PRK11650 161 PLSNLDAKlrvqmrLEiQRLHRRLKT-----TSLYVthdqveamtlADR----------VVVMNGGVAEQiGTPVEVYEK 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1041-1251 |
2.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1041 ERPAvpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVD----NNDLRQMNPKHLRKHIALVSQ--E 1114
Cdd:PRK13649 19 EGRA---LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtliTSTSKNKDIKQIRKKVGLVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1115 PILFDTSIRENIVYGLQPGEYTHEQIE-TACSKANIHKFIDELPDgyetrvgEKGTQLSGGQKQRIAIARALIRNPKILL 1193
Cdd:PRK13649 96 SQLFEETVLKDVAFGPQNFGVSQEEAEaLAREKLALVGISESLFE-------KNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1194 LDEATSALDTESEKQVQVALDAAAKDRTCIV-VAHRLSTIVN-AGCIMVVKNGQVVEQGT 1251
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1050-1255 |
2.13e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.00 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1050 GLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPK---HLRKHIALVSQEPiLFDTSIRENI 1126
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDP-LASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1127 vyglqpGEYTHEQIET---ACSKANIHKFIDELpdgyETRVG-------EKGTQLSGGQKQRIAIARALIRNPKILLLDE 1196
Cdd:PRK15079 118 ------GEIIAEPLRTyhpKLSRQEVKDRVKAM----MLKVGllpnlinRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1197 ATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
384-608 |
2.30e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.54 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPTRAdvkILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIK-YLRQLVG 462
Cdd:PRK10575 13 ALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNTSIEQNIRYGRSDVSDediarALKEANAADFIKTfpEGLNTLVG-----DRGV-QMSGGQKQRIAIARAL 536
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIGRYPWHG-----ALGRFGAADREKV--EEAISLVGlkplaHRLVdSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 537 VRNPKILLLDEATSALDAESESIVQSALENAS--RGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVGTHETLIE 608
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqeRGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
381-608 |
2.38e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 381 GRISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIiqllqrFY------NPDAGQILIDDIPIEDFNI 454
Cdd:COG1137 2 MTLEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 kYLRQLVGV--VSQEPNLF-NTSIEQNIR-----YGRSDVSDEDIARALKEanaaDFiktfpeGLNTLVGDRGVQMSGGQ 526
Cdd:COG1137 73 -HKRARLGIgyLPQEASIFrKLTVEDNILavlelRKLSKKEREERLEELLE----EF------GITHLRKSKAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 527 KQRIAIARALVRNPKILLLDEATSALD----AESESIVQSaLENASRGrttIVIA-HRlstVRNADKII----VMKAGQV 597
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRH-LKERGIG---VLITdHN---VRETLGICdrayIISEGKV 214
|
250
....*....|.
gi 17558664 598 MEVGTHETLIE 608
Cdd:COG1137 215 LAEGTPEEILN 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
378-618 |
2.48e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.62 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 378 KISGRISVNKVEFTYPTRAdVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILI---DDIPIEDFNI 454
Cdd:PRK15079 15 KVHFDIKDGKQWFWQPPKT-LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 KYLRQLVGVVSQEPnLFNTSIEQNI-------------RYGRSDVSDEDIARALKEANAADFIKTFPEglntlvgdrgvQ 521
Cdd:PRK15079 94 RAVRSDIQMIFQDP-LASLNPRMTIgeiiaeplrtyhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPH-----------E 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 522 MSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTVRN-ADKIIVMKAGQVM 598
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAV 241
|
250 260
....*....|....*....|
gi 17558664 599 EVGTHETlieqkgLYHELVH 618
Cdd:PRK15079 242 ELGTYDE------VYHNPLH 255
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
400-599 |
3.32e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.68 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYlrqlvGVVSQEPNLFN-TSIEQN 478
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 479 IRYGrsdVSDEDIARALKEANAADFIKtfpeglntLVGDRGV------QMSGGQKQRIAIARALVRNPKILLLDEATSAL 552
Cdd:PRK11248 91 VAFG---LQLAGVEKMQRLEIAHQMLK--------KVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17558664 553 DAESESIVQSALEN--ASRGRTTIVIAHRL-STVRNADKIIVMK--AGQVME 599
Cdd:PRK11248 160 DAFTREQMQTLLLKlwQETGKQVLLITHDIeEAVFMATELVLLSpgPGRVVE 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1047-1256 |
3.67e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.97 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPIL-FDTSIREN 1125
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1126 IVYGLQPGE--YT--HEQIETACSKANIHKFIDELpdgyetrVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSAL 1201
Cdd:PRK10253 102 VARGRYPHQplFTrwRKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1202 DTESEKQVQVALDAAAKDR--TCIVVAHRLstivNAGC-----IMVVKNGQVVEQGTHNELI 1256
Cdd:PRK10253 175 DISHQIDLLELLSELNREKgyTLAAVLHDL----NQACryashLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
706-914 |
4.12e-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: 92.10 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIIN-VFSNPDRDQMKkdghFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRS 784
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDdIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 785 KVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAV 864
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17558664 865 GQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIF 914
Cdd:cd18552 155 PIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRF 204
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1047-1255 |
4.73e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 90.66 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL-RKHIALVSQEPILFDT-SIRE 1124
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGLqpgeytheqietACSKANIHKFIDELPDGY---ETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSAL 1201
Cdd:TIGR03410 95 NLLTGL------------AALPRRSRKIPDEIYELFpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1202 DTESEKQVQVALD--AAAKDRTCIVVAHRLSTIVNAG-CIMVVKNGQVVEQGTHNEL 1255
Cdd:TIGR03410 163 QPSIIKDIGRVIRrlRAEGGMAILLVEQYLDFARELAdRYYVMERGRVVASGAGDEL 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
399-602 |
5.18e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRqlVGVVSQEPNLF-NTSIEQ 477
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 478 NIRYG----------RSDVSDEDIARALKEANAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARALVRNPKILLLDE 547
Cdd:PRK10851 94 NIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 548 ATSALDAEsesiVQSALENASRGR------TTIVIAH-RLSTVRNADKIIVMKAGQVMEVGT 602
Cdd:PRK10851 163 PFGALDAQ----VRKELRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1031-1208 |
5.33e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRyperpaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnpkHLR-KHIA 1109
Cdd:PRK10851 7 NIKKSFGR------TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARdRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILF-DTSIRENIVYGLQ--PgeyTHEQIETACSKANIHKFID-----ELPDGYETrvgekgtQLSGGQKQRIAI 1181
Cdd:PRK10851 78 FVFQHYALFrHMTVFDNIAFGLTvlP---RRERPNAAAIKAKVTQLLEmvqlaHLADRYPA-------QLSGGQKQRVAL 147
|
170 180
....*....|....*....|....*..
gi 17558664 1182 ARALIRNPKILLLDEATSALDTESEKQ 1208
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKE 174
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
395-620 |
5.73e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDdipiedfnikylrqlvGVVSQ--EPNL-F 471
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN----------------GRVSAllELGAgF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 NTSI--EQNIR-----YGrsdVSDEDIARALKE----ANAADFI----KTFpeglntlvgdrgvqmSGGQKQRIAIARAL 536
Cdd:COG1134 100 HPELtgRENIYlngrlLG---LSRKEIDEKFDEivefAELGDFIdqpvKTY---------------SSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 537 VRNPKILLLDEATSALDAE----SESIVQsalENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQkg 611
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA-- 236
|
....*....
gi 17558664 612 lYHELVHAQ 620
Cdd:COG1134 237 -YEALLAGR 244
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
130-354 |
6.32e-20 |
|
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: 91.73 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 130 ICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLLTLIM 209
Cdd:cd18551 63 TGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 210 MSLSPFMMICGLFLAKLLATAATKEakQYAVA--GGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFLIG 287
Cdd:cd18551 143 LAVVPLAFLIILPLGRRIRKASKRA--QDALGelSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEA 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 288 -----AGLASFFVIIyasycLAFWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIGTALGAAA 354
Cdd:cd18551 221 ligplMGLAVQLALL-----VVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALE 287
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1034-1229 |
7.84e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.71 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1034 KVFfryperPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH-IALVS 1112
Cdd:COG3845 13 KRF------GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1113 QEPILFDT-SIRENIVYGLQPGEYTHEQIETAcsKANIHKFIDEL-----PDgyeTRVGekgtQLSGGQKQRIAIARALI 1186
Cdd:COG3845 87 QHFMLVPNlTVAENIVLGLEPTKGGRLDRKAA--RARIRELSERYgldvdPD---AKVE----DLSVGEQQRVEILKALY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17558664 1187 RNPKILLLDEATSAL-DTESEKQVQVALDAAAKDRTCIVVAHRL 1229
Cdd:COG3845 158 RGARILILDEPTAVLtPQEADELFEILRRLAAEGKSIIFITHKL 201
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
691-1196 |
7.97e-20 |
|
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: 94.86 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 691 NLFKILRyaRPEWIYIFFAIIAALIQGAVMpafSLFFSQIINVFSNPDRDQMKkdghfWALMFLVLAAVQGTSMLFQCSL 770
Cdd:COG4615 2 NLLRLLL--RESRWLLLLALLLGLLSGLAN---AGLIALINQALNATGAALAR-----LLLLFAGLLVLLLLSRLASQLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 771 FGVAAERLTMRIRSKVYRNVLRqdATYFDMPKHSPGRITTRLATDAPNIKSAIdYRLGSIFNAIASVGGGLGIAFYYGWQ 850
Cdd:COG4615 72 LTRLGQHAVARLRLRLSRRILA--APLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAWLSPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 851 MaFLVMAIFPFMAVGQALMMKYHGGSATSDAKEMENAGKTAMEAIenIRTVQALTL-QTKLYNIFCSHLdAPHGGNISKA 929
Cdd:COG4615 149 L-FLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRAL--LEGFKELKLnRRRRRAFFDEDL-QPTAERYRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 930 IIRGLT-YGFANS-IQFFTYAAafrFGLFL-IFDKNVLMEPENVLRVLFAISFSFGTIGFAASYFPEYIKATFAAGLIFN 1006
Cdd:COG4615 225 RIRADTiFALANNwGNLLFFAL---IGLILfLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1007 M---LEEEPRIDGMTSSGTYPQLSGEVKLNKVFFRYP----ERP-AV-PIlqglNVHVKPGQTLALVGPSGCGKSTVISL 1077
Cdd:COG4615 302 LelaLAAAEPAAADAAAPPAPADFQTLELRGVTYRYPgedgDEGfTLgPI----DLTIRRGELVFIVGGNGSGKSTLAKL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1078 LERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTsireniVYGLQPGEyTHEQIETACSKANI-HKfidel 1156
Cdd:COG4615 378 LTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEA-DPARARELLERLELdHK----- 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 17558664 1157 pdgyeTRVgEKG----TQLSGGQKQRIAIARALIRNPKILLLDE 1196
Cdd:COG4615 446 -----VSV-EDGrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
383-608 |
8.18e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.79 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfNIKYLRQLVG 462
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLF-NTSIEQNIR-YGRSdvsdediaRALKEANAADFIKTFPE--GLNTLVGDRGVQMSGGQKQRIAIARALVR 538
Cdd:PRK13537 84 VVPQFDNLDpDFTVRENLLvFGRY--------FGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 539 NPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIE 608
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
376-599 |
9.19e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 9.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 376 PSKISGR--ISVNKVEFTYPtraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiedfN 453
Cdd:COG0488 307 PPERLGKkvLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE------T 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 454 IKylrqlVGVVSQEPNLFNT--SIEQNIRygrsdvsdeDIARALKEANAADFIKTF---PEGLNTLVGDrgvqMSGGQKQ 528
Cdd:COG0488 378 VK-----IGYFDQHQEELDPdkTVLDELR---------DGAPGGTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 529 RIAIARALVRNPKILLLDEATSALDAESESIVQSALENASrGrTTIVIAH-R--LSTVrnADKIIVMKAGQVME 599
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1038-1257 |
9.48e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.41 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1038 RYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH-------------L 1104
Cdd:PRK10619 14 RYGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1105 RKHIALVSQEPILFD-TSIRENI------VYGLQPGEyTHEQIETACSKANIHkfidelpdgyETRVGEKGTQLSGGQKQ 1177
Cdd:PRK10619 91 RTRLTMVFQHFNLWShMTVLENVmeapiqVLGLSKQE-ARERAVKYLAKVGID----------ERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1178 RIAIARALIRNPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVNAGC-IMVVKNGQVVEQGTHNEL 1255
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVlRIMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQL 239
|
..
gi 17558664 1256 IA 1257
Cdd:PRK10619 240 FG 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
398-597 |
1.32e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.96 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-VGVVSQEPNLF-NTSI 475
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFpNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNIRYG--RSDVSDEDIARALKEANAADFIKTFPEGLNtlVGDRgvqmsggqkQRIAIARALVRNPKILLLDEATSALD 553
Cdd:PRK15439 104 KENILFGlpKRQASMQKMKQLLAALGCQLDLDSSAGSLE--VADR---------QIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17558664 554 -AESESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQV 597
Cdd:PRK15439 173 pAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1030-1251 |
1.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPErpAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTV---DNNDLRQMnpKHLRK 1106
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgiDTGDFSKL--QGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 HIALVSQEP--ILFDTSIRENIVYG-----LQPGEyTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRI 1179
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIE-IRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1180 AIARALIRNPKILLLDEATSALDTESEKQVQVALDAA-AKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGT 1251
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
383-596 |
1.68e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 86.35 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipieDFNIKYLRQLvg 462
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----TVKIGYFEQL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 vvsqepnlfntsieqnirygrsdvsdediaralkeanaadfiktfpeglntlvgdrgvqmSGGQKQRIAIARALVRNPKI 542
Cdd:cd03221 72 ------------------------------------------------------------SGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 543 LLLDEATSALDAESesivQSALENASRG--RTTIVIAH-R--LSTVrnADKIIVMKAGQ 596
Cdd:cd03221 92 LLLDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1032-1256 |
2.33e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.46 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALV 1111
Cdd:PRK10575 14 LRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQE-PILFDTSIRENIVYGLQP--------GEYTHEQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIA 1182
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAIGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1183 RALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVNAgC--IMVVKNGQVVEQGTHNELI 1256
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARY-CdyLVALRGGEMIAQGTPAELM 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
397-608 |
2.46e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.77 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQIL-----IDDIPieDFNIKYLRQLVGVVSQEPNlf 471
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLS--PGKLQALRRDIQFIFQDPY-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 nTSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFPE--GLNTLVGDR-GVQMSGGQKQRIAIARALVRNPKILLLDEA 548
Cdd:PRK10261 412 -ASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLErvGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 549 TSALDAESESIVQSALENASR--GRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIE 608
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
398-627 |
2.61e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIK-YLRQLVGVVSQEPNLF-NTSI 475
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNIRYGRSDVSDEDIARALKEANAADFIKTFPEGL--NTLVGDrgvqMSGGQKQRIAIARALVRNPKILLLDEATSALD 553
Cdd:PRK11288 97 AENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 554 A-ESESIVQSALENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQvmEVGTHETLieqKGLYHE-LVHAQVFADVDD 627
Cdd:PRK11288 173 ArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGR--YVATFDDM---AQVDRDqLVQAMVGREIGD 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1044-1251 |
4.80e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 88.17 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1044 AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL-RKHIALVSQEPILFDT-S 1121
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1122 IRENIVYGLQPGeyTHEQIETAC--------SKANIHKFIDELPD--GYETRVGEKGTQLSGGQKQRIAIARALIRNPKI 1191
Cdd:COG0411 96 VLENVLVAAHAR--LGRGLLAALlrlprarrEEREARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1192 LLLDEATSAL-DTESEKQVQVALD-AAAKDRTCIVVAHRLStIVNAGC--IMVVKNGQVVEQGT 1251
Cdd:COG0411 174 LLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMD-LVMGLAdrIVVLDFGRVIAEGT 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1043-1245 |
4.81e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.30 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1043 PAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYdP---LEGAVTVDNNDLRQMNPKHL-RKHIALVSQEPILF 1118
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1119 -DTSIRENIVYG--LQPGEYTH-EQIETACSK--ANIHKFIDelPDgyeTRVGEkgtqLSGGQKQRIAIARALIRNPKIL 1192
Cdd:PRK13549 95 kELSVLENIFLGneITPGGIMDyDAMYLRAQKllAQLKLDIN--PA---TPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1193 LLDEATSALdTESEKQVQVAL--DAAAKDRTCIVVAHRLSTiVNAGC--IMVVKNGQ 1245
Cdd:PRK13549 166 ILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNE-VKAISdtICVIRDGR 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
396-619 |
5.23e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.22 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKS----TIIQLLQRFYNPDAGQILIDDIPIEDFNikyLR-QLVGVVSQEP-N 469
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCA---LRgRKIATIMQNPrS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 470 LFNT-------SIEQNIRYGRSDvSDEDIARALKE---ANAADFIKTFPeglntlvgdrgVQMSGGQKQRIAIARALVRN 539
Cdd:PRK10418 91 AFNPlhtmhthARETCLALGKPA-DDATLTAALEAvglENAARVLKLYP-----------FEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 540 PKILLLDEATSALDAESESIVQSALEN--ASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGTHETLIE--QKGLYH 614
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNapKHAVTR 238
|
....*
gi 17558664 615 ELVHA 619
Cdd:PRK10418 239 SLVSA 243
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1063-1255 |
8.32e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.14 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1063 LVGPSGCGKSTVISLLERLYDPLEGAVTV-------DNNDLRQMNP---------KHLRKHIALVSQEP--ILFDTSIRE 1124
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdKKNNHELITNpyskkiknfKELRRRVSMVFQFPeyQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGL----QPGEYTHEQIETACSKANI-HKFIDELPDGyetrvgekgtqLSGGQKQRIAIARALIRNPKILLLDEATS 1199
Cdd:PRK13631 137 DIMFGPvalgVKKSEAKKLAKFYLNKMGLdDSYLERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1200 ALDTESEKQ-VQVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK13631 206 GLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
397-606 |
9.00e-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: 86.65 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID--DIPIEDFNIkylRQLVGVVSQEPNLFN-- 472
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREPREV---RRRIGIVFQDLSVDDel 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 473 TSIEQNIRYGR-----SDVSDEDIARALKEANAADF----IKTFpeglntlvgdrgvqmSGGQKQRIAIARALVRNPKIL 543
Cdd:cd03265 89 TGWENLYIHARlygvpGAERRERIDELLDFVGLLEAadrlVKTY---------------SGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 544 LLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEklKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1024-1257 |
9.19e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1024 PQLSGEVKLNKVFFRYPERPAVpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPkH 1103
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVV---DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 LRKHIALVSQ----EPilfDTSIRENI-VYGLQPGeytheqIETACSKANIHKFID--ELPDGYETRVGEkgtqLSGGQK 1176
Cdd:PRK13537 78 ARQRVGVVPQfdnlDP---DFTVRENLlVFGRYFG------LSAAAARALVPPLLEfaKLENKADAKVGE----LSGGMK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1177 QRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDA-AAKDRTCIVVAHRLST---IVNAGCimVVKNGQVVEQGTH 1252
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEaerLCDRLC--VIEEGRKIAEGAP 222
|
....*
gi 17558664 1253 NELIA 1257
Cdd:PRK13537 223 HALIE 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1029-1255 |
9.77e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.24 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1029 EVK-LNKvffRYPERPAVpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNndlRQMNPKHlRKH 1107
Cdd:COG4152 3 ELKgLTK---RFGDKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILF-DTSIRENIVY-----GLQPGEytheqietacSKANIHKFID--ELPDGYETRVGEkgtqLSGGQKQRI 1179
Cdd:COG4152 73 IGYLPEERGLYpKMKVGEQLVYlarlkGLSKAE----------AKRRADEWLErlGLGDRANKKVEE----LSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1180 AIARALIRNPKILLLDEATSALDTES-EKQVQVALDAAAKDRTCIVVAHRLSTiVNAGC--IMVVKNGQVVEQGTHNEL 1255
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMEL-VEELCdrIVIINKGRKVLSGSVDEI 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1048-1251 |
1.02e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTvisLLERLYD--PLEGAVTVDNNDLRQMNPKHLRKHIA-LVSQEPILFDTSire 1124
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMAGllPGQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 niVYGL----QPGEYTHEQIETA----CSKANihkfideLPDGYETRVgekgTQLSGGQKQRIAIARALIR-----NP-- 1189
Cdd:COG4138 86 --VFQYlalhQPAGASSEAVEQLlaqlAEALG-------LEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptiNPeg 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1190 KILLLDEATSALDTeseKQvQVALDA-----AAKDRTCIVVAHRLS-TIVNAGCIMVVKNGQVVEQGT 1251
Cdd:COG4138 153 QLLLLDEPMNSLDV---AQ-QAALDRllrelCQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1030-1245 |
1.06e-18 |
|
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: 84.04 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNdlrqmnpkhlrkhia 1109
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 lvsqepilfdtsirENIVYglqpgeytheqietacskanihkfidelpdgYEtrvgekgtQLSGGQKQRIAIARALIRNP 1189
Cdd:cd03221 63 --------------VKIGY-------------------------------FE--------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALdaAAKDRTCIVVAH-R--LSTIVNAgcIMVVKNGQ 1245
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL--KEYPGTVILVSHdRyfLDQVATK--IIELEDGK 144
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
397-602 |
1.17e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.41 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRF---YNPDA---GQILIDDIPIEDFNIKYLRQLVGVVSQEPNL 470
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKIkvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 471 F-NTSIEQNIRYGRSDVSDEDiARALKEANAADFIKTfpeGLNTLVGDR----GVQMSGGQKQRIAIARALVRNPKILLL 545
Cdd:PRK14246 102 FpHLSIYDNIAYPLKSHGIKE-KREIKKIVEECLRKV---GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 546 DEATSALDAESESIVQSALENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQVMEVGT 602
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGS 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
395-578 |
1.45e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTS 474
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIRYGRSDVSDEDIARALKEANAADFiktfpeglntlvGDRGV-QMSGGQKQRIAIARALVRNPKILLLDEATSALD 553
Cdd:cd03231 90 VLENLRFWHADHSDEQVEEALARVGLNGF------------EDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 17558664 554 AESESIVQSAL-ENASRGRTTIVIAH 578
Cdd:cd03231 158 KAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
396-611 |
1.59e-18 |
|
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: 85.27 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRF--YNPDAGQILIDDIPIEDFNIkYLRQLVGV--VSQEPnlf 471
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPP-EERARLGIflAFQYP--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 ntsieqnirygrsdvsdEDIAralkEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:cd03217 87 -----------------PEIP----GVKNADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 552 LDAESESIVQSALEN-ASRGRTTIVIAH--RLSTVRNADKIIVMKAGQVMEVGTHETL--IEQKG 611
Cdd:cd03217 135 LDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELAleIEKKG 199
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1026-1257 |
1.92e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 86.81 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1026 LSGEVKLNKVFFRYPERPAVpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLR 1105
Cdd:COG4167 10 LSKTFKYRTGLFRRQQFEAV---KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1106 KHIALVSQEPilfDTSirenivygLQPGEYTHEQIE------TACSKANIHKFIDE-------LPDGYETRVGEkgtqLS 1172
Cdd:COG4167 87 KHIRMIFQDP---NTS--------LNPRLNIGQILEeplrlnTDLTAEEREERIFAtlrlvglLPEHANFYPHM----LS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1173 GGQKQRIAIARALIRNPKILLLDEATSALDTESEKQ-VQVALDAAAKDR-TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQ 1249
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQiINLMLELQEKLGiSYIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231
|
....*...
gi 17558664 1250 GTHNELIA 1257
Cdd:COG4167 232 GKTAEVFA 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
398-595 |
2.23e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-VGVVSQEPNLFNT-SI 475
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDElTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNIRYGR------SDVSDEDIARALKEANAADFIKTFPEGLNTLVGDrgvqMSGGQKQRIAIARALVRNPKILLLDEAT 549
Cdd:PRK09700 98 LENLYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17558664 550 SAL-DAESESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAG 595
Cdd:PRK09700 174 SSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
400-597 |
2.58e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.64 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL----VGVVSQEPNL---FN 472
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLlpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 473 TSieqnirygrsdvsdEDIARAL-------KEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLL 545
Cdd:PRK11629 104 AL--------------ENVAMPLligkkkpAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 546 DEATSALDAE-SESIVQSALE-NASRGRTTIVIAHRLSTVRNADKIIVMKAGQV 597
Cdd:PRK11629 170 DEPTGNLDARnADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1044-1257 |
3.15e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1044 AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH-IALVSQEPILF-DTS 1121
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1122 IRENIVYGLQPGEYTHEQIETACSKANIHKFIDelpdgyetrvgEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSAL 1201
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLD-----------SSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1202 dTESE-----KQVQVALDaaaKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG-----THNELIA 1257
Cdd:PRK15439 172 -TPAEterlfSRIRELLA---QGVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIQ 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1030-1255 |
3.21e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.71 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRY-PERP-AVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDN----NDLRQMNPKH 1103
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 LRKHIALVSQEP--ILFDTSIRENIVYGLQPGEYTHEQIET-ACSKANIHkfidelpdGYETRVGEKGT-QLSGGQKQRI 1179
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMV--------GLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1180 AIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKD-RTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
398-608 |
3.70e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.29 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIeDFNIKYLRQL--VGVVSQEPNLF-NTS 474
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPKSSQEagIGIIHQELNLIpQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 475 IEQNIRYGRSDVSDE---DIARALKEANAADFIKTFPEGLNTLVGDrgvqMSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:PRK10762 96 IAENIFLGREFVNRFgriDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 552 L-DAESESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQ------VMEVgTHETLIE 608
Cdd:PRK10762 172 LtDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQfiaereVADL-TEDSLIE 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
397-602 |
4.38e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.22 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYnPDA---GQILIDDIPIEDFNIKYLRQL-VGVVSQEPNLF- 471
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTERAgIAIIHQELALVk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 NTSIEQNI-------RYGRSDVsDEDIARA---LKEANaadfIKTFPeglNTLVGDRGvqmsGGQKQRIAIARALVRNPK 541
Cdd:PRK13549 96 ELSVLENIflgneitPGGIMDY-DAMYLRAqklLAQLK----LDINP---ATPVGNLG----LGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 542 ILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQvmEVGT 602
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDlKAHGIACIYISHKLNEVKAiSDTICVIRDGR--HIGT 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1045-1284 |
4.50e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.78 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL----RKHIALVSQE-PILFD 1119
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIRENIVYglqPGEYTheQIETACSKANIHKFIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATS 1199
Cdd:PRK10535 101 LTAAQNVEV---PAVYA--GLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1200 ALDTESEKQVQVALDA-AAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVVEQGTHNELIAKRGAYFALTQKQSS-NQSGGA 1277
Cdd:PRK10535 174 ALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTASGwRQFVSG 253
|
....*..
gi 17558664 1278 FdtSEAL 1284
Cdd:PRK10535 254 F--REAL 258
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
167-606 |
4.62e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 89.47 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 167 FDNLERVREG------TGD--KVGLAFQMMAQFIGGFAV---AFTY----DWLLTLIMMSLSPFMMICGLFLA----KLL 227
Cdd:COG4615 96 LERLERIGAArllaalTEDvrTISQAFVRLPELLQSVALvlgCLAYlawlSPPLFLLTLVLLGLGVAGYRLLVrrarRHL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 228 ATAATKEA---KQY-AVAGGIAEEVLTSIRTvIAFNGQEYE--CKRYEDaleHGKKTGIKKSFLIGAGLASFFVIIYAsy 301
Cdd:COG4615 176 RRAREAEDrlfKHFrALLEGFKELKLNRRRR-RAFFDEDLQptAERYRD---LRIRADTIFALANNWGNLLFFALIGL-- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 302 cLAFWVGTNFVYSGRLESGTVLTVFFsvMMGsmALGQAGQQFATIGTALGAAASLYEV---IDRIPEIDAYSTEGQTPSK 378
Cdd:COG4615 250 -ILFLLPALGWADPAVLSGFVLVLLF--LRG--PLSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPAD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 379 ISgRISVNKVEFTYPTRADVK--ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKY 456
Cdd:COG4615 325 FQ-TLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 457 LRQLVGVVSQEPNLFNTSieqnirYGRSDVSDEDIARA-LKEANAADfiKTfpeglnTLVGDR--GVQMSGGQKQRIAIA 533
Cdd:COG4615 404 YRQLFSAVFSDFHLFDRL------LGLDGEADPARARElLERLELDH--KV------SVEDGRfsTTDLSQGQRKRLALL 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 534 RALVRNPKILLLDEATS----------------ALDAesesivqsalenasRGRTTIVIAH--RLSTVrnADKIIVMKAG 595
Cdd:COG4615 470 VALLEDRPILVFDEWAAdqdpefrrvfytellpELKA--------------RGKTVIAISHddRYFDL--ADRVLKMDYG 533
|
490
....*....|.
gi 17558664 596 QVMEVGTHETL 606
Cdd:COG4615 534 KLVELTGPAAL 544
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1009-1250 |
4.71e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 90.61 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1009 EEEPRIDGMTSSGTYPQLSGEVKLNKVFFRYPERPAVpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGA 1088
Cdd:PTZ00243 638 IVEGGTGGGHEATPTSERSAKTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1089 VTVDnndlrqmnpkhlrKHIALVSQEPILFDTSIRENIVYGlqpGEYTHEQIETACSKANIHKFIDELPDGYETRVGEKG 1168
Cdd:PTZ00243 717 VWAE-------------RSIAYVPQQAWIMNATVRGNILFF---DEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKG 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1169 TQLSGGQKQRIAIARALIRNPKILLLDEATSALDTE-SEKQVQVALDAAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQVV 1247
Cdd:PTZ00243 781 VNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
...
gi 17558664 1248 EQG 1250
Cdd:PTZ00243 861 FSG 863
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
384-604 |
5.16e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLqrfynpdAGQILIDDIP---IEDF-------- 452
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAgshIELLgrtvqreg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 453 ----NIKYLRQLVGVVSQEPNLFNT-SIEQNIRYGR--------------SDVSDEDIARALKEANAADFIKtfpeglnt 513
Cdd:PRK09984 76 rlarDIRKSRANTGYIFQQFNLVNRlSVLENVLIGAlgstpfwrtcfswfTREQKQRALQALTRVGMVHFAH-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 514 lvgDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLS-TVRNADKII 590
Cdd:PRK09984 148 ---QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIV 224
|
250
....*....|....
gi 17558664 591 VMKAGQVMEVGTHE 604
Cdd:PRK09984 225 ALRQGHVFYDGSSQ 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1030-1259 |
6.77e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRY-PERPAVPI-LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVD----NNDLRQMNPKH 1103
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhiTPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 LRKHIALVSQ--EPILFDTSIRENIVYGLQPGEYTHEQietacSKANIHKFIDELpdGYETRVGEKGT-QLSGGQKQRIA 1180
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE-----AKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIAK 1258
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 17558664 1259 R 1259
Cdd:PRK13641 236 K 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
384-601 |
6.96e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.98 E-value: 6.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiedfNIKYLRQLVGV 463
Cdd:PRK11701 8 SVRGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM------RDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQEPN-LFNTS---IEQNIRYG-RSDVS-DEDIARALK----------EANAADFIKTFPEGLNTLvGDRGVQMSGGQK 527
Cdd:PRK11701 79 SEAERRrLLRTEwgfVHQHPRDGlRMQVSaGGNIGERLMavgarhygdiRATAGDWLERVEIDAARI-DDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 528 QRIAIARALVRNPKILLLDEATSALDAEsesiVQSALENASRGRTT------IVIAHRLSTVRN-ADKIIVMKAGQVMEV 600
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLLVMKQGRVVES 233
|
.
gi 17558664 601 G 601
Cdd:PRK11701 234 G 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
401-597 |
7.37e-18 |
|
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: 82.87 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL-VGVVSQEpnlfntsieqni 479
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPED------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 RYGRSDVSDEDIARalkeanaadfiktfpeglNTLVGdrgVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAES-ES 558
Cdd:cd03215 84 RKREGLVLDLSVAE------------------NIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAkAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17558664 559 IVQSALENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQV 597
Cdd:cd03215 143 IYRLIRELADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1027-1255 |
8.04e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 8.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1027 SGEVKLNKVFFRYP---ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLE-RLYDPLEGAVTVDNNDlRQMNPK 1102
Cdd:TIGR00955 17 DGSWKQLVSRLRGCfcrERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfRSPKGVKGSGSVLLNG-MPIDAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1103 HLRKHIALVSQEPILFDT-SIRENIVYglQPGEYTHEQIETACSKANIHKFIDE--LPDGYETRVGEKGTQ--LSGGQKQ 1177
Cdd:TIGR00955 96 EMRAISAYVQQDDLFIPTlTVREHLMF--QAHLRMPRRVTKKEKRERVDEVLQAlgLRKCANTRIGVPGRVkgLSGGERK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1178 RIAIARALIRNPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIV--NAGCIMVVKNGQVVEQGTHNE 1254
Cdd:TIGR00955 174 RLAFASELLTDPPLLFCDEPTSGLDSFMAYSVvQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSPDQ 253
|
.
gi 17558664 1255 L 1255
Cdd:TIGR00955 254 A 254
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1046-1227 |
8.51e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.42 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVdnndLRQMNPKHLR---KHIALVSQepilFDT-- 1120
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARlarARIGVVPQ----FDNld 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 ---SIREN-IVYGLQPGEYTHEqIETACSkaNIHKFIdELPDGYETRVGEkgtqLSGGQKQRIAIARALIRNPKILLLDE 1196
Cdd:PRK13536 127 lefTVRENlLVFGRYFGMSTRE-IEAVIP--SLLEFA-RLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 1197 ATSALDTESEKQVQVALDA-AAKDRTCIVVAH 1227
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSlLARGKTILLTTH 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1062-1257 |
1.52e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1062 ALVGPSGCGKSTVISLLERLYDPLEG------AVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVYGLQPGEY 1135
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1136 THEQIETACSKANIHKFidELPDGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDA 1215
Cdd:PRK14271 131 VPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17558664 1216 AAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:PRK14271 209 LADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
410-604 |
1.75e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 410 PGQTV-ALVGSSGCGKSTIIQLLQRFYNPDAGQILIDD-----------IPIEDFNIKYlrqlvgvVSQEPNLF-NTSIE 476
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgicLPPEKRRIGY-------VFQDARLFpHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 477 QNIRYGRSDVSDEDIARALKEANAADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIARALVRNPKILLLDEATSALDAES 556
Cdd:PRK11144 95 GNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 557 ESIVQSALENASRG-RTTIV-IAHRLSTV-RNADKIIVMKAGQVMEVGTHE 604
Cdd:PRK11144 164 KRELLPYLERLAREiNIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPLE 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
400-578 |
2.04e-17 |
|
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: 82.02 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDF------NIKYLRQLVGVvsqEPNLfnt 473
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrdepheNILYLGHLPGL---KPEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 SIEQNIRYGRSDVSDED--IARALKEANAADFIktfpeglNTLVGdrgvQMSGGQKQRIAIARALVRNPKILLLDEATSA 551
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQrtIEDALAAVGLTGFE-------DLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*...
gi 17558664 552 LDAESESIVQSALE-NASRGRTTIVIAH 578
Cdd:TIGR01189 158 LDKAGVALLAGLLRaHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1039-1255 |
2.42e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.70 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1039 YPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEP--I 1116
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 LFDTSIRENIVYG-----LQPGEYTHeQIETACSKANIHKFIDELPDgyetrvgekgtQLSGGQKQRIAIARALIRNPKI 1191
Cdd:PRK13652 91 IFSPTVEQDIAFGpinlgLDEETVAH-RVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1192 LLLDEATSALDTESEKQVQVALDAAAKD--RTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
400-610 |
2.44e-17 |
|
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: 83.75 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQIliddipiedfniKYLRQlVGVVSQEPNLFNTSIEQNI 479
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KHSGR-ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 RYGRSdvSDEDIARA-LKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESE- 557
Cdd:cd03291 119 IFGVS--YDEYRYKSvVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEk 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 558 SIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHETLIEQK 610
Cdd:cd03291 197 EIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1038-1196 |
2.46e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1038 RYPERPAVpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnPKHLR--KHIALVSQEP 1115
Cdd:COG1137 12 SYGKRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKRarLGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1116 ILF-DTSIRENIVYGLQPGEYTHEQIetacsKANIHKFIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLL 1194
Cdd:COG1137 88 SIFrKLTVEDNILAVLELRKLSKKER-----EERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
..
gi 17558664 1195 DE 1196
Cdd:COG1137 161 DE 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1057-1209 |
4.90e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.45 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1057 PGQTLALVGPSGCGKSTVISLLERLYDPLEGAVT-----VDNNDLRQMNPkhLRKHIALVSQEPI-------LFDTSIRE 1124
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGKLQA--LRRDIQFIFQDPYasldprqTVGDSIME 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NI-VYGLQPGEYTHEQIetacskANIHKFIDELPDgYETRVGEkgtQLSGGQKQRIAIARALIRNPKILLLDEATSALDT 1203
Cdd:PRK10261 427 PLrVHGLLPGKAAAARV------AWLLERVGLLPE-HAWRYPH---EFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
....*.
gi 17558664 1204 ESEKQV 1209
Cdd:PRK10261 497 SIRGQI 502
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1048-1204 |
4.93e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.46 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH---LRKHIALVSQEP-ILFDTSIR 1123
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1124 ENIVYGLQPGEYTHEQIETACSKAnihkfIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDT 1203
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAA-----LDKV--GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
.
gi 17558664 1204 E 1204
Cdd:PRK10908 171 A 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
393-617 |
6.41e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.60 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 393 PTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDD-IPIEDfNIKYLRQlVGVV----SQe 467
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKR-RKEFARR-IGVVfgqrSQ- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 pnL---------FNtsIEQNIrYGrsdVSDEDIARALKEanaadFIKTFpeGLNTLVgDRGV-QMSGGQKQRIAIARALV 537
Cdd:COG4586 107 --LwwdlpaidsFR--LLKAI-YR---IPDAEYKKRLDE-----LVELL--DLGELL-DTPVrQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 538 RNPKILLLDEATSALDAESESIVQSAL--ENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQKGLYH 614
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLkeYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
...
gi 17558664 615 ELV 617
Cdd:COG4586 251 TIV 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1045-1247 |
8.02e-17 |
|
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: 85.26 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLY--DPLEGAVTVDNNDLRQMNPKHL-RKHIALVSQEPILF-DT 1120
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYGLQ---PGEYTHEQIETACSKANIHKFidELPDGYETR-VGEKGtqlsGGQKQRIAIARALIRNPKILLLDE 1196
Cdd:TIGR02633 94 SVAENIFLGNEitlPGGRMAYNAMYLRAKNLLREL--QLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1197 ATSALdTESEKQVQVAL--DAAAKDRTCIVVAHRLSTiVNAGC--IMVVKNGQVV 1247
Cdd:TIGR02633 168 PSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNE-VKAVCdtICVIRDGQHV 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
380-606 |
8.61e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 380 SGRISVNKVEFTYPTRAdvkilkgvsldaqpgqTVALVGSSGCGKSTIIQLLQRFYNP-----DAGQILIDDIPIEDF-N 453
Cdd:PRK14271 32 AGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 454 IKYLRQLVGVVSQEPNLFNTSIEQNIRYG--------RSDVSDEDIARaLKEANAADFIKTfpeglntLVGDRGVQMSGG 525
Cdd:PRK14271 96 VLEFRRRVGMLFQRPNPFPMSIMDNVLAGvrahklvpRKEFRGVAQAR-LTEVGLWDAVKD-------RLSDSPFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 526 QKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVGTHE 604
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTE 247
|
..
gi 17558664 605 TL 606
Cdd:PRK14271 248 QL 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
397-608 |
9.40e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 9.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRF--YNPDAGQILiddipiedFNIKYLRQLVGVVSQE------P 468
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRII--------YHVALCEKCGYVERPSkvgepcP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 469 NLFNTSIEQNIRYGRSDvsdEDIARALKEANAADFIKTFP------------EGLNTL--VGDRGVQM------------ 522
Cdd:TIGR03269 84 VCGGTLEPEEVDFWNLS---DKLRRRIRKRIAIMLQRTFAlygddtvldnvlEALEEIgyEGKEAVGRavdliemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 523 ---------SGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTVRN-ADKII 590
Cdd:TIGR03269 161 rithiardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAI 240
|
250
....*....|....*...
gi 17558664 591 VMKAGQVMEVGTHETLIE 608
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1036-1262 |
9.44e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.83 E-value: 9.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1036 FFRyPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNndlrqMNP----KHLRKHIALV 1111
Cdd:COG4586 27 LFR-REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPfkrrKEFARRIGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 ----SQepILFDTSIRENI-----VYGLQPGEYtheqietacsKANIHKFIDELpdgyetRVGEKGT----QLSGGQKQR 1178
Cdd:COG4586 101 fgqrSQ--LWWDLPAIDSFrllkaIYRIPDAEY----------KKRLDELVELL------DLGELLDtpvrQLSLGQRMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1179 IAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVnAGC--IMVVKNGQVVEQGTHNE 1254
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIE-ALCdrVIVIDHGRIIYDGSLEE 241
|
....*...
gi 17558664 1255 LIAKRGAY 1262
Cdd:COG4586 242 LKERFGPY 249
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1046-1256 |
1.26e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKST---VISLLERlYDPLEGAVTVDNNDLRQMNP-KHLRKHIALVSQEPI----- 1116
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSPdERARAGIFLAFQYPVeipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 -LFD------TSIRENIVYGLQpgeyTHEQIETACSKANI-HKFID-ELPDGyetrvgekgtqLSGGQKQRIAIARALIR 1187
Cdd:COG0396 93 sVSNflrtalNARRGEELSARE----FLKLLKEKMKELGLdEDFLDrYVNEG-----------FSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1188 NPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAH--RLSTIVNAGCIMVVKNGQVVEQGTHnELI 1256
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVaEGVNKLRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELA 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
383-579 |
1.32e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 78.73 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTypTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQIlidDIPiEDFNIKYLrqlvg 462
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMP-EGEDLLFL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 vvSQEPNLFNTSIEQNIRYGRSDVsdediaralkeanaadfiktfpeglntlvgdrgvqMSGGQKQRIAIARALVRNPKI 542
Cdd:cd03223 70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 17558664 543 LLLDEATSALDAESESIVQSALEnaSRGRTTIVIAHR 579
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
400-606 |
1.34e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKS-TIIQLLQRFYNPDA----GQILIDDIPIEDFNIKYLRQLVG----VVSQEP-- 468
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPmv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 469 --NLFNTsIEQNI-------RYGRSDVSDEDIARALKEA---NAADFIKTFPEglntlvgdrgvQMSGGQKQRIAIARAL 536
Cdd:PRK15134 104 slNPLHT-LEKQLyevlslhRGMRREAARGEILNCLDRVgirQAAKRLTDYPH-----------QLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 537 VRNPKILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
365-598 |
1.40e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.45 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 365 EIDAYSTEGQTPSKISGRISVNKvEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILI 444
Cdd:cd03267 2 EVSNLSKSYRVYSKEPGLIGSLK-SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 445 DD-IPIEDfNIKYLRQLVGVVSQEPNL-FNTSIEQNIRYGRS--DVSDEDIARALKEAnaADFIKTFPEgLNTLVgdRgv 520
Cdd:cd03267 81 AGlVPWKR-RKKFLRRIGVVFGQKTQLwWDLPVIDSFYLLAAiyDLPPARFKKRLDEL--SELLDLEEL-LDTPV--R-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 521 QMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSAL--ENASRGRTTIVIAHRLSTV-RNADKIIVMKAGQV 597
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeYNRERGTTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
.
gi 17558664 598 M 598
Cdd:cd03267 233 L 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1047-1202 |
1.57e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPK---HLRKH-IALVSQ-EPILFDTS 1121
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1122 IRENIVYGLQPGEYTHEQIETacskanihKFIDELPD-GYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSA 1200
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINS--------RALEMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
..
gi 17558664 1201 LD 1202
Cdd:PRK11629 176 LD 177
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
375-597 |
1.59e-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: 80.27 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 375 TPSKISGRISVNKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID--DIPIEDF 452
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrVSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 453 NikylrqlVGVvsqEPNLfntSIEQNIR-YGR-SDVSDEDIARALkeanaaDFIKTFPEglntlVGDRGVQ----MSGGQ 526
Cdd:cd03220 92 G-------GGF---NPEL---TGRENIYlNGRlLGLSRKEIDEKI------DEIIEFSE-----LGDFIDLpvktYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 527 KQRIAIARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQV 597
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1047-1250 |
2.56e-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: 78.72 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKST---VISLLERlYDPLEGAVTVDNNDLRQMNP-KHLRKHIALVSQEPILFdtsi 1122
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTlakTIMGHPK-YEVTEGEILFKGEDITDLPPeERARLGIFLAFQYPPEI---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1123 renivyglqPGeytheqietacskANIHKFIDELPDGyetrvgekgtqLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:cd03217 90 ---------PG-------------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1203 TESEKQVQVALDA-AAKDRTCIVVAH--RLSTIVNAGCIMVVKNGQVVEQG 1250
Cdd:cd03217 137 IDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
391-613 |
3.21e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 391 TYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL--QRfyNPDAGQILIDDIPIEDFNIKYLRQL-VGVVSQE 467
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 -------PNLfntSIEQNI---RYGRSDVS-----DEDIARAlkeaNAADFIKTF---PEGLNTLVGdrgvQMSGGQKQR 529
Cdd:COG3845 342 rlgrglvPDM---SVAENLilgRYRRPPFSrggflDRKAIRA----FAEELIEEFdvrTPGPDTPAR----SLSGGNQQK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 530 IAIARALVRNPKILLLDEATSALDAES-ESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVM-EVGTHETL 606
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEAT 490
|
....*..
gi 17558664 607 IEQKGLY 613
Cdd:COG3845 491 REEIGLL 497
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
46-353 |
3.61e-16 |
|
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: 80.53 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 46 LAVGIIVSCATGVGLPLMSIIMGNVSQNFVTLGTIFLDPNSTAsekaaaraefsheVIQNCLKYVYLGCGIFAAGFLQAS 125
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSG-------------LLRILLLLLGLYLLSALFSYLQNR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 126 CFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLL 205
Cdd:cd18547 68 LMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 206 TLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFL 285
Cdd:cd18547 148 TLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 286 IGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIGTALGAA 353
Cdd:cd18547 228 SGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGA 295
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
398-599 |
3.91e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.92 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYnPDA---GQILIDDIPIEDFNIKYLRQLvGVV--SQE----P 468
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRFKDIRDSEAL-GIViiHQElaliP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 469 NLfntSIEQNIRYGRSDVSDEDIARALKEANAADFIKTFpeGLN----TLVGDRGVqmsgGQKQRIAIARALVRNPKILL 544
Cdd:NF040905 92 YL---SIAENIFLGNERAKRGVIDWNETNRRARELLAKV--GLDespdTLVTDIGV----GKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 545 LDEATSAL-DAESESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVME 599
Cdd:NF040905 163 LDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
709-920 |
3.97e-16 |
|
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: 80.22 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 709 AIIAALIQGAVMPAFSLFFSQIIN-VFSNPDRDQMkkDGHFWALMFLVLAAVQGTSMLFqcSLFGVAAERLTMRIRSKVY 787
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDqGFAAGNTALL--NRAFLLLLAVALVLALASALRF--YLVSWLGERVVADLRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 788 RNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIdyrlGSIF-----NAIASVgGGLGIAFYYGWQMAFLVMAIFPFM 862
Cdd:cd18575 77 AHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVV----GSSLsialrNLLLLI-GGLVMLFITSPKLTLLVLLVIPLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 863 AVGQALMMKY--HGGSATSDAkeMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDA 920
Cdd:cd18575 150 VLPIILFGRRvrRLSRASQDR--LADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEA 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
399-600 |
5.46e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.46 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFY--NPDAGQILIDDIPIedfnikylrqlvgvvSQEPNLfntsIE 476
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GREASL----ID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 477 QNIRYGRSDVSDEDIARAlKEANAADFIKTFPEglntlvgdrgvqMSGGQKQRIAIARALVRNPKILLLDEATSALDAES 556
Cdd:COG2401 105 AIGRKGDFKDAVELLNAV-GLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17558664 557 ESIVQSALENASR--GRTTIVIAHRlSTVRNA---DKIIVMKAGQVMEV 600
Cdd:COG2401 172 AKRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPEE 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1047-1258 |
5.64e-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: 82.54 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERL--YDPLEGAV---------------------------------TV 1091
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpvcggtlepeEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1092 DNNDLRQMNPKHLRKHIALVSQEPILF--DTSIRENIVYGLQPGEYTHEQietACSKAniHKFIDELpdGYETRVGEKGT 1169
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKE---AVGRA--VDLIEMV--QLSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1170 QLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQV 1246
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEI 247
|
250
....*....|..
gi 17558664 1247 VEQGTHNELIAK 1258
Cdd:TIGR03269 248 KEEGTPDEVVAV 259
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
112-346 |
6.06e-16 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 80.07 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 112 LGCGIFAAgfLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQF 191
Cdd:cd18590 47 LGSSLSAG--LRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 192 IGGFAVAFTYDWLLTLIMMSLSPFMMIcglfLAKLLAT--AATKEAKQYAVA--GGIAEEVLTSIRTVIAFNGQEYECKR 267
Cdd:cd18590 125 LGMLGFMLSLSWQLTLLTLIEMPLTAI----AQKVYNTyhQKLSQAVQDSIAkaGELAREAVSSIRTVRSFKAEEEEACR 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 268 YEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTVLtvffSVMMGSMALGQAGQQFATI 346
Cdd:cd18590 201 YSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLV----SFILYQKNLGSYVRTLVYI 275
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
101-328 |
6.33e-16 |
|
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: 79.76 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 101 EVIQNCLKYVYLGCGIFAAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGtgdk 180
Cdd:cd18541 38 QLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMA---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 181 VGLAFQMMAQ--FIGGFAVA--FTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVI 256
Cdd:cd18541 114 LGPGILYLVDalFLGVLVLVmmFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIK 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 257 AFNGQEYECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTvLTVFFS 328
Cdd:cd18541 194 AFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGD-LVAFNS 264
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1041-1215 |
6.77e-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: 77.40 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1041 ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPkHLRKHIALVSQEP-ILFD 1119
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPgLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIRENIVYGLQPGEYTHEQIETACSKANIhkfidelpDGYETRVGEkgtQLSGGQKQRIAIARALIRNPKILLLDEATS 1199
Cdd:TIGR01189 88 LSALENLHFWAAIHGGAQRTIEDALAAVGL--------TGFEDLPAA---QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170
....*....|....*.
gi 17558664 1200 ALDTESEKQVQVALDA 1215
Cdd:TIGR01189 157 ALDKAGVALLAGLLRA 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1048-1250 |
7.24e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.13 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVT---VDNNDLRQM---------------------NPKH 1103
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifKDEKNKKKTkekekvleklviqktrfkkikKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 LRKHIALVSQ--EPILFDTSIRENIVYGlqPGEYTHEQIETACSKANIHKFIDeLPDGYETRvgeKGTQLSGGQKQRIAI 1181
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFG--PVSMGVSKEEAKKRAAKYIELVG-LDESYLQR---SPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1182 ARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKD-RTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQG 1250
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDG 247
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1030-1248 |
7.68e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVdnndlrqmnPKHLRkhIA 1109
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETVK--IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDT--SIRENIVYGLQPGEYTH------------EQIETACSKanihkfidelpdgyetrvgekgtqLSGGQ 1175
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGTEQEvrgylgrflfsgDDAFKPVGV------------------------LSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 1176 KQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAakDRTCIVVAH-R--LSTIVNagCIMVVKNGQVVE 1248
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRVAT--RILEFEDGGVRE 509
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
399-607 |
7.76e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 399 KILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiEDFNIKYL----RQLVGVVSQEPNLFNT- 473
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD---EDISLLPLharaRRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 SIEQN------IRygrsdvsdEDIARALKEANAADFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDE 547
Cdd:PRK10895 94 SVYDNlmavlqIR--------DDLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 548 ATSALDAESESIVQSALEN-ASRGRTTIVIAHRL-STVRNADKIIVMKAGQVMEVGTHETLI 607
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHlRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
112-334 |
8.63e-16 |
|
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: 79.36 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 112 LGCGIfAAGFLQAscfmVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLfdnlervregTGD--KVGLAFQMMA 189
Cdd:cd18548 53 LIAGI-LAGYFAA----KASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRL----------TNDvtQVQNFVMMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 190 Q--------FIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQ 261
Cdd:cd18548 118 RmlvrapimLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNRE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 262 EYECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTV-------LTVFFSVMMGSM 334
Cdd:cd18548 198 DYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1030-1255 |
1.02e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.46 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPErpaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlRKHIA 1109
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILF-DTSIRENIVYGLQPGEYTHEQIETACSKA----NIHKFIDELPDGyetrvgekgtqLSGGQKQRIAIARA 1184
Cdd:PRK11000 79 MVFQSYALYpHLSVAENMSFGLKLAGAKKEEINQRVNQVaevlQLAHLLDRKPKA-----------LSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 1185 LIRNPKILLLDEATSALDTESEKQVQVALDAAAK--DRTCIVVAH-RLSTIVNAGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
394-577 |
1.17e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFN----IKYLRQLVGVvsqEPN 469
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeaCHYLGHRNAM---KPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 470 LfntSIEQNIR-----YGRSDvsdEDIARALkeanaADFiktfpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK13539 88 L---TVAENLEfwaafLGGEE---LDIAAAL-----EAV------GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|...
gi 17558664 545 LDEATSALDAESESIVQSALEnASRGRTTIVIA 577
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIR-AHLAQGGIVIA 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1041-1213 |
1.34e-15 |
|
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: 76.76 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1041 ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDT 1120
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYgLQPGEYThEQIETACSKANIHKFIDeLPDGyetrvgekgtQLSGGQKQRIAIARALIRNPKILLLDEATSA 1200
Cdd:cd03231 89 SVLENLRF-WHADHSD-EQVEEALARVGLNGFED-RPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|...
gi 17558664 1201 LDTESEKQVQVAL 1213
Cdd:cd03231 156 LDKAGVARFAEAM 168
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
398-599 |
1.34e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQL----VGVVSQEPNLFNT 473
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 474 -SIEQNIRY-----GRSDVSDEDIARALKEAnaadfiktfpEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDE 547
Cdd:PRK10584 103 lNALENVELpallrGESSRQSRNGAKALLEQ----------LGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 548 ATSALDAES-ESIVQSALE-NASRGRTTIVIAHRLSTVRNADKIIVMKAGQVME 599
Cdd:PRK10584 173 PTGNLDRQTgDKIADLLFSlNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1026-1257 |
1.67e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.51 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1026 LSGEVKLNKVFFRYPERPAVPI--LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDN----NDLRQM 1099
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTPFEFkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1100 NP-KHLRKHIALVSQEP--ILFDTSIRENIVYGlqpgeytheQIETACSKANIHKFIDEL------PDGYETRvgeKGTQ 1170
Cdd:PRK13645 83 KEvKRLRKEIGLVFQFPeyQLFQETIEKDIAFG---------PVNLGENKQEAYKKVPELlklvqlPEDYVKR---SPFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1171 LSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKD--RTCIVVAHRLSTIVN-AGCIMVVKNGQVV 1247
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVI 230
|
250
....*....|
gi 17558664 1248 EQGTHNELIA 1257
Cdd:PRK13645 231 SIGSPFEIFS 240
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1029-1257 |
1.70e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.29 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1029 EVK-LNKVFfRYP----ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH 1103
Cdd:PRK15112 6 EVRnLSKTF-RYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 LRKHIALVSQEPI-----------LFDTSIRENIvyGLQPGEYTHEQIETAcskanihKFIDELPDgyetRVGEKGTQLS 1172
Cdd:PRK15112 85 RSQRIRMIFQDPStslnprqrisqILDFPLRLNT--DLEPEQREKQIIETL-------RQVGLLPD----HASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1173 GGQKQRIAIARALIRNPKILLLDEATSALDTESEKQ-VQVALDAAAKDRTC-IVVAHRLSTIVN-AGCIMVVKNGQVVEQ 1249
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQlINLMLELQEKQGISyIYVTQHLGMMKHiSDQVLVMHQGEVVER 231
|
....*...
gi 17558664 1250 GTHNELIA 1257
Cdd:PRK15112 232 GSTADVLA 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1041-1251 |
2.03e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1041 ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPK-------------HLR-K 1106
Cdd:PRK10261 25 EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQvielseqsaaqmrHVRgA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 HIALVSQEPIlfdTSIRENIVYGLQPGEYT--HEQIETACSKANIHKFIDE--LPDGyETRVGEKGTQLSGGQKQRIAIA 1182
Cdd:PRK10261 105 DMAMIFQEPM---TSLNPVFTVGEQIAESIrlHQGASREEAMVEAKRMLDQvrIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1183 RALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRT--CIVVAHRLSTIVN-AGCIMVVKNGQVVEQGT 1251
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
118-328 |
2.20e-15 |
|
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: 78.71 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 118 AAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAV 197
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 198 AFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKK 277
Cdd:cd18564 149 MFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLR 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 278 TGIKksfliGAGLASFF-----VIIYASYCLAFWVGTNFVYSGRLESGTvLTVFFS 328
Cdd:cd18564 229 AGLR-----AARLQALLspvvdVLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLA 278
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
401-597 |
2.27e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.45 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIK--------YL---RQLVGVVsqePN 469
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagiaYVpedRKGEGLV---LD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 470 LfntSIEQNI------RYGRSDVsdedIARALKEANAADFIKTF---PEGLNTLVGdrgvQMSGGQKQRIAIARALVRNP 540
Cdd:COG1129 345 L---SIRENItlasldRLSRGGL----LDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 541 KILLLDEATSALD--AESEsIVQSALENASRGRTTIVIahrlST-----VRNADKIIVMKAGQV 597
Cdd:COG1129 414 KVLILDEPTRGIDvgAKAE-IYRLIRELAAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
397-602 |
2.35e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYnPDA---GQILIDDIPIEDFNIKYL-RQLVGVVSQEPNLF- 471
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 NTSIEQNIRYG--------RSDvSDEDIARA---LKEANAADFIKTFPeglntlVGDRGvqmsGGQKQRIAIARALVRNP 540
Cdd:TIGR02633 92 ELSVAENIFLGneitlpggRMA-YNAMYLRAknlLRELQLDADNVTRP------VGDYG----GGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 541 KILLLDEATSAL-DAESESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQvmEVGT 602
Cdd:TIGR02633 161 RLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ--HVAT 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
383-553 |
2.63e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDipiedfnikYLRqlVG 462
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------KLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQEPNLFNT---SIEQNIRYgRSDVSDEDIARALKEANAADFIktfpeglntlvgDRGVQ-MSGGQKQRIAIARALVR 538
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLI------------DAPMQkLSGGETQRVLLARALLN 137
|
170
....*....|....*
gi 17558664 539 NPKILLLDEATSALD 553
Cdd:PRK09544 138 RPQLLVLDEPTQGVD 152
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1022-1250 |
3.38e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.03 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1022 TYPQLSGEVKLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNdlrqmnp 1101
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1102 khLRKHIAL-VSQEPILfdtSIRENI-----VYGLQPGEytheqietacskanIHKFID------ELPDGYETRVGEkgt 1169
Cdd:cd03220 85 --VSSLLGLgGGFNPEL---TGRENIylngrLLGLSRKE--------------IDEKIDeiiefsELGDFIDLPVKT--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1170 qLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDA-AAKDRTCIVVAHRLSTIVNAgC--IMVVKNGQV 1246
Cdd:cd03220 143 -YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRL-CdrALVLEKGKI 220
|
....
gi 17558664 1247 VEQG 1250
Cdd:cd03220 221 RFDG 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
400-607 |
3.50e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPNL-FNTSIEQN 478
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 479 IRYGRSDvSDEDIARALKEANAADFIKTFPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESES 558
Cdd:PRK10253 102 VARGRYP-HQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17558664 559 IVQSALE--NASRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVGTHETLI 607
Cdd:PRK10253 181 DLLELLSelNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
403-604 |
3.51e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 403 GVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDF---------------NIKYLRQLVGV---- 463
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQE--------PNLFNTSieqniRYGRSdvsdediaralkEANAADFIKTFPE--GLNTLVGDRGVQMSGGQKQRIAIA 533
Cdd:PRK11300 103 VAQHqqlktglfSGLLKTP-----AFRRA------------ESEALDRAATWLErvGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 534 RALVRNPKILLLDEATSALDAEsESIVQSALENASR---GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHE 604
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPK-ETKELDELIAELRnehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPE 239
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
365-604 |
5.01e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.63 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 365 EIDAYSTEGQTPSKISG--RISVNKVEFTYPTRADVkiLKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQI 442
Cdd:PRK10522 303 ALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 443 LIDDIPIEDFNIKYLRQLVGVVSQEPNLFNTSIEQniryGRSDVSDEDIARALKEANAADfiKTfpeglnTLVGDR--GV 520
Cdd:PRK10522 381 LLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGP----EGKPANPALVEKWLERLKMAH--KL------ELEDGRisNL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 521 QMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTVRNADKIIVMKAGQVM 598
Cdd:PRK10522 449 KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
....*.
gi 17558664 599 EVGTHE 604
Cdd:PRK10522 529 ELTGEE 534
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1043-1250 |
6.34e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1043 PAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH-IALVSQEPILFDT- 1120
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENI---------VYGLQPGEYTHEQIETA--CSKANIHKFIDELpdgyetrVGEkgtqLSGGQKQRIAIARALIRNP 1189
Cdd:PRK09700 96 TVLENLyigrhltkkVCGVNIIDWREMRVRAAmmLLRVGLKVDLDEK-------VAN----LSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALDAAAKDRTCIV-VAHRLSTIVNAG-CIMVVKNGQVVEQG 1250
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRICdRYTVMKDGSSVCSG 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1055-1255 |
6.72e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 77.47 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1055 VKPGQTLALVGPSGCGKStVISL-LERLYDpLEGAVTVD-----NNDLRQMNPKHLRK----HIALVSQEPIlfdTSIRE 1124
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKS-VSSLaIMGLID-YPGRVMAEklefnGQDLQRISEKERRNlvgaEVAMIFQDPM---TSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1125 NIVYGLQPGEY--THEqieTACSKANIHKFIDEL-----PDGyETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEA 1197
Cdd:PRK11022 105 CYTVGFQIMEAikVHQ---GGNKKTRRQRAIDLLnqvgiPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1198 TSALDTESEKQ-VQVALDAAAKDRTCIV-VAHRLSTIVNAG-CIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK11022 181 TTALDVTIQAQiIELLLELQQKENMALVlITHDLALVAEAAhKIIVMYAGQVVETGKAHDI 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1046-1257 |
6.85e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKS-TVISLLERLYDP----LEGAVTVDNNDLRQMNPKHLRK----HIALVSQEPI 1116
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 lfdtsIRENIVYGLQPGEYT----HEQIETACSKANIHKFIDelpdgyetRVGEKGT---------QLSGGQKQRIAIAR 1183
Cdd:PRK15134 103 -----VSLNPLHTLEKQLYEvlslHRGMRREAARGEILNCLD--------RVGIRQAakrltdyphQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1184 ALIRNPKILLLDEATSALDTESEKQVQVALDAAAK--DRTCIVVAHRLStIVN--AGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLS-IVRklADRVAVMQNGRCVEQNRAATLFS 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
395-609 |
7.27e-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: 79.08 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQI-------LIDDIPIEDFNIKYLRQLVGVVSQE 467
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 PNLF-NTSIEQNIRYGRS-DVSDE-DIARALKEANAADFIKTFPEGLNTLVGDrgvQMSGGQKQRIAIARALVRNPKILL 544
Cdd:TIGR03269 374 YDLYpHRTVLDNLTEAIGlELPDElARMKAVITLKMVGFDEEKAEEILDKYPD---ELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 545 LDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQ 609
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
383-605 |
8.57e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.07 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEdfniKYLRQ-LV 461
Cdd:PRK15056 7 IVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEPNL---FNTSIEQNI---RYG------RSDVSDEDIA-RALKEANAADFiktfpegLNTLVGdrgvQMSGGQKQ 528
Cdd:PRK15056 81 AYVPQSEEVdwsFPVLVEDVVmmgRYGhmgwlrRAKKRDRQIVtAALARVDMVEF-------RHRQIG----ELSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 529 RIAIARALVRNPKILLLDEATSALDAESESIVQSAL-ENASRGRTTIVIAHRLSTVRNADKIIVMKAGQVMEVGTHET 605
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1062-1250 |
1.00e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1062 ALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMN-----PKHLRkHIALVSQEPILF-DTSIRENIVYGLQPgeY 1135
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclPPEKR-RIGYVFQDARLFpHYKVRGNLRYGMAK--S 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1136 THEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDA 1215
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 17558664 1216 AAKD-RTCIV-VAHRLSTIVN-AGCIMVVKNGQVVEQG 1250
Cdd:PRK11144 174 LAREiNIPILyVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1043-1257 |
1.06e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1043 PAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH-LRKHIALVSQEPILF-DT 1120
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVpEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYGLQPG-----------EYTHEQIEtacskaniHKFIDELPDgyeTRVGEkgtqLSGGQKQRIAIARALIRNP 1189
Cdd:PRK11288 95 TVAENLYLGQLPHkggivnrrllnYEAREQLE--------HLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1190 KILLLDEATSALDT-ESEKQVQVALDAAAKDRTCIVVAHRLSTIVnAGC--IMVVKNGQVVE------QGTHNELIA 1257
Cdd:PRK11288 160 RVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIF-ALCdaITVFKDGRYVAtfddmaQVDRDQLVQ 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1041-1257 |
1.58e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1041 ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVT-------VDNNDLRQMNPKHLRKHIALVSQ 1113
Cdd:TIGR03269 293 DRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1114 EPILF-DTSIRENI-----------------VYGLQPGEYTHEQIETacskanihkFIDELPDgyetrvgekgtQLSGGQ 1175
Cdd:TIGR03269 373 EYDLYpHRTVLDNLteaiglelpdelarmkaVITLKMVGFDEEKAEE---------ILDKYPD-----------ELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1176 KQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKD--RTCIVVAHRLStIVNAGC--IMVVKNGQVVEQGT 1251
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMD-FVLDVCdrAALMRDGKIVKIGD 511
|
....*.
gi 17558664 1252 HNELIA 1257
Cdd:TIGR03269 512 PEEIVE 517
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1031-1270 |
2.08e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.35 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPERPA--VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVdnndlrqmnpkhlRKHI 1108
Cdd:COG1134 23 SLKELLLRRRRTRReeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-------------NGRV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1109 AlvsqePIL-----FDTSI--RENI-----VYGLQPGEyTHEQIETACSKANIHKFIDeLPdgyetrVGekgtQLSGGQK 1176
Cdd:COG1134 90 S-----ALLelgagFHPELtgRENIylngrLLGLSRKE-IDEKFDEIVEFAELGDFID-QP------VK----TYSSGMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1177 QRIAIARALIRNPKILLLDEATSALDTE-SEKQVQVALDAAAKDRTCIVVAHRLSTIVNAgC--IMVVKNGQVVEQGTHN 1253
Cdd:COG1134 153 ARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRL-CdrAIWLEKGRLVMDGDPE 231
|
250
....*....|....*..
gi 17558664 1254 ELIAkrgAYFALTQKQS 1270
Cdd:COG1134 232 EVIA---AYEALLAGRE 245
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1048-1246 |
2.19e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.85 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH-IALVSQEP----ILFDTSI 1122
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1123 RENIVyglqpgeytheqietacskanihkfideLPDgyetrvgekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:cd03215 96 AENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17558664 1203 TESEKQV-QVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQV 1246
Cdd:cd03215 137 VGAKAEIyRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
706-903 |
2.78e-14 |
|
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: 74.78 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIINVFSNpdrdqmkKDGHFWALMFLVLAAV-QGTSMLFQCSLFGVAAERLTMRIRS 784
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSA-------GGSSGGLLALLVALFLlQAVLSALSSYLLGRTGERVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 785 KVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAV 864
Cdd:cd18551 74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 17558664 865 GQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQA 903
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKA 190
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1030-1263 |
2.83e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPErpaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQ-MNPKHLRKHI 1108
Cdd:PRK11614 6 LSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1109 ALVSQEPILFD-TSIRENIVYGLQPGEYTHEQietacskANIHKFIDELPDGYETRVGEKGTqLSGGQKQRIAIARALIR 1187
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQ-------ERIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1188 NPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVV----AHRLSTIVNAGciMVVKNGQVVEQGTHNELIAK---RG 1260
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLveqnANQALKLADRG--YVLENGHVVLEDTGDALLANeavRS 232
|
...
gi 17558664 1261 AYF 1263
Cdd:PRK11614 233 AYL 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1041-1207 |
2.99e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.98 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1041 ERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDlrQMNPKHlRKHIALVSQEPILFDT 1120
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD--IDDPDV-AEACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 -SIRENI-----VYGlqpgeyTHE-QIETACSKANIHKFIDeLPDGYetrvgekgtqLSGGQKQRIAIARALIRNPKILL 1193
Cdd:PRK13539 88 lTVAENLefwaaFLG------GEElDIAAALEAVGLAPLAH-LPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170
....*....|....
gi 17558664 1194 LDEATSALDTESEK 1207
Cdd:PRK13539 151 LDEPTAALDAAAVA 164
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1017-1255 |
3.87e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.15 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1017 MTSSGTYPQLsgEVKLNKVFFRYPErPAVPILQGLNVHVKPGQTLALVGPSGCGKS-TVISLLERLYDP--LEGAVTVDN 1093
Cdd:PRK09473 4 LAQQQADALL--DVKDLRVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1094 NDLRQMNPKHLRK----HIALVSQEPIlfdTSIRENIVYGLQPGE--YTHEQIETACSKANIHKFID--ELPDGYEtRVG 1165
Cdd:PRK09473 81 REILNLPEKELNKlraeQISMIFQDPM---TSLNPYMRVGEQLMEvlMLHKGMSKAEAFEESVRMLDavKMPEARK-RMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1166 EKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKD--RTCIVVAHRLStiVNAG-C--IMV 1240
Cdd:PRK09473 157 MYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLG--VVAGiCdkVLV 234
|
250
....*....|....*
gi 17558664 1241 VKNGQVVEQGTHNEL 1255
Cdd:PRK09473 235 MYAGRTMEYGNARDV 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
386-597 |
5.83e-14 |
|
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: 71.91 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 386 NKVEFTYPTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL----QRFYNPDaGQILIDDIPIEDFNIKYLRQLV 461
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSVE-GDIHYNGIPYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 gVVSQEPNLFNT-SIEQNIRYgrsdvsdediarALKeANAADFIktfpeglntlvgdRGVqmSGGQKQRIAIARALVRNP 540
Cdd:cd03233 87 -YVSEEDVHFPTlTVRETLDF------------ALR-CKGNEFV-------------RGI--SGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 541 KILLLDEATSALDAesesivQSALENASRGR--------TTIVIAHRLS--TVRNADKIIVMKAGQV 597
Cdd:cd03233 138 SVLCWDNSTRGLDS------STALEILKCIRtmadvlktTTFVSLYQASdeIYDLFDKVLVLYEGRQ 198
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
750-907 |
6.38e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 74.09 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 750 ALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGS 829
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVSGVLP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 830 IFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMavgqALMMKYHGG---SATSDAKEMENA-GKTAMEAIENIRTVQALT 905
Cdd:cd18564 135 LLTNLLTLVGMLGVMFWLDWQLALIALAVAPLL----LLAARRFSRrikEASREQRRREGAlASVAQESLSAIRVVQAFG 210
|
..
gi 17558664 906 LQ 907
Cdd:cd18564 211 RE 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
395-578 |
6.69e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPI----EDF--NIKYLRQLVGV---VS 465
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqrDEYhqDLLYLGHQPGIkteLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 466 QEPNL-FNTSIEQnirygrsDVSDEDIARALKEANAADFiktfpegLNTLVGdrgvQMSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK13538 91 ALENLrFYQRLHG-------PGDDEALWEALAQVGLAGF-------EDVPVR----QLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 17558664 545 LDEATSALDAESESIVQSALE-NASRGRTTIVIAH 578
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAqHAEQGGMVILTTH 187
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
709-949 |
9.11e-14 |
|
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: 73.29 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 709 AIIAALIQGAVMPAFSLFFSQIIN-VFSNPDRDQMKKDghfwALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSKVY 787
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDaALGGGDTASLNQI----ALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 788 RNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVGQA 867
Cdd:cd18576 77 RHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 868 LMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALT---LQTKLYNifcSHLDAPHGGNISKAIIRGLtygFANSIQF 944
Cdd:cd18576 155 LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTredYEIERYR---KALERVVKLALKRARIRAL---FSSFIIF 228
|
....*
gi 17558664 945 FTYAA 949
Cdd:cd18576 229 LLFGA 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1032-1276 |
1.10e-13 |
|
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: 76.59 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYpERPAVpilQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLrQMNPKHLRKHIALV 1111
Cdd:TIGR01257 934 LVKIFEPS-GRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQEPILFD-TSIRENIVYGLQPGEYTHEQietacSKANIHKFIDElpDGYETRVGEKGTQLSGGQKQRIAIARALIRNPK 1190
Cdd:TIGR01257 1009 PQHNILFHhLTVAEHILFYAQLKGRSWEE-----AQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1191 ILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAG-CIMVVKNGQVVEQGThnELIAKR----GAYFAL 1265
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGdRIAIISQGRLYCSGT--PLFLKNcfgtGFYLTL 1159
|
250
....*....|.
gi 17558664 1266 TQKQSSNQSGG 1276
Cdd:TIGR01257 1160 VRKMKNIQSQR 1170
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1047-1202 |
1.25e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnPKHLR--KHIALVSQEPILFDT-SIR 1123
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARarRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1124 ENIVYGLQ-PGEYTHEQIETACSKANIHKFIDELPDGYetrvgekGTQLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:PRK10895 97 DNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1057-1250 |
1.35e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.27 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1057 PGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL----RKHIA-----LVSQEPIlfdTSIRENIV 1127
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLLrtewgFVHQHPR---DGLRMQVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1128 YGLQPGE---------YTH---------EQIETACSKanihkfIDELPdgyetrvgekgTQLSGGQKQRIAIARALIRNP 1189
Cdd:PRK11701 108 AGGNIGErlmavgarhYGDiratagdwlERVEIDAAR------IDDLP-----------TTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1190 KILLLDEATSALDTesekQVQ-----------VALDAAAkdrtcIVVAHRLSTI-VNAGCIMVVKNGQVVEQG 1250
Cdd:PRK11701 171 RLVFMDEPTGGLDV----SVQarlldllrglvRELGLAV-----VIVTHDLAVArLLAHRLLVMKQGRVVESG 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
412-648 |
1.45e-13 |
|
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: 76.21 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 412 QTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfNIKYLRQLVGVVSQEPNLFN--TSIEQNIRYGRSDVSDE 489
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhlTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 490 DIARALKEANAADfiktfpEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASR 569
Cdd:TIGR01257 1036 EEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 570 GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIE--QKGLYHELVhaqvfadvddkpkkkeaeRRMSRQTSQRK 646
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLV------------------RKMKNIQSQRG 1171
|
..
gi 17558664 647 GS 648
Cdd:TIGR01257 1172 GC 1173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
387-602 |
1.47e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.61 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 387 KVEFTYPTrADVKILKGVSLDAQPGQTVALVGSSGCGKST-------------------------IIQLLQRFYNP-DAG 440
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgllaangriggsatfngreILNLPEKELNKlRAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 441 QI-LIDDIPIEDFNiKYLR---QLVGVVSQEPNLF-NTSIEQNIRygrsdvsdedIARALKEANAADFIKTFPEglntlv 515
Cdd:PRK09473 98 QIsMIFQDPMTSLN-PYMRvgeQLMEVLMLHKGMSkAEAFEESVR----------MLDAVKMPEARKRMKMYPH------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 516 gdrgvQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTT--IVIAHRLSTVRN-ADKIIVM 592
Cdd:PRK09473 161 -----EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVM 235
|
250
....*....|
gi 17558664 593 KAGQVMEVGT 602
Cdd:PRK09473 236 YAGRTMEYGN 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1013-1233 |
1.48e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1013 RIDGMTSSGTY--PQLSGEVKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLE-RLY-DPLEGA 1088
Cdd:PLN03211 50 KFENMKNKGSNikRILGHKPKISDETRQIQERT---ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1089 VTVDNNDLrqmnPKHLRKHIALVSQEPILF-DTSIRENIVYG--LQPGEYTHEQIETACSKANIHKFidELPDGYETRVG 1165
Cdd:PLN03211 127 ILANNRKP----TKQILKRTGFVTQDDILYpHLTVRETLVFCslLRLPKSLTKQEKILVAESVISEL--GLTKCENTIIG 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1166 EKGTQ-LSGGQKQRIAIARALIRNPKILLLDEATSALD-TESEKQVQVALDAAAKDRTCIVVAHRLSTIV 1233
Cdd:PLN03211 201 NSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSRV 270
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1043-1248 |
1.57e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1043 PAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYdP---LEGAVTVDNN-----DLRQMNpkhlRKHIALVSQE 1114
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEvcrfkDIRDSE----ALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1115 ----PILfdtSIRENIVYGLQPGEY-------THEQIETACSKANihkfIDELPDgyeTRVGEKGTqlsgGQKQRIAIAR 1183
Cdd:NF040905 87 laliPYL---SIAENIFLGNERAKRgvidwneTNRRARELLAKVG----LDESPD---TLVTDIGV----GKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1184 ALIRNPKILLLDEATSAL-DTESEKQVQVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVE 1248
Cdd:NF040905 153 ALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1038-1247 |
1.80e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1038 RYPERPAV---PIL--QGLNV---------HVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH 1103
Cdd:COG1129 244 LFPKRAAApgeVVLevEGLSVggvvrdvsfSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1104 -LRKHIALVS----QEPILFDTSIRENIVYGLQPGEYTHEQIETACSKANIHKFIDEL---PDGYETRVGekgtQLSGGQ 1175
Cdd:COG1129 324 aIRAGIAYVPedrkGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1176 KQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVV-----------AHRlstivnagcIMVVKNG 1244
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVisselpellglSDR---------ILVMREG 470
|
...
gi 17558664 1245 QVV 1247
Cdd:COG1129 471 RIV 473
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
707-907 |
1.91e-13 |
|
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: 72.46 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 707 FFAIIAALIQGAVMPAFSLFFSQII-NVFSNPDRDqmkkdgHFW--ALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIR 783
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIIdSVIGGGLRE------LLWllALLILGVALLRGVFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 784 SKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMA 863
Cdd:cd18542 76 NDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17558664 864 VGQALMMKyHGGSATSDAKEME---NAgkTAMEAIENIRTVQALTLQ 907
Cdd:cd18542 154 LFSYVFFK-KVRPAFEEIREQEgelNT--VLQENLTGVRVVKAFARE 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1051-1254 |
2.11e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1051 LNVHVKPGQTLALVGPSGCGKSTVISLLERLYdPLEGAVTVDNNDLRQMNPKHLRKHIALVSQE---PILFDtsireniV 1127
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtpPFAMP-------V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1128 YG-LQpgEYTHEQIETACSKANIHKFIDELpdGYETRVGEKGTQLSGGQKQRIAIARALIR-----NP--KILLLDEATS 1199
Cdd:PRK03695 87 FQyLT--LHQPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1200 ALDTESekqvQVALDA-----AAKDRTCIVVAHRLS-TIVNAGCIMVVKNGQVVEQGTHNE 1254
Cdd:PRK03695 163 SLDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1042-1251 |
2.26e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1042 RPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLE-RLYDP-------LEGAVTVDNNDLRQMNPKHLRKHIALVSQ 1113
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1114 --EPIlFDTSIRENIVYGLQP-----GEYTHEQ---IETACSKAnihkfidelpdGYETRVGEKGTQLSGGQKQRIAIAR 1183
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGRYPharraGALTHRDgeiAWQALALA-----------GATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1184 AL---------IRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAhrlstIVN--------AGCIMVVKNGQV 1246
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLA-----IVHdpnlaarhADRIAMLADGAI 233
|
....*
gi 17558664 1247 VEQGT 1251
Cdd:PRK13547 234 VAHGA 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1009-1230 |
3.89e-13 |
|
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: 74.01 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1009 EEEPRIDGMTSSGTYPQLS------GEVKLNKVFFRYPERPAVP-----ILQGLNVHVKPGQTLALVGPSGCGKSTVISL 1077
Cdd:TIGR00954 418 FKRPRVEEIESGREGGRNSnlvpgrGIVEYQDNGIKFENIPLVTpngdvLIESLSFEVPSGNNLLICGPNGCGKSSLFRI 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1078 LERLYDPLEGAVTVDNndlrqmnpkhlRKHIALVSQEPILFDTSIRENIVYGLQPgeytHEQIETACSKANIHKFIDELP 1157
Cdd:TIGR00954 498 LGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIYPDSS----EDMKRRGLSDKDLEQILDNVQ 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1158 DGY--ETRVGEKGTQ-----LSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKqvqvALDAAAKDR--TCIVVAHR 1228
Cdd:TIGR00954 563 LTHilEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG----YMYRLCREFgiTLFSVSHR 638
|
..
gi 17558664 1229 LS 1230
Cdd:TIGR00954 639 KS 640
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
400-602 |
4.21e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQ-RFYNPDA-------GQILIDDIPIEDFNIKYLRQLVGVVSQ--EPN 469
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 470 lFNTSIEQNIRYGR---------SDVSDEDIA-RALKEANAAdfiktfpeglnTLVGDRGVQMSGGQKQRIAIARAL--- 536
Cdd:PRK13547 96 -FAFSAREIVLLGRypharragaLTHRDGEIAwQALALAGAT-----------ALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 537 ------VRNPKILLLDEATSALDAESESIVQSALENASR----GRTTIVIAHRLSTvRNADKIIVMKAGQVMEVGT 602
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGA 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
384-578 |
7.96e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.66 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPtrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLqrfynpdAGqilIDdipiEDFNIKYLRQL--- 460
Cdd:TIGR03719 6 TMNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD----KDFNGEARPQPgik 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 461 VGVVSQEPNLFNT-SIEQNIRYGRSDVSD-----EDIARALKEANAaDFIKTFPE------------------------- 509
Cdd:TIGR03719 70 VGYLPQEPQLDPTkTVRENVEEGVAEIKDaldrfNEISAKYAEPDA-DFDKLAAEqaelqeiidaadawdldsqleiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 510 GLNTLVGDRGVQ-MSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASrGrTTIVIAH 578
Cdd:TIGR03719 149 ALRCPPWDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP-G-TVVAVTH 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
381-595 |
9.58e-13 |
|
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: 68.42 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 381 GRISVNKVEFTYPTRADVK-ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL-QRfynPDA----GQILIDDIPIEdfni 454
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAgvitGEILINGRPLD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 455 KYLRQLVGVVSQEPNLFNTS-IEQNIRYgrsdvsdediaralkEANAadfiktfpeglntlvgdRGvqMSGGQKQRIAIA 533
Cdd:cd03232 75 KNFQRSTGYVEQQDVHSPNLtVREALRF---------------SALL-----------------RG--LSVEQRKRLTIG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 534 RALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTV--RNADKIIVMKAG 595
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
400-601 |
9.60e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQ-RFY-NPDAGQILIDDIPIedfnIKYLRQLVGVVSQEPNLF-NTSIE 476
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKP----TKQILKRTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 477 QNI------RYGRSDVSDEDIARAlkEANAADFIKTFPEglNTLVGD---RGVqmSGGQKQRIAIARALVRNPKILLLDE 547
Cdd:PLN03211 159 ETLvfcsllRLPKSLTKQEKILVA--ESVISELGLTKCE--NTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 548 ATSALDAESE-SIVQSALENASRGRTTIVIAHRLST--VRNADKIIVMKAGQVMEVG 601
Cdd:PLN03211 233 PTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1031-1250 |
1.02e-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: 68.44 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKST---VISLLERLYDPLEGAVTVDNNDLRQMNPKHlRKH 1107
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKY-PGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 IALVSQEPILFDT-SIRENivyglqpgeytheqIETACsKANIHKFIdelpdgyetrvgeKGtqLSGGQKQRIAIARALI 1186
Cdd:cd03233 85 IIYVSEEDVHFPTlTVRET--------------LDFAL-RCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1187 RNPKILLLDEATSALDTESekqvqvALDAAAKDRTCivvAHRLSTIVNAGC-------------IMVVKNGQVVEQG 1250
Cdd:cd03233 135 SRASVLCWDNSTRGLDSST------ALEILKCIRTM---ADVLKTTTFVSLyqasdeiydlfdkVLVLYEGRQIYYG 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
410-602 |
1.16e-12 |
|
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: 67.01 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 410 PGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIddipiedfnikylrqlvgvvsqepnlfntsieqnirygrsdVSDE 489
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 490 DIARALKEANaadfiktfpegLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENAS- 568
Cdd:smart00382 40 DILEEVLDQL-----------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17558664 569 ------RGRTTIVIAHRLSTVRnaDKIIVMKAGQVMEVGT 602
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLL 146
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
706-864 |
1.23e-12 |
|
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: 70.11 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIINVFSNPDRDQMKkDGHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSK 785
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQ-GLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 786 VYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAV 864
Cdd:cd18544 80 LFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1046-1252 |
1.57e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.05 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLL--ERLYDPLEGAVTVDNNDLRQMNPK-HLRKHIALVSQEPI------ 1116
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEdRAGEGIFMAFQYPVeipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 ---LFDTSIRENIVYGLQPgeytheqietACSKANIHKFIDE------LPDGYETRVGEKGtqLSGGQKQRIAIARALIR 1187
Cdd:PRK09580 95 nqfFLQTALNAVRSYRGQE----------PLDRFDFQDLMEEkiallkMPEDLLTRSVNVG--FSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1188 NPKILLLDEATSALDTESEKQVQVALDAAAK-DRTCIVVAH--RLSTIVNAGCIMVVKNGQVVEQGTH 1252
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1030-1255 |
1.79e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.02 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL---RK 1106
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1107 HIALVSQEPILF-DTSIRENIVYGLQpgeyTHEQIETACSKANIHKFIDElpdgyetrVGEKG------TQLSGGQKQRI 1179
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLR----EHTQLPAPLLHSTVMMKLEA--------VGLRGaaklmpSELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1180 AIARALIRNPKILLLDEATSALDTESEKQVQVALDA--AAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
395-604 |
2.15e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDD----------IPIEDFNIKYLRQLVG-- 462
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 --VVSQEP----NLFNTSIEQ---NIRYGRSDVSDEdiarALKEANAADFIKTFPEGlNTLVGDRGVQMSGGQKQRIAIA 533
Cdd:PRK10261 106 maMIFQEPmtslNPVFTVGEQiaeSIRLHQGASREE----AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 534 RALVRNPKILLLDEATSALD----AESESIVQSALENASRGrtTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHE 604
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMYQGEAVETGSVE 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1025-1245 |
2.71e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1025 QLSGevkLNKVFfryperPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHL 1104
Cdd:PRK10762 6 QLKG---IDKAF------PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1105 RKH-IALVSQEPILFDT-SIRENIVYGlqpgeythEQIETACSKANIHKFIDE---------LPDGYETRVGEkgtqLSG 1173
Cdd:PRK10762 77 QEAgIGIIHQELNLIPQlTIAENIFLG--------REFVNRFGRIDWKKMYAEadkllarlnLRFSSDKLVGE----LSI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1174 GQKQRIAIARALIRNPKILLLDEATSAL-DTESEKQVQVALDAAAKDRTCIVVAHRLSTIVNAgC--IMVVKNGQ 1245
Cdd:PRK10762 145 GEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIFEI-CddVTVFRDGQ 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
404-604 |
2.88e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.39 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 404 VSLDAQPGQTVALVGSSGCGKS----TIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG----VVSQEPNlfnTSI 475
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPM---TSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNIRYGRSdvsdedIARALK--EANAADFIKTFPEGLNTLVG--DRGV-------QMSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK11022 103 NPCYTVGFQ------IMEAIKvhQGGNKKTRRQRAIDLLNQVGipDPASrldvyphQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 545 LDEATSALDAESES-IVQSALENASRGRTTIV-IAHRLSTV-RNADKIIVMKAGQVMEVGTHE 604
Cdd:PRK11022 177 ADEPTTALDVTIQAqIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAH 239
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
713-942 |
3.05e-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: 68.88 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 713 ALIQGAVMPAFSLFFS-QIIN-VFSNPDRDQMKKdghfwALMFLVLAAVqGTSMLFQC--SLFGVAAERLTMRIRSKVYR 788
Cdd:cd18784 4 FLLAAAVGEIFIPYYTgQVIDgIVIEKSQDKFSR-----AIIIMGLLAI-ASSVAAGIrgGLFTLAMARLNIRIRNLLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 789 NVLRQDATYFDMPKhsPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVgqal 868
Cdd:cd18784 78 SIVSQEIGFFDTVK--TGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAI---- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 869 MMKYHGGSATSDAKEMEN----AGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGGNISKAIIRGlTYGFANSI 942
Cdd:cd18784 152 VSKVYGDYYKKLSKAVQDslakANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNEL 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1049-1226 |
3.05e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1049 QGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIRENIVY 1128
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1129 gLQP--GEYTHEQIETACSKANIHKFIDeLPDGyetrvgekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESE 1206
Cdd:PRK13538 98 -YQRlhGPGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|
gi 17558664 1207 KQVQVALDAAAKDRTCIVVA 1226
Cdd:PRK13538 166 ARLEALLAQHAEQGGMVILT 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
383-552 |
3.88e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNI-KYLRQLV 461
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 462 GVVSQEPNLFN-TSIEQNIRYGRSDVSDEDIARALKEAnaadfIKTFPEgLNTLVGDRGVQMSGGQKQRIAIARALVRNP 540
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV-----YELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 17558664 541 KILLLDEATSAL 552
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1031-1225 |
5.56e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPErpavpiLQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLY--DPLEGA------VTVDNNDLRQMNPK 1102
Cdd:PRK09984 9 KLAKTFNQHQA------LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShiellgRTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1103 HLRKHIALVSQEPILFDT-SIRENIVYGLQPGEYTHEQIETACSKANIHKFIDELpdgyeTRVG------EKGTQLSGGQ 1175
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1176 KQRIAIARALIRNPKILLLDEATSALDTESEKQVQVAL-DAAAKDRTCIVV 1225
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrDINQNDGITVVV 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1058-1227 |
6.27e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 67.05 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1058 GQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDlrqmnpkhlrkhialVSQEP----ILFDTSIREnIVYGLQPG 1133
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSYKPqyikADYEGTVRD-LLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1134 EYTHEQIETACSKA-NIHKFID-ELPDgyetrvgekgtqLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQV 1211
Cdd:cd03237 89 FYTHPYFKTEIAKPlQIEQILDrEVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170
....*....|....*...
gi 17558664 1212 ALD--AAAKDRTCIVVAH 1227
Cdd:cd03237 157 VIRrfAENNEKTAFVVEH 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
398-596 |
8.16e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKY-LRQLVGVVSQEPNLF-NTSI 475
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVlQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 EQNIRYGRSDVS----DEDiaralKEANaaDFIKTFPE-GLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATS 550
Cdd:PRK10982 91 MDNMWLGRYPTKgmfvDQD-----KMYR--DTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17558664 551 ALdAESE-----SIVQSALEnasRGRTTIVIAHRLSTVRN-ADKIIVMKAGQ 596
Cdd:PRK10982 164 SL-TEKEvnhlfTIIRKLKE---RGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1057-1232 |
8.67e-12 |
|
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: 64.32 E-value: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1057 PGQTLALVGPSGCGKSTVISLLERLYDPLEGAVtvdnndlrqmnpkhlrkhialvsqepILFDTSIRENIVYGLQPGEYt 1136
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDILEEVLDQLLLII- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1137 heqietacskanihkfidelpdgyetrVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAA 1216
Cdd:smart00382 54 ---------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR 106
|
170 180
....*....|....*....|...
gi 17558664 1217 A-------KDRTCIVVAHRLSTI 1232
Cdd:smart00382 107 LllllkseKNLTVILTTNDEKDL 129
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
398-1205 |
9.04e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL----QRFYNPDAGQILIDDIPIEDFnIKYLRQLVGVVSQEPNLF-N 472
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFpH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 473 TSIEQNIRYG--------RSD-VSDEDIARALKEANAADFiktfpeGL----NTLVGD---RGVqmSGGQKQRIAIARAL 536
Cdd:TIGR00956 153 LTVGETLDFAarcktpqnRPDgVSREEYAKHIADVYMATY------GLshtrNTKVGNdfvRGV--SGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 537 VRNPKILLLDEATSALDAesesivQSALENASRGRTTIVIAHRLSTV------RNA----DKIIVMKAGQVMEVG-THET 605
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDS------ATALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGpADKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 606 LIEQKGLYHELVHAQVFAD----VDDkPK----KKEAERRMSRQTSQR----KGSVNFKTQESQVDEKPGAPPAPEaaek 673
Cdd:TIGR00956 299 KQYFEKMGFKCPDRQTTADfltsLTS-PAerqiKPGYEKKVPRTPQEFetywRNSPEYAQLMKEIDEYLDRCSESD---- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 674 eikrlKKELEEEGAVK-------------ANLFKILRY--ARPEW------IYIFFAIIAALIQGAVmpAFSLFFsqiin 732
Cdd:TIGR00956 374 -----TKEAYRESHVAkqskrtrpsspytVSFSMQVKYclARNFLrmkgnpSFTLFMVFGNIIMALI--LSSVFY----- 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 733 vfsnpdRDQMKKDGHFW---ALMFlvlaavqgtSMLFqCSLFGVAAERLTMRIRSKVYRNvlRQDATYfdmpkhspgrit 809
Cdd:TIGR00956 442 ------NLPKNTSDFYSrggALFF---------AILF-NAFSSLLEIASMYEARPIVEKH--RKYALY------------ 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 810 tRLATDA-PNIKSAIDYRL--GSIFNAIASVGGGL----GIAFYYgwqmaFLVMAIFPFMAVGqalMMKYHGGSATSDAK 882
Cdd:TIGR00956 492 -HPSADAiASIISEIPFKIieSVVFNIILYFMVNFrrtaGRFFFY-----LLILFICTLAMSH---LFRSIGAVTKTLSE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 883 EMENAGKTAME-------AIEN---------IRTVQ--ALTLQTKLYNIF------CSHLdAPHGGNISkaiirglTYGF 938
Cdd:TIGR00956 563 AMTPAAILLLAlsiytgfAIPRpsmlgwskwIYYVNplAYAFESLMVNEFhgrrfeCSQY-VPSGGGYD-------NLGV 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 939 ANSIQFFTYAaafrfglfLIFDKNVLmePENVLRVLFAISFS-----FG-TIGFAASYFPEYIKAT-FAAG-------LI 1004
Cdd:TIGR00956 635 TNKVCTVVGA--------EPGQDYVD--GDDYLKLSFQYYNShkwrnFGiIIGFTVFFFFVYILLTeFNKGakqkgeiLV 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1005 F---------NMLEEEP--RID---GMTSSGTYPQLSGEVKLNKVFFRYPERPAV-----------------PILQGLNV 1053
Cdd:TIGR00956 705 FrrgslkrakKAGETSAsnKNDieaGEVLGSTDLTDESDDVNDEKDMEKESGEDIfhwrnltyevkikkekrVILNNVDG 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1054 HVKPGQTLALVGPSGCGKSTvisLLERLYDPLEGAVTVDNNDLRQMNP--KHLRKHIALVSQEPILFDTS-IRENIVYGL 1130
Cdd:TIGR00956 785 WVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLVNGRPldSSFQRSIGYVQQQDLHLPTStVRESLRFSA 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1131 ---QPGEytheqietaCSKANIHKFIDELPDGYETR------VGEKGTQLSGGQKQRIAIARALIRNPKILL-LDEATSA 1200
Cdd:TIGR00956 862 ylrQPKS---------VSKSEKMEYVEEVIKLLEMEsyadavVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
....*
gi 17558664 1201 LDTES 1205
Cdd:TIGR00956 933 LDSQT 937
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
362-581 |
1.25e-11 |
|
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: 69.01 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 362 RIPEIDAYSTEGQTPSKISGRISV----NKVEF-TYP--TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRF 434
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRGIVeyqdNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 435 YNPDAGQILIDdipiEDFNIKYlrqlvgvVSQEPNLFNTSIEQNIRY-------GRSDVSDEDIARALKEANAADFIKTf 507
Cdd:TIGR00954 502 WPVYGGRLTKP----AKGKLFY-------VPQRPYMTLGTLRDQIIYpdssedmKRRGLSDKDLEQILDNVQLTHILER- 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 508 pEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENAsrGRTTIVIAHRLS 581
Cdd:TIGR00954 570 -EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
390-578 |
1.58e-11 |
|
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: 65.89 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 390 FTYPTRadVKILKGVSLDAQPG-----QTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDdipiedfnikylrqlVGVV 464
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE---------------LDTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 465 SQEPNLFNTSIEQNIRYGRSDVSDEDIARALKEANAADfiktfPEGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILL 544
Cdd:cd03237 64 SYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTEIAK-----PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 17558664 545 LDEATSALDAESESIVQSAL----ENASrgRTTIVIAH 578
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIrrfaENNE--KTAFVVEH 174
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1043-1257 |
1.70e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.88 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1043 PAVPILQGLNVHVKPGQTLALVGPSGCGKS-TVISLLERLydP-----LEGAVTVDNndlRQMNPKHLR-KHIALVSQEP 1115
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PagvrqTAGRVLLDG---KPVAPCALRgRKIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1116 -ILFD------TSIRENI-VYGLQPGEYTHEQIETACSKANIHKFIDELPdgyetrvgekgTQLSGGQKQRIAIARALIR 1187
Cdd:PRK10418 89 rSAFNplhtmhTHARETClALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1188 NPKILLLDEATSALDTESEKQVQVALDAAAKDRT--CIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
397-611 |
1.77e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLqrfynpdAG----QILIDDIPIEDFNIKYL----RQLVGVVSQep 468
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-------AGhpayKILEGDILFKGESILDLepeeRAHLGIFLA-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 469 nlFNTSIEQNirygrsDVSDEDIARA----------LKEANAADFIKTFPEGLNtLVG------DRGVQ--MSGGQKQRI 530
Cdd:CHL00131 90 --FQYPIEIP------GVSNADFLRLaynskrkfqgLPELDPLEFLEIINEKLK-LVGmdpsflSRNVNegFSGGEKKRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 531 AIARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAH--RLSTVRNADKIIVMKAGQVMEVGTHE--T 605
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaK 240
|
....*.
gi 17558664 606 LIEQKG 611
Cdd:CHL00131 241 ELEKKG 246
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
383-587 |
1.98e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 383 ISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVG 462
Cdd:PRK13540 2 LDVIELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQ---EPNLfntSIEQN----IRYGRSDVSDEDIARALKEANAADfiktFPEGLntlvgdrgvqMSGGQKQRIAIARA 535
Cdd:PRK13540 79 VGHRsgiNPYL---TLRENclydIHFSPGAVGITELCRLFSLEHLID----YPCGL----------LSSGQKRQVALLRL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 536 LVRNPKILLLDEATSALDAES-ESIVQSALENASRGRTTIVIAHRLSTVRNAD 587
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1046-1251 |
2.17e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLL--ERLYDPLEGAVTVDNNDLRQMNPK---HL---------------- 1104
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEeraHLgiflafqypieipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1105 ------------RKHIALVSQEPILFDTSIRENI-VYGLQPgeytheqietacskANIHKFIDElpdGYetrvgekgtql 1171
Cdd:CHL00131 101 nadflrlaynskRKFQGLPELDPLEFLEIINEKLkLVGMDP--------------SFLSRNVNE---GF----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1172 SGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIV-VAH--RLSTIVNAGCIMVVKNGQVVE 1248
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
...
gi 17558664 1249 QGT 1251
Cdd:CHL00131 233 TGD 235
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
137-353 |
2.22e-11 |
|
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: 66.34 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 137 RFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLLTLIMMSLSPFM 216
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 217 MICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFLIGA-------- 288
Cdd:cd18589 150 LLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVsmwtssfs 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 289 GLASFFVIIYasyclafwVGTNFVYSGRLESGTVLTVFFSVMMGSMALGQAGQQFATIGTALGAA 353
Cdd:cd18589 230 GLALKVGILY--------YGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSS 286
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
404-629 |
4.00e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 404 VSLDAQPGQTVALVGSSGCGKSTiiqLLQRFYN--PDAGQILIDDIPIEDFNIKYLRQLVGVVSQEPN-LFNTSIEQ--- 477
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQylt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 478 -------NIRYGRSDVsdEDIARALKEANAadfiktfpegLNTLVGdrgvQMSGGQKQRIAIARALVR-----NP--KIL 543
Cdd:PRK03695 92 lhqpdktRTEAVASAL--NEVAEALGLDDK----------LGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 544 LLDEATSALDAESESIVQSAL-ENASRGRTTIVIAHRLS-TVRNADKIIVMKAGQVMEVGTHETLIEQKGLyhelvhAQV 621
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLsELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL------AQV 229
|
250
....*....|....
gi 17558664 622 FA------DVDDKP 629
Cdd:PRK03695 230 FGvnfrrlDVEGHP 243
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
705-914 |
4.11e-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: 65.57 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 705 YIFFAIIAALIQGAVMPAFSLFFSQIInvfsnpDRDQMKKDGH---FWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMR 781
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAI------DEYIPNGDLSgllIIALLFLALNLVNWVASRLRIYLMAKVGQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 782 IRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPF 861
Cdd:cd18545 75 LRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 862 MAVGqALMMKYHGGSATSDAKEMeNAGKTAM--EAIENIRTVQALTLQTKLYNIF 914
Cdd:cd18545 153 LVLV-VFLLRRRARKAWQRVRKK-ISNLNAYlhESISGIRVIQSFAREDENEEIF 205
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
709-919 |
4.91e-11 |
|
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: 65.26 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 709 AIIAALIQGAVMPAFSLFFSQIINVFSnpdRDQMKKDGHFW------ALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRI 782
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVIS---RSLKETNGDFIedlkkpALKLLGLYLLQSLLTFAYISLLSVVGERVAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 783 RSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFM 862
Cdd:cd18574 78 RNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 863 AVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLD 919
Cdd:cd18574 156 VLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVE 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1042-1204 |
5.73e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1042 RPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKhlrKHIALVSQEPIL-FDT 1120
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLkADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVY--GLQpGEYTHEQIETACSkanihkfIDELPDGYETRVgekgTQLSGGQKQRIAIARALIRNPKILLLDEAT 1198
Cdd:PRK13543 98 STLENLHFlcGLH-GRRAKQMPGSALA-------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....*.
gi 17558664 1199 SALDTE 1204
Cdd:PRK13543 166 ANLDLE 171
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1043-1247 |
6.00e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1043 PAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH-LRKHIALVSQE-PILFDT 1120
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1121 SIRENIVYGLQP--GEYTHEQIETACSKAnihkFIDELPDGYETRvgEKGTQLSGGQKQRIAIARALIRNPKILLLDEAT 1198
Cdd:PRK10982 89 SVMDNMWLGRYPtkGMFVDQDKMYRDTKA----IFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1199 SALdteSEKQVQ--VALDAAAKDRTC--IVVAHRLSTIVNAgC--IMVVKNGQVV 1247
Cdd:PRK10982 163 SSL---TEKEVNhlFTIIRKLKERGCgiVYISHKMEEIFQL-CdeITILRDGQWI 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
384-556 |
6.32e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 384 SVNKVEFTYPtrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLqrfynpdAGqilIDD------IPIEDFNIKYL 457
Cdd:PRK11819 8 TMNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VDKefegeaRPAPGIKVGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 458 rqlvgvvSQEPNLFNT-SIEQNIRYGRSDVSD-----EDIARALKEANAaDFIKTFPE-----------GLNTLvgDRGV 520
Cdd:PRK11819 76 -------PQEPQLDPEkTVRENVEEGVAEVKAaldrfNEIYAAYAEPDA-DFDALAAEqgelqeiidaaDAWDL--DSQL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 521 QM-----------------SGGQKQRIAIARALVRNPKILLLDEATSALDAES 556
Cdd:PRK11819 146 EIamdalrcppwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1046-1205 |
6.56e-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: 63.03 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLL-ERLYDPL-EGAVTVDNndlrQMNPKHLRKHIALVSQEPILFDTS-I 1122
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING----RPLDKNFQRSTGYVEQQDVHSPNLtV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1123 RENIVYglqpgeytheqieTACSKAnihkfidelpdgyetrvgekgtqLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:cd03232 97 REALRF-------------SALLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
...
gi 17558664 1203 TES 1205
Cdd:cd03232 141 SQA 143
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1030-1228 |
6.95e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRyperpavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLY--DPLEGAVTVDNNDLRQmnpkhlrkh 1107
Cdd:COG2401 36 VELRVVERY--------VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1108 ialvsqepilfDTSIRENIVYGLQPGEYTheQIETACSkanihkfideLPDG--YETRVGEkgtqLSGGQKQRIAIARAL 1185
Cdd:COG2401 99 -----------EASLIDAIGRKGDFKDAV--ELLNAVG----------LSDAvlWLRRFKE----LSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17558664 1186 IRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHR 1228
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgiTLVVATHH 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
398-578 |
6.97e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQ-----TVALVGSSGCGKSTIIQLLQRFYNPDAGQIliddipieDFNIKylrqlvgvVSQEPnlfn 472
Cdd:PRK13409 347 TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK--------ISYKP---- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 473 tsieQNIRyGRSDVSDEDIARALKEANAADFIKT---FPEGLNTLVgDRGV-QMSGGQKQRIAIARALVRNPKILLLDEA 548
Cdd:PRK13409 407 ----QYIK-PDYDGTVEDLLRSITDDLGSSYYKSeiiKPLQLERLL-DKNVkDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 549 TSALDAESESIVQSALEN--ASRGRTTIVIAH 578
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRiaEEREATALVVDH 512
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1030-1214 |
8.04e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLlerlydplegaVTVD-----NNDL----RQMN 1100
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL-----------ITGDhpqgySNDLtlfgRRRG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1101 PKH----LRKHIALVSQEPIL---FDTSIRENIVYGL--QPGEYtheqieTACSKANiHKFIDELPD--GYETRVGEKGT 1169
Cdd:PRK10938 327 SGEtiwdIKKHIGYVSSSLHLdyrVSTSVRNVILSGFfdSIGIY------QAVSDRQ-QKLAQQWLDilGIDKRTADAPF 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17558664 1170 Q-LSGGQkQRIA-IARALIRNPKILLLDEATSALDTESEKQVQVALD 1214
Cdd:PRK10938 400 HsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD 445
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
706-914 |
2.44e-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: 63.23 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIqgavMPAFSL---FFSQII--NVFSNPDRDQMkkdgHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTM 780
Cdd:cd18570 4 LILILLLSLL----ITLLGIagsFFFQILidDIIPSGDINLL----NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 781 RIRSKVYRNVLRQDATYFDmpKHSPGRITTRLaTDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFP 860
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFE--TRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 861 FMAVgqaLMMKYHGGSATSDAKEMENAGKTA---MEAIENIRTVQALTLQTKLYNIF 914
Cdd:cd18570 153 LYIL---IILLFNKPFKKKNREVMESNAELNsylIESLKGIETIKSLNAEEQFLKKI 206
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
132-331 |
2.75e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 62.91 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 132 EKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLLTLIMMS 211
Cdd:cd18563 72 ERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 212 LSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKK--------- 282
Cdd:cd18563 152 PVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAeklwatffp 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 283 --SFLIGAGLasffVIIYasyclafWVGTNFVYSGRLESGTvLTVFFSVMM 331
Cdd:cd18563 232 llTFLTSLGT----LIVW-------YFGGRQVLSGTMTLGT-LVAFLSYLG 270
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
708-1001 |
3.86e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 62.50 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 708 FAIIAALIQGAVMPAFSLFFSQIINVFSNPDrDQMKKDGHFWALMFLVLAAVQgtSMLFQCSLFGVaaERLTMRIRS--- 784
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYP-DEPLSEGYLLALALFLVSLLQ--SLLLHQYFFLS--FRLGMRVRSals 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 785 -KVYRNVLRQDATyfDMPKHSPGRITTRLATDAPNIKSAIDYrLGSIFNAIASVGGGLGIAFYY-GWQmAFLVMAIFPFM 862
Cdd:cd18579 76 sLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLF-LHYLWSAPLQIIVALYLLYRLlGWA-ALAGLGVLLLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 863 AVGQALMMKYhggSATSDAKEMENAGK--TAM-EAIENIRTVqaltlqtKLY---NIFCSHLDAPHG---GNISK-AIIR 932
Cdd:cd18579 152 IPLQAFLAKL---ISKLRKKLMKATDErvKLTnEILSGIKVI-------KLYaweKPFLKRIEELRKkelKALRKfGYLR 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 933 GLTYGFANSIQFFtyAAAFRFGLFLIFDKNvlMEPEnvlRVLFAISFsFGTIGFAASYFPEYIKATFAA 1001
Cdd:cd18579 222 ALNSFLFFSTPVL--VSLATFATYVLLGNP--LTAA---KVFTALSL-FNLLRFPLLMLPQAISSLIEA 282
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1048-1251 |
5.25e-10 |
|
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: 61.48 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVI--SLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIAlVSQEPI--------- 1116
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIV-IDQSPIgrtprsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 ----LFDTsIRENIVYGLQPGEYTHEQIE--------------TAC-------SKANIHKFIDELPD---GYeTRVGEKG 1168
Cdd:cd03271 90 tytgVFDE-IRELFCEVCKGKRYNRETLEvrykgksiadvldmTVEealeffeNIPKIARKLQTLCDvglGY-IKLGQPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1169 TQLSGGQKQRIAIARALIR---NPKILLLDEATSALDTESEKQVQVALDA-AAKDRTCIVVAHRLSTIVNAGCIMV---- 1240
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWIIDlgpe 247
|
250
....*....|...
gi 17558664 1241 --VKNGQVVEQGT 1251
Cdd:cd03271 248 ggDGGGQVVASGT 260
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
398-591 |
6.13e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQ-----TVALVGSSGCGKSTIIQLLQRFYNPDAGQIliddipieDFNIKylrqlvgvVSQEPnlfn 472
Cdd:COG1245 348 TKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK--------ISYKP---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 473 tsieqniRYGRSDvSDEDIARALKEANAADFIKTF-------PEGLNTLVgDRGV-QMSGGQKQRIAIARALVRNPKILL 544
Cdd:COG1245 408 -------QYISPD-YDGTVEEFLRSANTDDFGSSYykteiikPLGLEKLL-DKNVkDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17558664 545 LDEATSALDAESESIVQSALEN--ASRGRTTIVIAHRLSTVRN-ADKIIV 591
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRRfaENRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1030-1261 |
7.53e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTvdnndlrqmNPKHLRkhIA 1109
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEpILFDTSIRENI--VYGLQPGeYTHEQIETACSKANIHKFIDElpdgyetrvgeKGTQLSGGQKQRIAIARALIR 1187
Cdd:PRK09544 71 YVPQK-LYLDTTLPLTVnrFLRLRPG-TKKEDILPALKRVQAGHLIDA-----------PMQKLSGGETQRVLLARALLN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1188 NPKILLLDEATSALDTESekqvQVAL----DAAAKDRTCIV--VAHRLSTIVNAGCIMVVKNGQVVEQGT------HNEL 1255
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNG----QVALydliDQLRRELDCAVlmVSHDLHLVMAKTDEVLCLNHHICCSGTpevvslHPEF 213
|
....*....
gi 17558664 1256 IA---KRGA 1261
Cdd:PRK09544 214 ISmfgPRGA 222
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
706-872 |
9.86e-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: 61.27 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIINVFSNPDRDQMKKDGH---FWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRI 782
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSgllRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 783 RSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFM 862
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170
....*....|
gi 17558664 863 AVGQALMMKY 872
Cdd:cd18547 159 LLVTKFIAKR 168
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
398-607 |
1.13e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL----QRFYNPDAGQILIDDIPIEDFNIKYLRQLVG----VVSQEPN 469
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGhnvsMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 470 L-------FNTSIEQNI-----------RYG-RSDVSDEDIAR-ALKEANaaDFIKTFPeglntlvgdrgVQMSGGQKQR 529
Cdd:PRK15093 100 ScldpserVGRQLMQNIpgwtykgrwwqRFGwRKRRAIELLHRvGIKDHK--DAMRSFP-----------YELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 530 IAIARALVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKEL 246
|
.
gi 17558664 607 I 607
Cdd:PRK15093 247 V 247
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
398-602 |
1.48e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 398 VKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQrfyNPDAGQILIDDIPIEDFNIKY--LRQLVGVVSQ----EPNLf 471
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA---GRKTGGYIEGDIRISGFPKKQetFARISGYCEQndihSPQV- 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 ntSIEQNIRYGR-----SDVSDEDIARALKEANAADFIKTFPEGLNTLVGDRGvqMSGGQKQRIAIARALVRNPKILLLD 546
Cdd:PLN03140 969 --TVRESLIYSAflrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 547 EATSALDAESESIVQSALENA-SRGRTTIVIAHRLS--TVRNADKIIVMK-AGQVMEVGT 602
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTvDTGRTVVCTIHQPSidIFEAFDELLLMKrGGQVIYSGP 1104
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
750-903 |
1.61e-09 |
|
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: 60.58 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 750 ALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGS 829
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 830 IFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVgqaLMMKYHGGSATSDAKEMENAGK---TAMEAIENIRTVQA 903
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL---ATRWFRRRSSRAYRRARERIAAvnaDLQETLAGIRVVQA 193
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1048-1256 |
1.95e-09 |
|
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: 62.34 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVHVKPGQTLALVGPSGCGKSTVIS--LLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIAlVSQEPI--------- 1116
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIH-IDQSPIgrtprsnpa 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 ----LFDtSIR-------ENIVYGLQPGEYT------------------------------------------------- 1136
Cdd:TIGR00630 703 tytgVFD-EIRelfaetpEAKVRGYTPGRFSfnvkggrceacqgdgvikiemhflpdvyvpcevckgkrynretlevkyk 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1137 ----HEQIETACSKA--------NIHKFIDELPD---GYeTRVGEKGTQLSGGQKQRIAIARALIR---NPKILLLDEAT 1198
Cdd:TIGR00630 782 gkniADVLDMTVEEAyeffeavpSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPT 860
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1199 SALDTESEKQ-VQVALDAAAKDRTCIVVAHRLSTIVNAGCIMV------VKNGQVVEQGTHNELI 1256
Cdd:TIGR00630 861 TGLHFDDIKKlLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDlgpeggDGGGTVVASGTPEEVA 925
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1046-1205 |
2.08e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLL--ERLYDplEGAVTVDNN----DLRQMNPKHlrkhialvsQEPILFD 1119
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILngEVLLD--DGRIIYEQDlivaRLQQDPPRN---------VEGTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TsirenIVYGLQP-GEYTHE------QIETACSKANIHKF------IDELpDGY--ETRVGE-----------KGTQLSG 1173
Cdd:PRK11147 86 F-----VAEGIEEqAEYLKRyhdishLVETDPSEKNLNELaklqeqLDHH-NLWqlENRINEvlaqlgldpdaALSSLSG 159
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 1174 GQKQRIAIARALIRNPKILLLDEATSALDTES 1205
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
139-331 |
2.18e-09 |
|
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: 60.16 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 139 RRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREgtgdkvgLAFQM-------MAQFIGGFAVAFTYDWLLTLIMMS 211
Cdd:cd18549 78 RRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISE-------LAHHGpedlfisIITIIGSFIILLTINVPLTLIVFA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 212 LSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYE---DALEHGKKTGIK------- 281
Cdd:cd18549 151 LLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDegnDRFLESKKKAYKamayffs 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17558664 282 -KSFLIgaGLASFFVIIYASYclafwvgtnFVYSGRLESGTVLTVFFSVMM 331
Cdd:cd18549 231 gMNFFT--NLLNLVVLVAGGY---------FIIKGEITLGDLVAFLLYVNV 270
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
765-958 |
2.32e-09 |
|
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: 60.04 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 765 LFQCSLFgvaaeRLTMRIRSKVYRNVLRQDATYFDMPKhsPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIA 844
Cdd:cd18590 59 LFMCTLS-----RLNLRLRHQLFSSLVQQDIGFFEKTK--TGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 845 FYYGWQMAFLVMAIFPFMAVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQALTLQTKLYNIFCSHLDAPHGG 924
Cdd:cd18590 132 LSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNL 211
|
170 180 190
....*....|....*....|....*....|....
gi 17558664 925 NISKAIIRGLTYGFANSIQFFTYAAAFRFGLFLI 958
Cdd:cd18590 212 KDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLI 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1046-1205 |
2.59e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1046 PILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIALVSQEPILFDTSIREN 1125
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1126 IVYGLQPGEyTHEQIETACSKANIHKFIDeLPDGYetrvgekgtqLSGGQKQRIAIARALIRNPKILLLDEATSALDTES 1205
Cdd:PRK13540 95 CLYDIHFSP-GAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1048-1230 |
3.35e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVhVKPGQTLALVGPSGCGKSTVISLLERlydplegavtvdnndlrQMNPkHLRKHialvsQEPILFDTSIRENIV 1127
Cdd:cd03236 17 LHRLPV-PREGQVLGLVGPNGIGKSTALKILAG-----------------KLKP-NLGKF-----DDPPDWDEILDEFRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1128 YGLQpgEYTHEQIETACSKANIHKFIDELPDGYETRVG-------EKGT-------------------QLSGGQKQRIAI 1181
Cdd:cd03236 73 SELQ--NYFTKLLEGDVKVIVKPQYVDLIPKAVKGKVGellkkkdERGKldelvdqlelrhvldrnidQLSGGELQRVAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17558664 1182 ARALIRNPKILLLDEATSALDTESE-KQVQVALDAAAKDRTCIVVAHRLS 1230
Cdd:cd03236 151 AAALARDADFYFFDEPSSYLDIKQRlNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
395-612 |
3.47e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKG------VSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPI-----------------ED 451
Cdd:PRK11288 257 RLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsprdairagimlcpED 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 452 fnikylRQ---LVGVVSQEPNLfntsieqNIRYGRSDVSDEDIARALKEA-NAADFIKTfpegLNTLVGDRG---VQMSG 524
Cdd:PRK11288 337 ------RKaegIIPVHSVADNI-------NISARRHHLRAGCLINNRWEAeNADRFIRS----LNIKTPSREqliMNLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 525 GQKQRIAIARALVRNPKILLLDEATSALD--AESEsIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVG 601
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGEL 478
|
250
....*....|.
gi 17558664 602 THETLIEQKGL 612
Cdd:PRK11288 479 AREQATERQAL 489
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
394-606 |
3.93e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILID--DIPIEDFNIKY-LRQLVGVVSQEPNL 470
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgeNIPAMSRSRLYtVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 471 FntsieqnirygrSDVSD-EDIARALKEANAadfiktFPEGL--NTL------VGDRGV------QMSGGQKQRIAIARA 535
Cdd:PRK11831 96 F------------TDMNVfDNVAYPLREHTQ------LPAPLlhSTVmmkleaVGLRGAaklmpsELSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 536 LVRNPKILLLDEATSALDAESESIVQSALE--NASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETL 606
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISelNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1032-1205 |
4.13e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.72 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPerPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVtvdnndLRQMNPKhlrkhIALV 1111
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA------RPQPGIK-----VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1112 SQEPILFDT-SIRENIVYGLQP---------------GEYTHEQIETACSKANIHKFID------------------ELP 1157
Cdd:TIGR03719 74 PQEPQLDPTkTVRENVEEGVAEikdaldrfneisakyAEPDADFDKLAAEQAELQEIIDaadawdldsqleiamdalRCP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17558664 1158 DGyETRVgekgTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTES 1205
Cdd:TIGR03719 154 PW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1032-1196 |
4.31e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1032 LNKVFFRYPERP-AV-PIlqglNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKHIA 1109
Cdd:PRK10522 325 LRNVTFAYQDNGfSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDTsireniVYGLQPGEYTHEQIETACSKANI-HKFidELPDGYETRvgekgTQLSGGQKQRIAIARALIRN 1188
Cdd:PRK10522 401 AVFTDFHLFDQ------LLGPEGKPANPALVEKWLERLKMaHKL--ELEDGRISN-----LKLSKGQKKRLALLLALAEE 467
|
....*...
gi 17558664 1189 PKILLLDE 1196
Cdd:PRK10522 468 RDILLLDE 475
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
741-872 |
5.32e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 59.06 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 741 QMKKDGHFWALMFLV--LAAVQGTSMLFQCS---LFGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLATD 815
Cdd:cd18563 32 QLGPGGNTSLLLLLVlgLAGAYVLSALLGILrgrLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSD 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 816 APNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVGQALMMKY 872
Cdd:cd18563 110 TDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKK 166
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1055-1202 |
6.79e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.18 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1055 VKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNdlrqmnpkhlrKHIALVSQEPILFDTSIRENIVyglqPGE 1134
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-----------WQLAWVNQETPALPQPALEYVI----DGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1135 YTHEQIETACSKAN----------IHKFIDELpDGYETR---------VGEKGTQL-------SGGQKQRIAIARALIRN 1188
Cdd:PRK10636 89 REYRQLEAQLHDANerndghaiatIHGKLDAI-DAWTIRsraasllhgLGFSNEQLerpvsdfSGGWRMRLNLAQALICR 167
|
170
....*....|....
gi 17558664 1189 PKILLLDEATSALD 1202
Cdd:PRK10636 168 SDLLLLDEPTNHLD 181
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
397-608 |
7.82e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL-QRFynpDAGQILIDDIPI------EDF--NIKYLRQlvgvvsQE 467
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVITGGDRLVngrpldSSFqrSIGYVQQ------QD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 PNLFNTSIEQNIRYGR-----SDVSD-------EDIARALKEANAADFIKTFP-EGLNTlvgdrgvqmsgGQKQRIAIAR 534
Cdd:TIGR00956 846 LHLPTSTVRESLRFSAylrqpKSVSKsekmeyvEEVIKLLEMESYADAVVGVPgEGLNV-----------EQRKRLTIGV 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 535 ALVRNPKILL-LDEATSALDAESE-SIVQSALENASRGRTTIVIAHRLSTVRNA--DKIIVM-KAGQVM---EVGTH-ET 605
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQTAwSICKLMRKLADHGQAILCTIHQPSAILFEefDRLLLLqKGGQTVyfgDLGENsHT 994
|
...
gi 17558664 606 LIE 608
Cdd:TIGR00956 995 IIN 997
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1045-1225 |
8.10e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1045 VPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKHLRKH-IALVSQEP-----ILf 1118
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrglVP- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1119 DTSIRENIVygLqpGEYTHEQIETAC--SKANIHKFIDEL-------PDGYETRVGekgtQLSGGQKQRIAIARALIRNP 1189
Cdd:COG3845 350 DMSVAENLI--L--GRYRRPPFSRGGflDRKAIRAFAEELieefdvrTPGPDTPAR----SLSGGNQQKVILARELSRDP 421
|
170 180 190
....*....|....*....|....*....|....*.
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALDAAAKDRTCIVV 1225
Cdd:COG3845 422 KLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1050-1255 |
9.59e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.69 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1050 GLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnPKHL--RKHIALVSQEPILF-DTSIRENI 1126
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQiaRMGVVRTFQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1127 VYGlqpgeyTHEQIET----------ACSKANIHKFidELPDGYETRVG-------EKGTqLSGGQKQRIAIARALIRNP 1189
Cdd:PRK11300 102 LVA------QHQQLKTglfsgllktpAFRRAESEAL--DRAATWLERVGllehanrQAGN-LAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1190 KILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNEL 1255
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1055-1250 |
1.04e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1055 VKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVdnndLRQMNPKHLRKH-IALVSQE-------PILFdtsirENI 1126
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNlVAYVPQSeevdwsfPVLV-----EDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1127 V----YG-----LQPGEYTHEQIETACSKANIHKFidelpdgYETRVGEkgtqLSGGQKQRIAIARALIRNPKILLLDEA 1197
Cdd:PRK15056 101 VmmgrYGhmgwlRRAKKRDRQIVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1198 TSALDTESEKQVqVALDAAAKD--RTCIVVAHRLSTIVNAGCIMVVKNGQVVEQG 1250
Cdd:PRK15056 170 FTGVDVKTEARI-ISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
115-331 |
1.12e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 57.88 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 115 GIFAAGFLQASCFMV---ICEKLSNRF----RRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGdKVGLAFQM 187
Cdd:cd18543 44 LLLALGVAEAVLSFLrryLAGRLSLGVehdlRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 188 MAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLaTAATKEAKQYA--VAgGIAEEVLTSIRTVIAFNGQEYEC 265
Cdd:cd18543 123 LLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRY-FPASRRAQDQAgdLA-TVVEESVTGIRVVKAFGRERREL 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 266 KRYEDALEHGKKTGIKKSFLIGAGLASFFVIIYASYCLAFWVGTNFVYSGRLESGTvLTVFFSVMM 331
Cdd:cd18543 201 DRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGT-LVAFSAYLT 265
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
706-871 |
1.27e-08 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 57.79 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIINV-FSNPDRDQMKKdghfWALMFLVLAAVQGTSMLFqCSLFG-VAAERLTMRIR 783
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEgIANGDLSYILR----TGLLMLLLALLGLIAGIL-AGYFAaKASQGFGRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 784 SKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMA 863
Cdd:cd18548 76 KDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILA 153
|
....*...
gi 17558664 864 VGQALMMK 871
Cdd:cd18548 154 LVVFLIMK 161
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
703-864 |
2.60e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 57.10 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 703 WIYIFFAIIAALIQgAVMPafsLFFSQIINVFSNPDRDQMKKdghFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRI 782
Cdd:cd18540 5 ILLIILMLLVALLD-AVFP---LLTKYAIDHFITPGTLDGLT---GFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 783 RSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFM 862
Cdd:cd18540 78 RKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVL 155
|
..
gi 17558664 863 AV 864
Cdd:cd18540 156 AV 157
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
409-581 |
2.73e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 409 QPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQIliDDIPIEDFNIKYLRQlvgvvSQEPNLFNTSIEQNIRYGRSDVSD 488
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPDWDEILDEFRG-----SELQNYFTKLLEGDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 489 EDIARALKeANAADFIKTFPE--GLNTLVG--------DRGV-QMSGGQKQRIAIARALVRNPKILLLDEATSALDAESE 557
Cdd:cd03236 97 DLIPKAVK-GKVGELLKKKDErgKLDELVDqlelrhvlDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|....*
gi 17558664 558 -SIVQSALENASRGRTTIVIAHRLS 581
Cdd:cd03236 176 lNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
706-871 |
2.88e-08 |
|
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: 56.65 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQgAVMPafsLFFSQIINVFSNPDRDQmkKDGHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSK 785
Cdd:cd18541 5 ILFLILVDLLQ-LLIP---RIIGRAIDALTAGTLTA--SQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 786 VYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVG 865
Cdd:cd18541 79 LFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALL 156
|
....*.
gi 17558664 866 QALMMK 871
Cdd:cd18541 157 VYRLGK 162
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1014-1202 |
5.69e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1014 IDGMTSSGTYPQLSGEVKLNKVF--FRYPERPAVPILQ----------GLNVHVKPGQTLALVGPSGCGKSTVISLLERL 1081
Cdd:PRK15439 233 IQAITPAAREKSLSASQKLWLELpgNRRQQAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1082 YDPLEGAVTVDNNDLRQMNPKHlRKHIALV-----SQEPILF-DTSIRENiVYGL---QPGEYTHEQIETA-----CSKA 1147
Cdd:PRK15439 313 RPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYlDAPLAWN-VCALthnRRGFWIKPARENAvleryRRAL 390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 1148 NIhKFIDElpdgyETRVGekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:PRK15439 391 NI-KFNHA-----EQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
401-596 |
6.86e-08 |
|
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: 53.87 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIiqLLQRFYNpDAGQILIDDIPiedfniKYLRQLVGVVSQEPNLFNTSIEQnIR 480
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA-SGKARLISFLP------KFSRNKLIFIDQLQFLIDVGLGY-LT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 481 YGRSdvsdediaralkeanaadfiktfpegLNTLvgdrgvqmSGGQKQRIAIARALVRNPK--ILLLDEATSALDAESES 558
Cdd:cd03238 81 LGQK--------------------------LSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 17558664 559 IVQSALEN-ASRGRTTIVIAHRLSTVRNADKIIVMKAGQ 596
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1051-1232 |
7.68e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1051 LNVH---VKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAV-------------------TVDNNdLRQMNPKhlrkhi 1108
Cdd:PRK13409 355 LEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqyikpdydgTVEDL-LRSITDD------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1109 alvsqepilFDTS-IRENIVYGLQpgeytheqietacskanihkfIDELpdgYETRVGEkgtqLSGGQKQRIAIARALIR 1187
Cdd:PRK13409 428 ---------LGSSyYKSEIIKPLQ---------------------LERL---LDKNVKD----LSGGELQRVAIAACLSR 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17558664 1188 NPKILLLDEATSALDteSEKQVQVALD----AAAKDRTCIVVAHRLSTI 1232
Cdd:PRK13409 471 DADLYLLDEPSAHLD--VEQRLAVAKAirriAEEREATALVVDHDIYMI 517
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1008-1209 |
8.24e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1008 LEEE-PRIDgmtssgtypQLSGEVKLNkvffryperpaVPILQGLNVH-----VKPGQTLALVGPSGCGKStviSLLERL 1081
Cdd:PRK10762 242 LEDQyPRLD---------KAPGEVRLK-----------VDNLSGPGVNdvsftLRKGEILGVSGLMGAGRT---ELMKVL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1082 YDPL---EGAVTVDNNDLRQMNPKH-LRKHIALVSQEP----ILFDTSIRENI-VYGLQPGEYTHEQIETACSKANIHKF 1152
Cdd:PRK10762 299 YGALprtSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSVKENMsLTALRYFSRAGGSLKHADEQQAVSDF 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 1153 ID----ELPdGYETRVGEkgtqLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQV 1209
Cdd:PRK10762 379 IRlfniKTP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI 434
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
418-611 |
9.70e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 418 GSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKyLRQLVGVVSQEPNLFNT-SIEQNIR-----YgrsDVSDEDI 491
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA-TRRRVGYMSQAFSLYGElTVRQNLElharlF---HLPAAEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 492 ARALKEANA----ADFIKTFPEGLntlvgdrgvqmSGGQKQRIAIARALVRNPKILLLDEATSALD-AESESIVQSALEN 566
Cdd:NF033858 375 AARVAEMLErfdlADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLILDEPTSGVDpVARDMFWRLLIEL 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17558664 567 ASRGRTTIVIA-HRLSTVRNADKIIVMKAGQVMEVGTHETLIEQKG 611
Cdd:NF033858 444 SREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1030-1205 |
1.25e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVffrYPerPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNdlrqmnpkhlrKHIA 1109
Cdd:PRK11819 10 NRVSKV---VP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG-----------IKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDT-SIRENIVYGLQP-----GEYthEQI--ETACSKANIHKFIDE-------------------------- 1155
Cdd:PRK11819 74 YLPQEPQLDPEkTVRENVEEGVAEvkaalDRF--NEIyaAYAEPDADFDALAAEqgelqeiidaadawdldsqleiamda 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17558664 1156 --LPDGyETRVgekgTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTES 1205
Cdd:PRK11819 152 lrCPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
393-597 |
1.29e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.99 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 393 PTRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFY-NPDAGQILIDDIPIEDFN-IKYLRQLVGVVSQE--- 467
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 ----PNLfntSIEQNI------RY-GRSDVSDEDIARALKEANAADFIKTFPEGLNTlvgdrgVQMSGGQKQRIAIARAL 536
Cdd:TIGR02633 348 hgivPIL---GVGKNItlsvlkSFcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI------GRLSGGNQQKAVLAKML 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 537 VRNPKILLLDEATSALD--AESEsIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQV 597
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDvgAKYE-IYKLINQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
387-597 |
1.68e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 387 KVEFTYP--------TRADVKILKG-----VSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIE--- 450
Cdd:PRK10762 241 KLEDQYPrldkapgeVRLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrs 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 451 -----DFNIKYL---RQLVGVV---SQEPNLFNTSIEQNIR-YGRSDVSDEDIAralkeanAADFIKTF----PeGLNTL 514
Cdd:PRK10762 321 pqdglANGIVYIsedRKRDGLVlgmSVKENMSLTALRYFSRaGGSLKHADEQQA-------VSDFIRLFniktP-SMEQA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 515 VGdrgvQMSGGQKQRIAIARALVRNPKILLLDEATSALD--AESEsIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIV 591
Cdd:PRK10762 393 IG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgAKKE-IYQLINQFKAEGLSIILVSSEMPEVLGmSDRILV 467
|
....*.
gi 17558664 592 MKAGQV 597
Cdd:PRK10762 468 MHEGRI 473
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
396-625 |
1.97e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIKYLRQLVgvvSQEPNLFNTSI 475
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLV---SDEWQRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 476 -----EQNIRYGRSDVSDEDIARALKEANAADFiktfpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNPKILLLDEATS 550
Cdd:PRK10938 91 lspgeDDTGRTTAEIIQDEVKDPARCEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 551 ALDAESESIVQSALENASRGRTTIV-IAHRLSTVRN-ADKIIVMKAGQVMEVGTHETlIEQKGLYHELVHAQVFADV 625
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREE-ILQQALVAQLAHSEQLEGV 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
409-580 |
2.52e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 409 QPGQTVALVGSSGCGKSTIIQLLqrfynpdAGQIL-----------IDDIpIEDFNIK----YLRQLVG---VVSQEPNL 470
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKIL-------SGELIpnlgdyeeepsWDEV-LKRFRGTelqnYFKKLYNgeiKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 471 fntsIEQNIRYGRSDVSDedIARALKEANAAD-FIKTFpeGLNTLVgDRGV-QMSGGQKQRIAIARALVRNPKILLLDEA 548
Cdd:PRK13409 169 ----VDLIPKVFKGKVRE--LLKKVDERGKLDeVVERL--GLENIL-DRDIsELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 549 TSALDAESESIVQSALENASRGRTTIVIAHRL 580
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
397-609 |
3.60e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.87 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL--QRFYNPDAGQI------LIDDIPIED------FNIKYLRQLVG 462
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVefkgkdLLELSPEDRagegifMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 463 VVSQepNLFNTSIEQNIRYGRSDvsdediarALKEANAADFIK------TFPEGLntLVGDRGVQMSGGQKQRIAIARAL 536
Cdd:PRK09580 93 VSNQ--FFLQTALNAVRSYRGQE--------PLDRFDFQDLMEekiallKMPEDL--LTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 537 VRNPKILLLDEATSALDAESESIVQSALENASRG-RTTIVIAH--RLSTVRNADKIIVMKAGQVMEVGTHeTLIEQ 609
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF-TLVKQ 235
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
410-640 |
4.32e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 410 PGQTVALVGSSGCGKSTIIQLLQRFYNPDAGqiliddipieDFNIKYLRQLVGVVSQEPNLFNTSIEQNIRYGRSDVSDE 489
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGG----------SYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 490 DIARALKEANAADFIKTFPEGLNTL---------------VGDRGVQM-------SGGQKQRIAIARALVRNPKILLLDE 547
Cdd:PRK10636 96 AQLHDANERNDGHAIATIHGKLDAIdawtirsraasllhgLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 548 ATSALDAESESIVQSALENASrgRTTIVIAHR---LSTVrnADKIIVMKAGQVME-VGTHET--------LIEQKGLYH- 614
Cdd:PRK10636 176 PTNHLDLDAVIWLEKWLKSYQ--GTLILISHDrdfLDPI--VDKIIHIEQQSLFEyTGNYSSfevqratrLAQQQAMYEs 251
|
250 260
....*....|....*....|....*....
gi 17558664 615 ---ELVHAQVFADvDDKPKKKEAERRMSR 640
Cdd:PRK10636 252 qqeRVAHLQSYID-RFRAKATKAKQAQSR 279
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
710-910 |
4.34e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 52.98 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 710 IIAALIQGAVMPAFSLFFSQIIN---VFSNPDRDQMkkdghfWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSKV 786
Cdd:cd18782 8 LALSFVVQLLGLANPLLFQVIIDkvlVQQDLATLYV------IGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 787 YRNVLRQDATYFDmpKHSPGRITTRLAtDAPNIKS-AIDYRLGSIFNAIASVGGgLGIAFYYGWQMAFLVMAIFPFMA-- 863
Cdd:cd18782 82 IDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRGfLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLll 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17558664 864 ---VGQALMMKYHggsatsdaKEMENAGKTA---MEAIENIRTVQALTLQTKL 910
Cdd:cd18782 158 tflFGPILRRQIR--------RRAEASAKTQsylVESLTGIQTVKAQNAELKA 202
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
115-325 |
4.61e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 53.34 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 115 GIFAAG----FLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFD---NLERVREGTgdkVGLAFQM 187
Cdd:cd18565 62 AAFLLEslfqYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNdvnQLERFLDDG---ANSIIRV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 188 MAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLataatkEAKQYAV---AGGIA---EEVLTSIRTVIAFNGQ 261
Cdd:cd18565 139 VVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRI------EPRYRAVreaVGDLNarlENNLSGIAVIKAFTAE 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 262 EYECKR-------YEDALEHGKKTGIKKSFLIGAGLASFFVIIyasyclaFWVGTNFVYSGRLESGTVLTV 325
Cdd:cd18565 213 DFERERvadaseeYRDANWRAIRLRAAFFPVIRLVAGAGFVAT-------FVVGGYWVLDGPPLFTGTLTV 276
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1048-1229 |
4.67e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1048 LQGLNVhVKPGQTLALVGPSGCGKSTVISLLERLYDP----LEGAVTVDN--------------NDLRQMNPKHLRKhIA 1109
Cdd:PRK13409 90 LYGLPI-PKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWDEvlkrfrgtelqnyfKKLYNGEIKVVHK-PQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILFDTSIRENIvyglqpgeytheqietacSKANIHKFIDELPD--GYETRVGEKGTQLSGGQKQRIAIARALIR 1187
Cdd:PRK13409 168 YVDLIPKVFKGKVRELL------------------KKVDERGKLDEVVErlGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17558664 1188 NPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRL 1229
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1055-1232 |
4.88e-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: 54.02 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1055 VKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVtvdNNDLR-----Q-MNPK-------HLRKHIAlvsqePILFDTS 1121
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKisykpQyISPDydgtveeFLRSANT-----DDFGSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1122 IRENIVYGLQpgeytheqietacskanihkfIDELpdgYETRVGEkgtqLSGGQKQRIAIARALIRNPKILLLDEATSAL 1201
Cdd:COG1245 435 YKTEIIKPLG---------------------LEKL---LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190
....*....|....*....|....*....|....*
gi 17558664 1202 DteSEKQVQVALD----AAAKDRTCIVVAHRLSTI 1232
Cdd:COG1245 487 D--VEQRLAVAKAirrfAENRGKTAMVVDHDIYLI 519
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
404-597 |
4.97e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 404 VSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDFNIK--------YL---RQLVGVVSQEPNLFN 472
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvYLpedRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 473 T-SIEQN-----IRYGRSDVSDEDIARAL--KEANAADFIKTfpeglntlvgdrgvqMSGGQKQRIAIARALVRNPKILL 544
Cdd:PRK15439 362 VcALTHNrrgfwIKPARENAVLERYRRALniKFNHAEQAART---------------LSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 545 LDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQV 597
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSiAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
397-597 |
6.05e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 397 DVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRfynpdagqilidDIPIEDFNIKYLRQLVgvVS---QEP----- 468
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG------------EVLLDDGRIIYEQDLI--VArlqQDPprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 469 -NLFNTsIEQNI--------RYGR------SDVSDEDIAR------ALKEANAADFIKTFPEGLNTLVGDRGVQM---SG 524
Cdd:PRK11147 81 gTVYDF-VAEGIeeqaeylkRYHDishlveTDPSEKNLNElaklqeQLDHHNLWQLENRINEVLAQLGLDPDAALsslSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 525 GQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENAsRGrTTIVIAHRLSTVRN-ADKIIVMKAGQV 597
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF-QG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1065-1202 |
6.22e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1065 GPSGCGKSTVISLLERLYDPLEGAVT-----VDNNDLRqmnpkhLRKHIALVSQEPILF-DTSIRENIV-----YGLqPG 1133
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIA------TRRRVGYMSQAFSLYgELTVRQNLElharlFHL-PA 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1134 EYTHEQIETACSKANIHKFIDELPDGyetrvgekgtqLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:NF033858 372 AEIAARVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
394-602 |
6.46e-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: 52.23 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQ------LLQRFYNPDAGQILIDDIPiedfNIKYLRQLVgVVSQE 467
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHLKKEQPGNHDRIE----GLEHIDKVI-VIDQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 468 P-------------NLFnTSIEQ----------------NIRY-GRS--DVSDEDIARALkeanaaDFIKTFP---EGLN 512
Cdd:cd03271 79 PigrtprsnpatytGVF-DEIRElfcevckgkrynretlEVRYkGKSiaDVLDMTVEEAL------EFFENIPkiaRKLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 513 TLV---------GDRGVQMSGGQKQRIAIARALVR---NPKILLLDEATSALDAESES----IVQSALENasrGRTTIVI 576
Cdd:cd03271 152 TLCdvglgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKklleVLQRLVDK---GNTVVVI 228
|
250 260 270
....*....|....*....|....*....|..
gi 17558664 577 AHRLSTVRNADKIIVM------KAGQVMEVGT 602
Cdd:cd03271 229 EHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
385-612 |
6.77e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 385 VNKVEFTYPTRadvKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDdipiEDFNIKYLRQLVGV- 463
Cdd:PRK15064 322 VENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS----ENANIGYYAQDHAYd 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 464 VSQEPNLFN--------TSIEQNIR--YGRSDVSDEDIARALKeanaadfiktfpeglntlvgdrgvQMSGGQKQRIAIA 533
Cdd:PRK15064 395 FENDLTLFDwmsqwrqeGDDEQAVRgtLGRLLFSQDDIKKSVK------------------------VLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 534 RALVRNPKILLLDEATSALDAESESIVQSALENaSRGrTTIVIAHRLSTVRN-ADKIIVMKAGQVMEV-GTHETLIEQKG 611
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMALEK-YEG-TLIFVSHDREFVSSlATRIIEITPDGVVDFsGTYEEYLRSQG 528
|
.
gi 17558664 612 L 612
Cdd:PRK15064 529 I 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
380-566 |
6.93e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 380 SGRI--SVNKVEFTYPtraDVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDdipiEDFNIKYL 457
Cdd:PRK11147 315 SGKIvfEMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 458 RQLVGVVSQEpnlfnTSIEQNIRYGRSDVSDEDIARalkeaNAADFIKTF---PEGLNTLVGdrgvQMSGGQKQRIAIAR 534
Cdd:PRK11147 388 DQHRAELDPE-----KTVMDNLAEGKQEVMVNGRPR-----HVLGYLQDFlfhPKRAMTPVK----ALSGGERNRLLLAR 453
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 535 ALVRNPKILLLDEATSALDAESESIVQSALEN 566
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETLELLEELLDS 485
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1159-1256 |
1.32e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1159 GYETRVGekgtQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVN-AG 1236
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTD 459
|
90 100
....*....|....*....|....*
gi 17558664 1237 CIMVVKNGQVV-----EQGTHNELI 1256
Cdd:PRK10982 460 RILVMSNGLVAgivdtKTTTQNEIL 484
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
522-605 |
1.39e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 522 MSGGQKQRIAIARALVRNPKILLLDEATSALD--AESEsIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVM 598
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVA 470
|
....*...
gi 17558664 599 E-VGTHET 605
Cdd:PRK10982 471 GiVDTKTT 478
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
746-865 |
1.43e-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: 51.80 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 746 GHFWALMFLVLAAVQGTSmLFQcSLFGVAAERLTMRI----RSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKS 821
Cdd:cd18565 51 GQLWLLGGLTVAAFLLES-LFQ-YLSGVLWRRFAQRVqhdlRTDTYDHVQRLDMAFFE--DRQTGDLMSVLNNDVNQLER 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17558664 822 AIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVG 865
Cdd:cd18565 127 FLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAG 170
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
706-864 |
1.49e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 51.33 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPafsLFFSQIINV-FSNPDRDQMkkdghFWALMFLV-LAAVQGTSMLFQCSLFGVAAERLTMRIR 783
Cdd:cd18550 4 VLLLILLSALLGLLPP---LLLREIIDDaLPQGDLGLL-----VLLALGMVaVAVASALLGVVQTYLSARIGQGVMYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 784 SKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMA 863
Cdd:cd18550 76 VQLYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
.
gi 17558664 864 V 864
Cdd:cd18550 154 L 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1034-1217 |
1.60e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1034 KVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVI-SLLERLYDPL---EGAVTVDNNDLRQMNpKHLRKHIA 1109
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGFHigvEGVITYDGITPEEIK-KHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1110 LVSQEPILF---------DTSIR----ENIVYGLQPGEYtheqietACSKANIHKFIDELPDGYETRVGE---KGtqLSG 1173
Cdd:TIGR00956 142 YNAETDVHFphltvgetlDFAARcktpQNRPDGVSREEY-------AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSG 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17558664 1174 GQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAA 1217
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSA 256
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
500-607 |
1.64e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 500 AADFIKTFP---EGLNTLVgDRGVQ----------MSGGQKQRIAIARALVR---NPKILLLDEATSALDAES----ESI 559
Cdd:TIGR00630 796 AYEFFEAVPsisRKLQTLC-DVGLGyirlgqpattLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDikklLEV 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17558664 560 VQSALENasrGRTTIVIAHRLSTVRNADKIIVM------KAGQVMEVGTHETLI 607
Cdd:TIGR00630 875 LQRLVDK---GNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEVA 925
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
191-332 |
2.00e-06 |
|
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: 51.29 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 191 FIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYED 270
Cdd:cd18570 129 VIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEK 208
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 271 ALE-------HGKKTGIKKSFLIGAGLASFFVIIyasyclaFWVGTNFVYSGRLESGTVLTvfFSVMMG 332
Cdd:cd18570 209 KFSkllkksfKLGKLSNLQSSIKGLISLIGSLLI-------LWIGSYLVIKGQLSLGQLIA--FNALLG 268
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
409-582 |
2.00e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 409 QPGQTVALVGSSGCGKSTIIQLLqrfynpdAGQIL-----IDDIPIEDFNIKYLRqlvGVVSQepNLFNTSIEQNIRygr 483
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGELKpnlgdYDEEPSWDEVLKRFR---GTELQ--DYFKKLANGEIK--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 484 sdVSD-----EDIARALK-----------EANAAD-FIKTFpeGLNTLVgDRGV-QMSGGQKQRIAIARALVRNPKILLL 545
Cdd:COG1245 162 --VAHkpqyvDLIPKVFKgtvrellekvdERGKLDeLAEKL--GLENIL-DRDIsELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17558664 546 DEATSALD----AESESIVQsalENASRGRTTIVIAHRLST 582
Cdd:COG1245 237 DEPSSYLDiyqrLNVARLIR---ELAEEGKYVLVVEHDLAI 274
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
362-587 |
3.04e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 362 RIPEIDAYSTEGQTPSKISgRISVNKVEFTYptrADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLL-----QRFYN 436
Cdd:PRK10938 241 QLPEPDEPSARHALPANEP-RIVLNNGVVSY---NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGYSN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 437 P--------DAGQILIDdipiedfnIKylrQLVGVVSQEPNL---FNTSIEQNIRYGRSD-------VSDediARALKEA 498
Cdd:PRK10938 317 DltlfgrrrGSGETIWD--------IK---KHIGYVSSSLHLdyrVSTSVRNVILSGFFDsigiyqaVSD---RQQKLAQ 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 499 NAADFIktfpeGLNTLVGDRGVQ-MSGGQkQRIA-IARALVRNPKILLLDEATSALDAESESIVQSALEN-ASRGRTTIV 575
Cdd:PRK10938 383 QWLDIL-----GIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLL 456
|
250 260
....*....|....*....|....
gi 17558664 576 ------------IAHRLSTVRNAD 587
Cdd:PRK10938 457 fvshhaedapacITHRLEFVPDGD 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
355-561 |
3.04e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 355 SLYEVIDRIPEIDA------YSTEGQTPSKISGR--ISVNKVEFTYPTRADV-KILK-GVSLDAQpgqtVALVGSSGCGK 424
Cdd:PLN03073 473 SRIKALDRLGHVDAvvndpdYKFEFPTPDDRPGPpiISFSDASFGYPGGPLLfKNLNfGIDLDSR----IAMVGPNGIGK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 425 STIIQLLQRFYNPDAGQILID-DIPIEDFNIKYLRQLVgvVSQEPNL-----FNTSIEQNIRygrsdvsdediaralkeA 498
Cdd:PLN03073 549 STILKLISGELQPSSGTVFRSaKVRMAVFSQHHVDGLD--LSSNPLLymmrcFPGVPEQKLR-----------------A 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 499 NAADFiktfpeglnTLVGDRGVQ----MSGGQKQRIAIARALVRNPKILLLDEATSALDAES-ESIVQ 561
Cdd:PLN03073 610 HLGSF---------GVTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
139-338 |
3.25e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 50.61 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 139 RRQFFHSVMRQEIAWYDKNTSGTLSNKLF---DNLERV-REGTGDKVGLAFQmmaqFIGGFAVAFTYDWLLTLIMMSLSP 214
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQTGDLMSRVIndvANVERLiADGIPQGITNVLT----LVGVAIILFSINPKLALLTLIPIP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 215 FMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFLIGaglasff 294
Cdd:cd18778 152 FLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWA------- 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17558664 295 viiyasyclAFWVGTNFVYSgrleSGTVLTVFF---SVMMGSMALGQ 338
Cdd:cd18778 225 ---------IFHPLMEFLTS----LGTVLVLGFggrLVLAGELTIGD 258
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
110-353 |
3.47e-06 |
|
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: 50.46 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 110 VYLGC--GIFAAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQM 187
Cdd:cd18544 46 LYLGLllLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 188 MAQFIGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKR 267
Cdd:cd18544 126 LLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 268 YEDALEHGKKTGIkKSFLIGAGLASFFVIIYA-SYCLAFWVGTNFVYSGRLESGtVLTVFFS-VMMGSMALGQAGQQFAT 345
Cdd:cd18544 206 FDEINQEYRKANL-KSIKLFALFRPLVELLSSlALALVLWYGGGQVLSGAVTLG-VLYAFIQyIQRFFRPIRDLAEKFNI 283
|
....*...
gi 17558664 346 IGTALGAA 353
Cdd:cd18544 284 LQSAMASA 291
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1040-1225 |
6.50e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1040 PERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYdP--LEGAVTVDNNDLRQMNPKH-LRKHIALVSQEP- 1115
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDGKPVKIRNPQQaIAQGIAMVPEDRk 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1116 ---ILFDTSIRENIVYGLQPGEYTHEQIETACSKANIHKFIDEL------PdgyETRVGekgtQLSGGQKQRIAIARALI 1186
Cdd:PRK13549 349 rdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLkvktasP---ELAIA----RLSGGNQQKAVLAKCLL 421
|
170 180 190
....*....|....*....|....*....|....*....
gi 17558664 1187 RNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVV 1225
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
520-593 |
8.32e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 8.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 520 VQMSGGQKQRIAIARAL----VRNPKILLLDEATSALDAES-ESIVQSALENASRGRTTIVIAHRLSTVRNADKIIVMK 593
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1055-1225 |
8.73e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.82 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1055 VKPGQTLALVGPSGCGKSTVISLLERLYD-PLEGAVTVDNNDLRQMNP-KHLRKHIALVSQEP----ILFDTSIRENIVY 1128
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPaQAIRAGIAMVPEDRkrhgIVPILGVGKNITL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1129 GLQPGEYTHEQIETACSKANIHKFIDEL------PDGYETRvgekgtqLSGGQKQRIAIARALIRNPKILLLDEATSALD 1202
Cdd:TIGR02633 363 SVLKSFCFKMRIDAAAELQIIGSAIQRLkvktasPFLPIGR-------LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180
....*....|....*....|...
gi 17558664 1203 TESEKQVQVALDAAAKDRTCIVV 1225
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIV 458
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1031-1262 |
9.95e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1031 KLNKVFFRYPERPAVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGavTVDnndlrqmnpkhLRKHIAL 1110
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG--TVD-----------IKGSAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQEPILFD--TSIrENI-VYGLQPGeYTHEQIETACSK----ANIHKFIDELPDGYetrvgekgtqlSGGQKQRIAIAR 1183
Cdd:PRK13545 90 IAISSGLNGqlTGI-ENIeLKGLMMG-LTKEKIKEIIPEiiefADIGKFIYQPVKTY-----------SSGMKSRLGFAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1184 ALIRNPKILLLDEATSALD-TESEKQVQVALDAAAKDRTCIVVAHRLSTiVNAGCI--MVVKNGQVVEQGTHNELIAKRG 1260
Cdd:PRK13545 157 SVHINPDILVIDEALSVGDqTFTKKCLDKMNEFKEQGKTIFFISHSLSQ-VKSFCTkaLWLHYGQVKEYGDIKEVVDHYD 235
|
..
gi 17558664 1261 AY 1262
Cdd:PRK13545 236 EF 237
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
396-602 |
1.18e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 396 ADVKILKGVSLDAQPGQTVALVGSSGCGKSTIiQLLQRFYNPDAGQIliddiPIEDF----NIKYLRQLVGVvsqepnlf 471
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRR-----PWRF*twcaNRRALRRTIG*-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 472 ntsiEQNIRYGRSDV-----------SDEDIARALKEANAADFIKTFpeGLNTLVGDRGVQMSGGQKQRIAIARALVRNP 540
Cdd:NF000106 90 ----HRPVR*GRRESfsgrenlymigR*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 541 KILLLDEATSALDAESESIVQSALENASRGRTTIV-----------IAHRLSTVrnaDKIIVMKAGQVMEVGT 602
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVI---DRGRVIADGKVDELKT 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
416-578 |
1.55e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 416 LVGSSGCGKSTIIQLLQRFYNPDAGQILIDdiPIEdfNIKYLRQ----------LVGVVSQEPNLFNTSIEQNIRYGRSD 485
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD--PNE--RLGKLRQdqfafeeftvLDTVIMGHTELWEVKQERDRIYALPE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 486 VSDEDIARALK-------------EANAADFI--KTFPE----GLntlvgdrgvqMSG---GQKQRIAIARALVRNPKIL 543
Cdd:PRK15064 108 MSEEDGMKVADlevkfaemdgytaEARAGELLlgVGIPEeqhyGL----------MSEvapGWKLRVLLAQALFSNPDIL 177
|
170 180 190
....*....|....*....|....*....|....*
gi 17558664 544 LLDEATSALDAESESIVQSALENasRGRTTIVIAH 578
Cdd:PRK15064 178 LLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1047-1225 |
1.81e-05 |
|
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: 49.16 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNdlrqmnpkhlrKHIALVSQEpilfdtsiREni 1126
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-----------VKLAYVDQS--------RD-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1127 vyGLQPGEYTHEQIETACSKANIHKFidELPD-GYETRVGEKGT-------QLSGGQKQRIAIARALIRNPKILLLDEAT 1198
Cdd:TIGR03719 396 --ALDPNKTVWEEISGGLDIIKLGKR--EIPSrAYVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170 180
....*....|....*....|....*..
gi 17558664 1199 SALDTESEKQVQVALDAAAKdrtCIVV 1225
Cdd:TIGR03719 472 NDLDVETLRALEEALLNFAG---CAVV 495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1056-1231 |
1.90e-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: 49.01 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1056 KPGQTLALVGPSGCGKSTVISLLErlydpleGavtvdnndlrQMNPkHLRKHIALVSQEPIL--FDTSIRENIVYGLQPG 1133
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------G----------ELKP-NLGDYDEEPSWDEVLkrFRGTELQDYFKKLANG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1134 EytheqIETAcskaniHK--FIDELPDGYE-------TRVGEKG-------------------TQLSGGQKQRIAIARAL 1185
Cdd:COG1245 159 E-----IKVA------HKpqYVDLIPKVFKgtvrellEKVDERGkldelaeklglenildrdiSELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17558664 1186 IRNPKILLLDEATSALD-TESEKQVQVALDAAAKDRTCIVVAHRLST 1231
Cdd:COG1245 228 LRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
521-597 |
1.97e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 521 QMSGGQKQRIAIARALVRNPKILLLDEATSALD--AESEsIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQV 597
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYE-IYKLINQLVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
706-865 |
2.20e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 47.92 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMPAFSLFFSQIINVFSNPDRDQmkkdGHFWALMfLVLAAVQGTSMLFQC---SLFGVAAERLTMRI 782
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL----GLLLGLA-LLLLGAYLLRALLNFlriYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 783 RSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLGSIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFM 862
Cdd:cd18778 76 RSDLYDKLQRLSLRYFD--DRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFL 153
|
...
gi 17558664 863 AVG 865
Cdd:cd18778 154 ALG 156
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
750-903 |
2.21e-05 |
|
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: 47.85 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 750 ALMFLVLAAVQGTSMLFQCSL-FGVAAERLTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDAPNIKSAIDYRLG 828
Cdd:cd18589 38 AITVMSLLTIASAVSEFVCDLiYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLS 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 829 SIFNAIASVGGGLGIAFYYGWQMAFLVMAIFPFMAVGQALMMKYHGGSATSDAKEMENAGKTAMEAIENIRTVQA 903
Cdd:cd18589 116 LLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRS 190
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1030-1261 |
2.92e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1030 VKLNKVFFRYPERPavpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVT-VDNNDLRQMNpkhlRKHI 1108
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwSENANIGYYA----QDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1109 ALVSQEPILFD--TSIRenivyglQPGEytHEQIETAC------SKANIHKFIdelpdgyetRVgekgtqLSGGQKQRIA 1180
Cdd:PRK15064 393 YDFENDLTLFDwmSQWR-------QEGD--DEQAVRGTlgrllfSQDDIKKSV---------KV------LSGGEKGRML 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1181 IARALIRNPKILLLDEATSALDTESEKQVQVALDAAakDRTCIVVAH------RLSTIVnagcIMVVKNGQVVEQGTHNE 1254
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EGTLIFVSHdrefvsSLATRI----IEITPDGVVDFSGTYEE 522
|
....*..
gi 17558664 1255 LIAKRGA 1261
Cdd:PRK15064 523 YLRSQGI 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
409-611 |
3.01e-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: 48.86 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 409 QPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDDIPIEDfNIKYLRQLVGVVSQEPNLFN--TSIEQNIRYGR-SD 485
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDllTGREHLYLYARlRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 486 VSDEDIARAlkeANAAdfIKTFpeGLnTLVGDR-GVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSAL 564
Cdd:TIGR01257 2042 VPAEEIEKV---ANWS--IQSL--GL-SLYADRlAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17558664 565 ENASR-GRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQKG 611
Cdd:TIGR01257 2114 VSIIReGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1171-1245 |
3.34e-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: 46.03 E-value: 3.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 1171 LSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALD--AAAKDRTCIVVAHRLSTIVNAGCIMVVKNGQ 1245
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
520-591 |
3.54e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 3.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558664 520 VQMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASR--GRTTIVIAHRLSTVRN-ADKIIV 591
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHV 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1052-1227 |
3.75e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1052 NVHVK--PGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNND----LRQ---------------MNPKHLRKhial 1110
Cdd:PRK15064 19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErlgkLRQdqfafeeftvldtviMGHTELWE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1111 VSQEpilfdtsiRENIvYGLqpGEYTHE------QIETacskanihKFIdELpDGY--ETRVGE--------------KG 1168
Cdd:PRK15064 95 VKQE--------RDRI-YAL--PEMSEEdgmkvaDLEV--------KFA-EM-DGYtaEARAGElllgvgipeeqhygLM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 1169 TQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDaaAKDRTCIVVAH 1227
Cdd:PRK15064 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN--ERNSTMIIISH 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
400-582 |
4.52e-05 |
|
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: 47.62 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 400 ILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQILIDdipiEDFNIKYLRQlvgvvSQEPNLFNTSIEQNI 479
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVKLAYVDQ-----SRDALDPNKTVWEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 480 rygrSDVSDEdIARALKEANAADFIKTFpeglNTLVGD---RGVQMSGGQKQRIAIARALVRNPKILLLDEATSALDAES 556
Cdd:TIGR03719 408 ----SGGLDI-IKLGKREIPSRAYVGRF----NFKGSDqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 557 ESIVQSALENAsrGRTTIVIAH------RLST 582
Cdd:TIGR03719 479 LRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1037-1205 |
5.18e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1037 FRYPERPAvpILQGLNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTvdnndlrqmnpKHLRKHIALVSQEPI 1116
Cdd:PLN03073 516 FGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHHV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1117 L-FDTSIREnIVYGLQ--PGeyTHEQietacsKANIHKfidelpdGYETRVGEKGTQ----LSGGQKQRIAIARALIRNP 1189
Cdd:PLN03073 583 DgLDLSSNP-LLYMMRcfPG--VPEQ------KLRAHL-------GSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKP 646
|
170
....*....|....*.
gi 17558664 1190 KILLLDEATSALDTES 1205
Cdd:PLN03073 647 HILLLDEPSNHLDLDA 662
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
401-553 |
5.33e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.92 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVaLVGSSGCGKSTIIQLLQRFYNPDAG-QILIDDIPIEDfNIKYLRQLVGVVsqepnlFNTSIEQNI 479
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSrKFDEEDFYLGD-DPDLPEIEIELT------FGSLLSRLL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 480 RYGRSDVSDEDIARALKEANAAdfIKTFPEGLNTLVGDRGVQMSGGQKQRIAIA----RALVRNPKILLLDEATSALD 553
Cdd:COG3593 86 RLLLKEEDKEELEEALEELNEE--LKEALKALNELLSEYLKELLDGLDLELELSldelEDLLKSLSLRIEDGKELPLD 161
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1037-1257 |
6.45e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1037 FRYPERPaVPILQGLNVHVKPGQTLALVGPSGCGKSTVISLLerlydpleGAVTVDN------------NDLRQMNPKHL 1104
Cdd:PRK15093 13 FKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAI--------CGVTKDNwrvtadrmrfddIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1105 RK----HIALVSQEP-ILFDTSirENIvyGLQ-----PGeYTHEQIETACSKANIHKFIDELpdgyeTRVGEKG------ 1168
Cdd:PRK15093 84 RKlvghNVSMIFQEPqSCLDPS--ERV--GRQlmqniPG-WTYKGRWWQRFGWRKRRAIELL-----HRVGIKDhkdamr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1169 ---TQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDR--TCIVVAHRLSTIVN-AGCIMVVK 1242
Cdd:PRK15093 154 sfpYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLY 233
|
250
....*....|....*
gi 17558664 1243 NGQVVEQGTHNELIA 1257
Cdd:PRK15093 234 CGQTVETAPSKELVT 248
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1170-1282 |
7.40e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1170 QLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKdrTCIVVAHR---LSTIVNAgcIMVVKNgqv 1246
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSHArefLNTVVTD--ILHLHG--- 416
|
90 100 110
....*....|....*....|....*....|....*...
gi 17558664 1247 veqgthNELIAKRGAY--FALTQKQSSNQSGGAFDTSE 1282
Cdd:PLN03073 417 ------QKLVTYKGDYdtFERTREEQLKNQQKAFESNE 448
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
394-619 |
1.03e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 394 TRADVKILKGVSLDAQPGQTVALVGSSGCGKStiiQLLQRFYNPD---AGQILIDDIPIEDFN-IKYLRQLVGVVSQ--- 466
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDkraGGEIRLNGKDISPRSpLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 467 EPNLF-NTSIEQNIRYGRSdVSDEDIARALKEANAADFIKTFPEGLNTL------VGDRGVQMSGGQKQRIAIARALVRN 539
Cdd:PRK09700 349 DNGFFpNFSIAQNMAISRS-LKDGGYKGAMGLFHEVDEQRTAENQRELLalkchsVNQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 540 PKILLLDEATSALDAESESIVQSALEN-ASRGRTTIVIAHRLSTVRNA-DKIIVMKAGQVMEVGTH-ETLIEQKGLYHEL 616
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNrDDMSEEEIMAWAL 507
|
...
gi 17558664 617 VHA 619
Cdd:PRK09700 508 PQE 510
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
134-343 |
1.07e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 45.66 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 134 LSNR----FRRQFFHSVMRQEIAWYDKNTSGTLSNKlFDNLERVRE---GTGDKVGLAFqmmAQFIGGFAVAFTYDWLLT 206
Cdd:cd18782 69 TANRidleLGGTIIDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGfltGTALTTLLDV---LFSVIYIAVLFSYSPLLT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 207 LIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFL- 285
Cdd:cd18782 145 LVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLg 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558664 286 -IGAGLASFfvIIYASYCLAFWVGTNFVYSGRLESGTVLTvfFSVMMGSMA-----LGQAGQQF 343
Cdd:cd18782 225 tTSGSLSQF--LNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILSGYVTgpilrLSTLWQQF 284
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
706-864 |
1.07e-04 |
|
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: 45.60 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQGAVMpAFSLFFSQIINVFSNPDRDQMKKDGHFWALMFLVLAAVQGTSMLFQCSLFGVAAERLTMRIRSK 785
Cdd:cd18605 2 ILILLSLILMQASRN-LIDFWLSYWVSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 786 VYRNVLRQDATYFDmpKHSPGRITTRLATDApnikSAIDYRLGSIFN-AIASVGGGLGIAFYYGWQMAFLVMAIFPFMAV 864
Cdd:cd18605 81 LLSSILFAKMSFFD--KTPVGRILNRFSSDV----YTIDDSLPFILNiLLAQLFGLLGYLVVICYQLPWLLLLLLPLAFI 154
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1047-1251 |
1.38e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1047 ILQGLNVHVKPGQTLALVGPSGCGKSTVISLL--ERLYDPLEGAVTVDNNDLRQmnpkhlrKHIALVS----QEPILF-D 1119
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQ-------ETFARISgyceQNDIHSpQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1120 TSIRENIVYGlqpgeyTHEQIETACSKANIHKFID------ELPDGYETRVGEKG-TQLSGGQKQRIAIARALIRNPKIL 1192
Cdd:PLN03140 968 VTVRESLIYS------AFLRLPKEVSKEEKMMFVDevmelvELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558664 1193 LLDEATSALDTESEKQVQVAL-DAAAKDRTCIVVAHRLST-IVNA--GCIMVVKNGQVVEQGT 1251
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSIdIFEAfdELLLMKRGGQVIYSGP 1104
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1165-1261 |
1.43e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1165 GEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEKQVQVALDAAAKDRTCIVVAHRLSTIVN--AGCIMVVK 1242
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218
|
90
....*....|....*....
gi 17558664 1243 NGQVVEQGTHNELIAKRGA 1261
Cdd:NF000106 219 RGRVIADGKVDELKTKVGG 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1055-1254 |
1.49e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1055 VKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNPKH-LRKHIALV----SQEPILFDTSIRENIV-- 1127
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLCpedrKAEGIIPVHSVADNINis 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1128 ---YGLQPGEYTHEQIEtacsKANIHKFIDEL----PDGyETRVGekgtQLSGGQKQRIAIARALIRNPKILLLDEATSA 1200
Cdd:PRK11288 356 arrHHLRAGCLINNRWE----AENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 1201 LDTESEKQV-QVALDAAAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNE 1254
Cdd:PRK11288 427 IDVGAKHEIyNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
521-590 |
1.91e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 1.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 521 QMSGGQKQRIAIAraLV-----RNPK-ILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLSTVRNADKII 590
Cdd:pfam02463 1077 LLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
401-611 |
2.07e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPDAGQIliddipiedfNIKYLRQLVGVVS----QEPNLFNTSIE 476
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----------DIKGSAALIAISSglngQLTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 477 QNIRYGRSDVSDEDIARALKEANAADFI----KTFpeglntlvgdrgvqmSGGQKQRIAIARALVRNPKILLLDEATSAL 552
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIIEFADIGKFIyqpvKTY---------------SSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 553 DAE-SESIVQSALENASRGRTTIVIAHRLSTVRN-ADKIIVMKAGQVMEVGTHETLIEQKG 611
Cdd:PRK13545 175 DQTfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYD 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
521-578 |
2.88e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 521 QMSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALenASRGRTTIVIAH 578
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
401-431 |
3.88e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.15 E-value: 3.88e-04
10 20 30
....*....|....*....|....*....|....*..
gi 17558664 401 LKGVSLDA-----QPGQTVALVGSSGCGKSTII-QLL 431
Cdd:PRK01889 180 LDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1052-1257 |
5.39e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1052 NVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTvdnNDLRqmnpkhlrkHIALVS---QEPILFDTSIRENiVY 1128
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ---SQFS---------HITRLSfeqLQKLVSDEWQRNN-TD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1129 GLQPGE-----YTHEQIETACSKANIHKFIDELPdGYETRVGEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDT 1203
Cdd:PRK10938 90 MLSPGEddtgrTTAEIIQDEVKDPARCEQLAQQF-GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 1204 ESEKQVQVALDA-AAKDRTCIVVAHRLSTIVN-AGCIMVVKNGQVVEQGTHNELIA 1257
Cdd:PRK10938 169 ASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
500-613 |
7.40e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 500 AADFIKTFP---EGLNTLV---------GDRGVQMSGGQKQRIAIARALVRNP--KIL-LLDEATSALDAESesiVQSAL 564
Cdd:PRK00349 797 ALEFFEAIPkiaRKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFED---IRKLL 873
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 565 ENASR----GRTTIVIAHRLSTVRNADKIIVM------KAGQVMEVGTHETLIEQKGLY 613
Cdd:PRK00349 874 EVLHRlvdkGNTVVVIEHNLDVIKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
509-590 |
8.87e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 509 EGLNTLVGDRGVQMSGGQKQ------RIAIARALVRNPKILLLDEATSALDAES-----ESIVQSALEnaSRGRTTIVIA 577
Cdd:cd03240 103 GESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENieeslAEIIEERKS--QKNFQLIVIT 180
|
90
....*....|...
gi 17558664 578 HRLSTVRNADKII 590
Cdd:cd03240 181 HDEELVDAADHIY 193
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
111-321 |
9.17e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 42.96 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 111 YLGCGIFAA-------GFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDnLERVREG-TGDKVG 182
Cdd:cd18566 43 VLVIGVVIAillesllRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIREFlTGQALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 183 LAFQMMAQFIGgFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQE 262
Cdd:cd18566 122 ALLDLPFVLIF-LGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEP 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558664 263 YECKRYEDALEHGKKTGIKKSFL--IGAGLASFFVIIYASYCLafWVGTNFVYSGRLESGT 321
Cdd:cd18566 201 QMLRRYERLQANAAYAGFKVAKInaVAQTLGQLFSQVSMVAVV--AFGALLVINGDLTVGA 259
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
110-323 |
1.21e-03 |
|
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: 42.45 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 110 VYLGCGI--FAAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSG-----------TLSNkLFDNlervreg 176
Cdd:cd18545 45 LFLALNLvnWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGkilsrvindvnSLSD-LLSN------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 177 tgdkvGLaFQMMAQF---IGGFAVAFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIR 253
Cdd:cd18545 117 -----GL-INLIPDLltlVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558664 254 TVIAFNGQEYECKRYED-ALEHgkktgiKKSFLIGAGLASFFV----IIYA-SYCLAFWVGTNFVYSGRLESGTVL 323
Cdd:cd18545 191 VIQSFAREDENEEIFDElNREN------RKANMRAVRLNALFWplveLISAlGTALVYWYGGKLVLGGAITVGVLV 260
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1043-1078 |
1.49e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 42.23 E-value: 1.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 17558664 1043 PAVPIL-------QGLNV---HVKPGQTLALVGPSGCGKSTVISLL 1078
Cdd:PRK01889 170 PGVPVLavsaldgEGLDVlaaWLSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1137-1229 |
1.58e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1137 HEQIETACSKAnihkfIDELPdgyetrVGEKGTQLSGGQKQRIAIARALI---RNPKILLLDEATSALDTESEKQ-VQVA 1212
Cdd:PRK00635 787 HEKIHALCSLG-----LDYLP------LGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKAlIYVL 855
|
90
....*....|....*..
gi 17558664 1213 LDAAAKDRTCIVVAHRL 1229
Cdd:PRK00635 856 QSLTHQGHTVVIIEHNM 872
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
139-330 |
1.60e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 42.02 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 139 RRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAVAFTYDWLLTLIMMSLSPFMMI 218
Cdd:cd18554 82 RKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYIL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 219 CGLFLAKLLATAATKEAKQYAVAGGIAEEVLTSIRTVIAFNGQEYECKRYEDALEHGKKTGIKKSFLIGAGLASFFVIIY 298
Cdd:cd18554 162 AVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITD 241
|
170 180 190
....*....|....*....|....*....|..
gi 17558664 299 ASYCLAFWVGTNFVYSGRLESGTvLTVFFSVM 330
Cdd:cd18554 242 LAPLLVIGFAAYLVIEGNLTVGT-LVAFVGYM 272
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1051-1207 |
1.65e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1051 LNVHVKPGQTLALVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMnPKHLRKHIAlvSQEPILFDTSIRENIVYGL 1130
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-AKPYCTYIG--HNLGLKLEMTVFENLKFWS 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 1131 QpgeyTHEQIETAcsKANIHKF-IDELPDgyetrvgEKGTQLSGGQKQRIAIARALIRNPKILLLDEATSALDTESEK 1207
Cdd:PRK13541 96 E----IYNSAETL--YAAIHYFkLHDLLD-------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
401-480 |
2.11e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 42.20 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 401 LKGVSLDAQPGQTVaLVGSSGCGKSTIIQLLQRFYNPDagqiliDDIPIEDFNIKYLRQLVGVVSQEPNLF-NTSIEQNI 479
Cdd:pfam13175 14 LKDTEIDLDEDLTV-LIGKNNSGKSSILEALDIFLNNK------EKFFEDDFLVLYLKDVIKIDKEDLNIFeNISFSIDI 86
|
.
gi 17558664 480 R 480
Cdd:pfam13175 87 E 87
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1061-1235 |
2.32e-03 |
|
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: 40.04 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1061 LALVGPSGCGKSTVIsllerlydplegavtvdnndlrqmnpkhlrKHIALvsqepILFDTSIRENIVYGLQPGEYTheqi 1140
Cdd:cd03227 24 TIITGPNGSGKSTIL------------------------------DAIGL-----ALGGAQSATRRRSGVKAGCIV---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 1141 etACSKANIHKFIDelpdgyetrvgekgtQLSGGQKQRIAIARALI---RNPKIL-LLDEATSALDTESEKQV-QVALDA 1215
Cdd:cd03227 65 --AAVSAELIFTRL---------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALaEAILEH 127
|
170 180
....*....|....*....|
gi 17558664 1216 AAKDRTCIVVAHRLSTIVNA 1235
Cdd:cd03227 128 LVKGAQVIVITHLPELAELA 147
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
395-608 |
2.40e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 395 RADVKILKGVSLDAQPGQTVALVGSSGCGKSTIIQLLQRFYNPD---AGQILIDDIPIEDF----NIKYLRQ---LVGVV 464
Cdd:PLN03140 175 KTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFvprkTSAYISQndvHVGVM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 465 SQEPNLFNTSIEQNIRYgRSDVSDEdIARALK------EANAADFIK-TFPEGL-------------------NTLVGD- 517
Cdd:PLN03140 255 TVKETLDFSARCQGVGT-RYDLLSE-LARREKdagifpEAEVDLFMKaTAMEGVksslitdytlkilgldickDTIVGDe 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 518 --RGVqmSGGQKQRIAIARALVRNPKILLLDEATSALDAESESIVQSALENASRGRTTIVIAHRLS----TVRNADKIIV 591
Cdd:PLN03140 333 miRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDIIL 410
|
250
....*....|....*..
gi 17558664 592 MKAGQVMEVGTHETLIE 608
Cdd:PLN03140 411 LSEGQIVYQGPRDHILE 427
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
703-920 |
3.24e-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: 40.95 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 703 WIYIFFAIIAAliqgavmpAFSLFFSQIINVFSNPDRDQMKKDGHFWALMFLVLAAVQGTSMLFQCS-LFGVAAERLTMR 781
Cdd:cd18580 2 LLLLLLLLLLA--------FLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWlLFVLAGLRASRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 782 IRSKVYRNVLRQDATYFDmpKHSPGRITTRLATDApnikSAIDYRL----GSIFNAIASVGGGLGIAFYYGWQMAflvmA 857
Cdd:cd18580 74 LHDKLLRSVLRAPMSFFD--TTPSGRILNRFSKDI----GLIDEELplalLDFLQSLFSVLGSLIVIAIVSPYFL----I 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558664 858 IFPFMAVGQALMMKYHggSATS-DAKEMENAGKTAM-----EAIENIRTVQALTLQTKLYNIFCSHLDA 920
Cdd:cd18580 144 VLPPLLVVYYLLQRYY--LRTSrQLRRLESESRSPLyshfsETLSGLSTIRAFGWQERFIEENLRLLDA 210
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
706-901 |
4.21e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 40.94 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 706 IFFAIIAALIQgaVMPAFSLFfsQIINVFSNPDRDQMKKdGHFWALMFLVLAAVQgtSMLFQCSLFgvAAERLTMRIRS- 784
Cdd:cd18596 3 ALLAVLSSVLS--FAPPFFLN--RLLRYLEDPGEDATVR-PWVWVLLLFLGPLLS--SLLDQQYLW--IGRRLSVRLRAi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 785 ---KVYRNVLR---------QDATYFDMP--------KHSPGRITTRLATDAPNIKSAIDYrLGSIFNAIASVggGLGIA 844
Cdd:cd18596 74 ltqLIFEKALRrrdksgsskSSESKKKDKeededeksSASVGKINNLMSVDANRISEFAAF-LHLLVSAPLQI--VIAIV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558664 845 FYY---GWQM--AFLVMAI-FP--------FMAVGQALMmkyhggsATSDAKeMenagkTAM-EAIENIRTV 901
Cdd:cd18596 151 FLYrllGWSAlvGLAVMVLlLPlngylakrYSRAQKELM-------KARDAR-V-----QLVtEVLQGIRMI 209
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
1063-1101 |
4.50e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 39.65 E-value: 4.50e-03
10 20 30
....*....|....*....|....*....|....*....
gi 17558664 1063 LVGPSGCGKSTVISLLERLYDPLEGAVTVDNNDLRQMNP 1101
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
503-595 |
5.04e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 503 FIKTFPEGLNTLV---------GDRGVQMSGGQKQRIAIARALVRNPK---ILLLDEATSALDAESESIVQSALEN-ASR 569
Cdd:PRK00635 1672 FLKKIQKPLQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSL 1751
|
90 100
....*....|....*....|....*.
gi 17558664 570 GRTTIVIAHRLSTVRNADKIIVMKAG 595
Cdd:PRK00635 1752 GHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
703-911 |
5.25e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 40.62 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 703 WIYIFFAIIAAL-IQ--GAVMPafslFFSQII--NVFSNPDRDQMkkdgHFWALMFLVLAAVQGTSMLFQCSLFGVAAER 777
Cdd:cd18568 1 RKLLAEILLASLlLQllGLALP----LFTQIIldRVLVHKNISLL----NLILIGLLIVGIFQILLSAVRQYLLDYFANR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 778 LTMRIRSKVYRNVLRQDATYFDmpKHSPGRITTR----------LATDApnIKSAIDyrLGSIFNAiasvgggLGIAFYY 847
Cdd:cd18568 73 IDLSLLSDFYKHLLSLPLSFFA--SRKVGDIITRfqenqkirrfLTRSA--LTTILD--LLMVFIY-------LGLMFYY 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558664 848 GWQMAFLVMAIFPFMA----VGQALMMKYHGGSATSDAKEMenagKTAMEAIENIRTVQALTLQTKLY 911
Cdd:cd18568 140 NLQLTLIVLAFIPLYVlltlLSSPKLKRNSREIFQANAEQQ----SFLVEALTGIATIKALAAERPIR 203
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
118-345 |
5.63e-03 |
|
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: 40.16 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 118 AAGFLQASCFMVICEKLSNRFRRQFFHSVMRQEIAWYDKNTSGTLSNKLFDNLERVREGTGDKVGLAFQMMAQFIGGFAV 197
Cdd:cd18550 54 LLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 198 AFTYDWLLTLIMMSLSPFMMICGLFLAKLLATAATKEAKQYAVAGGIAEEVLT--SIRTVIAFNGQEYECKRYEDALEHG 275
Cdd:cd18550 134 MLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSREL 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558664 276 KKTGIKKSfLIGaglASFFVIIYASYCLA----FWVGTNFVYSGRLESGTV--LTVFFSVMMGS-MALGQAGQQFAT 345
Cdd:cd18550 214 RDLGVRQA-LAG---RWFFAALGLFTAIGpalvYWVGGLLVIGGGLTIGTLvaFTALLGRLYGPlTQLLNIQVDLMT 286
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
191-273 |
8.50e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 39.82 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558664 191 FIGGFAVAFTYDWLLTLIMMslspFMMICGLFLAKLLATAATKEAKQYAVAG----GIAEEVLTSIRTVIAFNGQEYECK 266
Cdd:cd18583 125 VIAIVYLYYLFDPYMGLIVA----VVMVLYVWSTIKLTSWRTKLRRDMIDADreerSILTESLLNWETVKYFNREPYEKE 200
|
....*..
gi 17558664 267 RYEDALE 273
Cdd:cd18583 201 RYREAVK 207
|
|
| |
